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acetyl-CoA + 2,5-dimethoxyphenylethylamine
CoA + ?
Substrates: 24% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2,5-dimethoxyphenylethylamine
CoA + N-acetyl-2,5-dimethoxyphenylethylamine
-
Substrates: 68% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(2,3-dichlorophenyl)-ethylamine
CoA + N-acetyl-2-(2,3-dichlorophenyl)-ethylamine
acetyl-CoA + 2-(2-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(2-chlorophenyl)-ethylamine
acetyl-CoA + 2-(3,4-dihydroxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dihydroxyphenyl)-ethylamine
acetyl-CoA + 2-(3,4-dimethoxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dimethoxyphenyl)-ethylamine
acetyl-CoA + 2-(3-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(3-chlorophenyl)-ethylamine
acetyl-CoA + 2-(3-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(3-fluorophenyl)-ethylamine
acetyl-CoA + 2-(4-bromophenyl)-ethylamine
CoA + N-acetyl-2-(4-bromophenyl)-ethylamine
acetyl-CoA + 2-(4-chlorophenyl)ethylamine
CoA + N-acetyl-2-(4-chlorophenyl)ethylamine
acetyl-CoA + 2-(4-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(4-fluorophenyl)-ethylamine
acetyl-CoA + 2-(p-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(p-fluorophenyl)-ethylamine
acetyl-CoA + 2-(p-nitrophenyl)-ethylamine
CoA + N-acetyl-2-(p-nitrophenyl)-ethylamine
acetyl-CoA + 2-(p-tolyl)-ethylamine
CoA + N-acetyl-2-(p-tolyl)-ethylamine
acetyl-CoA + 2-fluorophenylethylamine
CoA + ?
Substrates: 69% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-fluorophenylethylamine
CoA + N-acetyl-2-fluorophenylethylamine
-
Substrates: 52% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-methoxyphenylethylamine
CoA + N-acetyl-2-methoxyphenylethylamine
acetyl-CoA + 2-phenylethylamine
CoA + N-acetyl-2-phenylethylamine
acetyl-CoA + 3-(trifluoromethyl)phenethylamine
CoA + N-acetyl-3-(trifluoromethyl)phenethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + 3-hydroxy-4-methoxyphenethylamine
CoA + ?
Substrates: 1% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 3-hydroxy-4-methoxyphenethylamine
CoA + N-acetyl-3-hydroxy-4-methoxyphenethylamine
-
Substrates: 7.2% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 3-hydroxyphenethylamine
CoA + ?
Substrates: 24% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 3-hydroxyphenethylamine
CoA + N-acetyl-3-hydroxyphenethylamine
-
Substrates: 36% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 3-indolebutylamine
CoA + N-acetyl-(3-indol-3-yl-butyl)-amine
-
Substrates: 60-fold less efficiently than serotonin
Products: -
?
acetyl-CoA + 3-indolepropylamine
CoA + N-acetyl-(3-indol-3-yl-propyl)-amine
-
Substrates: 20-fold less efficiently than serotonin
Products: -
?
acetyl-CoA + 3-methoxy-2-phenylethylamine
CoA + ?
Substrates: 23% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 3-methoxy-2-phenylethylamine
CoA + N-acetyl-3-methoxy-2-phenylethylamine
-
Substrates: 55% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 3-methoxyphenethylamine
CoA + N-acetyl-3-methoxyphenethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + 3-methoxytyramine
CoA + ?
Substrates: 17% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 3-methoxytyramine
CoA + N-acetyl-3-methoxytyramine
-
Substrates: 73% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 4-(2-aminoethyl)-benzenesulfonamide
CoA + ?
-
Substrates: 1% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 4-(2-aminoethyl)-benzenesulfonyl fluoride
CoA + ?
acetyl-CoA + 4-methoxyphenylethylamine
CoA + N-acetyl-4-methoxyphenylethylamine
acetyl-CoA + 5-benzyloxytryptamine
CoA + N-acetyl-5-benzyloxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 5-hydroxydopamine
CoA + N-acetyl-5-hydroxydopamine
-
Substrates: 4.4% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 5-hydroxytryptamine
CoA + N-acetyl-5-hydroxytryptamine
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
acetyl-CoA + 6-fluorotryptamine
CoA + N-acetyl-6-fluorotryptamine
acetyl-CoA + 6-hydroxydopamine
CoA + ?
Substrates: 51% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 6-hydroxydopamine
CoA + N-acetyl-6-hydroxydopamine
-
Substrates: 1.5% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
acetyl-CoA + alpha-methyltryptamine
CoA + N-acetyl-alpha-methyltryptamine
-
Substrates: racemic, 9:1 stereoselectivity for R-enantiomer, less efficiently than serotonin
Products: -
?
acetyl-CoA + beta-methylphenethylamine
CoA + N-acetyl-beta-methylphenethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
acetyl-CoA + dopamine
CoA + N-acetyldopamine
acetyl-CoA + histamine
CoA + N-acetylhistamine
acetyl-CoA + methoxytryptamine
CoA + N-acetylmethoxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + Nomega-methyltryptamine
CoA + ?
-
Substrates: less efficiently than serotonin
Products: -
?
acetyl-CoA + norepinephrine
CoA + N-acetylnorepinephrine
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
acetyl-CoA + p-phenetidine
CoA + N-(4-ethoxyphenyl)-aecetamide
-
Substrates: -
Products: -
?
acetyl-CoA + phenethylamine
CoA + N-acetyl-phenethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetyl-phenylethylamine
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
acetyl-CoA + serotonin
CoA + N-acetylserotonin
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
acetyl-CoA + tryptamine
N-acetyltryptamine + CoA
-
Substrates: -
Products: -
?
acetyl-CoA + tryptophol
CoA + N-acetyltryptophol
-
Substrates: structural analogue to tryptamine
Products: -
?
acetyl-CoA + tyramine
CoA + ?
Substrates: 8% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
arachidonoyl-CoA + octopamine
CoA + N-arachidonoyloctopamine
Substrates: -
Products: -
?
butanoyl-CoA + dopamine
CoA + N-butanoyldopamine
Substrates: -
Products: -
?
butanoyl-CoA + histamine
CoA + N-butanoylhistamine
-
Substrates: -
Products: -
?
hexanoyl-CoA + histamine
CoA + N-hexanoylhistamine
-
Substrates: -
Products: -
?
oleoyl-CoA + octopamine
CoA + N-oleoyloctopamine
Substrates: -
Products: -
?
palmitoyl-CoA + octopamine
CoA + N-palmitoyloctopamine
Substrates: -
Products: -
?
propionyl-CoA + histamine
CoA + N-propionylhistamine
propionyl-CoA + tyramine
CoA + N-propionyltyramine
stearoyl-CoA + octopamine
CoA + N-stearoyloctopamine
Substrates: -
Products: -
?
additional information
?
-
acetyl-CoA + 2-(2,3-dichlorophenyl)-ethylamine
CoA + N-acetyl-2-(2,3-dichlorophenyl)-ethylamine
Substrates: 78% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(2,3-dichlorophenyl)-ethylamine
CoA + N-acetyl-2-(2,3-dichlorophenyl)-ethylamine
-
Substrates: 84% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(2-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(2-chlorophenyl)-ethylamine
Substrates: 130% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(2-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(2-chlorophenyl)-ethylamine
-
Substrates: 102% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(3,4-dihydroxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dihydroxyphenyl)-ethylamine
Substrates: 7% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(3,4-dihydroxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dihydroxyphenyl)-ethylamine
-
Substrates: 64% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(3,4-dimethoxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dimethoxyphenyl)-ethylamine
Substrates: 4.4% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(3,4-dimethoxyphenyl)-ethylamine
CoA + N-acetyl-2-(3,4-dimethoxyphenyl)-ethylamine
-
Substrates: 15% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(3-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(3-chlorophenyl)-ethylamine
Substrates: 67% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(3-chlorophenyl)-ethylamine
CoA + N-acetyl-2-(3-chlorophenyl)-ethylamine
-
Substrates: 110% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(3-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(3-fluorophenyl)-ethylamine
Substrates: 65% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(3-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(3-fluorophenyl)-ethylamine
-
Substrates: 93% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(4-bromophenyl)-ethylamine
CoA + N-acetyl-2-(4-bromophenyl)-ethylamine
Substrates: 48% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(4-bromophenyl)-ethylamine
CoA + N-acetyl-2-(4-bromophenyl)-ethylamine
-
Substrates: 87% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(4-chlorophenyl)ethylamine
CoA + N-acetyl-2-(4-chlorophenyl)ethylamine
Substrates: 68% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(4-chlorophenyl)ethylamine
CoA + N-acetyl-2-(4-chlorophenyl)ethylamine
-
Substrates: 91% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(4-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(4-fluorophenyl)-ethylamine
Substrates: 116% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(4-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(4-fluorophenyl)-ethylamine
-
Substrates: 60% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(p-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(p-fluorophenyl)-ethylamine
Substrates: 56% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(p-fluorophenyl)-ethylamine
CoA + N-acetyl-2-(p-fluorophenyl)-ethylamine
-
Substrates: as active as with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(p-nitrophenyl)-ethylamine
CoA + N-acetyl-2-(p-nitrophenyl)-ethylamine
Substrates: 9% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(p-nitrophenyl)-ethylamine
CoA + N-acetyl-2-(p-nitrophenyl)-ethylamine
-
Substrates: 53% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(p-tolyl)-ethylamine
CoA + N-acetyl-2-(p-tolyl)-ethylamine
Substrates: 60% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-(p-tolyl)-ethylamine
CoA + N-acetyl-2-(p-tolyl)-ethylamine
-
Substrates: 87% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-methoxyphenylethylamine
CoA + N-acetyl-2-methoxyphenylethylamine
Substrates: 52% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-methoxyphenylethylamine
CoA + N-acetyl-2-methoxyphenylethylamine
-
Substrates: 97% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 2-phenylethylamine
CoA + N-acetyl-2-phenylethylamine
Substrates: -
Products: -
?
acetyl-CoA + 2-phenylethylamine
CoA + N-acetyl-2-phenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + 2-phenylethylamine
CoA + N-acetyl-2-phenylethylamine
Substrates: -
Products: -
?
acetyl-CoA + 4-(2-aminoethyl)-benzenesulfonyl fluoride
CoA + ?
Substrates: 8% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 4-(2-aminoethyl)-benzenesulfonyl fluoride
CoA + ?
-
Substrates: 7.4% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 4-methoxyphenylethylamine
CoA + N-acetyl-4-methoxyphenylethylamine
Substrates: 11% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 4-methoxyphenylethylamine
CoA + N-acetyl-4-methoxyphenylethylamine
-
Substrates: 10% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + 5-hydroxytryptamine
CoA + N-acetyl-5-hydroxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 5-hydroxytryptamine
CoA + N-acetyl-5-hydroxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
Substrates: -
Products: -
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 5-methoxytryptamine
CoA + N-acetyl-5-methoxytryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 6-fluorotryptamine
CoA + N-acetyl-6-fluorotryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + 6-fluorotryptamine
CoA + N-acetyl-6-fluorotryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
Substrates: -
Products: -
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + a 2-arylethylamine
CoA + an N-acetyl-2-arylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
Substrates: -
Products: -
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
Substrates: -
Products: -
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
Substrates: -
Products: -
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
Substrates: -
Products: -
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
Substrates: -
Products: -
?
acetyl-CoA + beta-phenylethylamine
CoA + N-(2-phenylethyl)-acetaminde
-
Substrates: also substrate: phenylethylamine derivatives without a beta-hydroxy group
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
-
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
Substrates: -
Products: -
?
acetyl-CoA + dopamine
CoA + N-acetyldopamine
Substrates: -
Products: -
?
acetyl-CoA + histamine
CoA + N-acetylhistamine
-
Substrates: -
Products: -
?
acetyl-CoA + histamine
CoA + N-acetylhistamine
Substrates: -
Products: -
?
acetyl-CoA + histamine
CoA + N-acetylhistamine
-
Substrates: -
Products: -
?
acetyl-CoA + histamine
CoA + N-acetylhistamine
Substrates: -
Products: -
?
acetyl-CoA + histamine
CoA + N-acetylhistamine
Substrates: -
Products: -
?
acetyl-CoA + norepinephrine
CoA + N-acetylnorepinephrine
-
Substrates: -
Products: -
?
acetyl-CoA + norepinephrine
CoA + N-acetylnorepinephrine
Substrates: -
Products: -
?
acetyl-CoA + norepinephrine
CoA + N-acetylnorepinephrine
-
Substrates: -
Products: -
?
acetyl-CoA + norepinephrine
CoA + N-acetylnorepinephrine
Substrates: -
Products: -
?
acetyl-CoA + norepinephrine
CoA + N-acetylnorepinephrine
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
-
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
-
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
-
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
-
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
-
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
-
Substrates: -
Products: -
?
acetyl-CoA + octopamine
CoA + N-acetyloctopamine
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetyl-phenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetyl-phenylethylamine
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + phenylethylamine
CoA + N-acetylphenylethylamine
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: i.e. 5-hydroxytryptamine
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: rate-limiting in melatonin, i.e. N-acetyl-5-methoxytryptamine synthesis
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: best substrate
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: key enzyme of circadian rhythm of melatonin synthesis
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: i.e. 5-hydroxytryptamine
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: rate-limiting in melatonin synthesis
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: the enzyme catalyzes the first step in melatonin biosynthesis
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: i.e. 5-hydroxytryptamine
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: initial reaction in melatonin synthesis from serotonin
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: penultimate enzyme in melatonin pathway
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: penultimate step in melatonin biosynthesis
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: reaction mechanism involving Pro64 that plays a critical role in structure and catalysis
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: i.e. 5-hydroxytryptamine
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: i.e. 5-hydroxytryptamine
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: initial reaction in melatonin synthesis from serotonin
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: first step in melatonin biosynthesis
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
Substrates: AANAT2 acetylates serotonin about 10times faster than AANAT1
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + serotonin
CoA + N-acetylserotonin
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Esox sp.
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
-
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
Substrates: -
Products: -
?
acetyl-CoA + tryptamine
CoA + N-acetyltryptamine
trout
-
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
Substrates: very poor substrate
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
Substrates: 10% of the activity with 2-phenylethylamine
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
-
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
Substrates: -
Products: -
?
acetyl-CoA + tyramine
CoA + N-acetyltyramine
Substrates: -
Products: -
?
propionyl-CoA + histamine
CoA + N-propionylhistamine
Substrates: -
Products: -
?
propionyl-CoA + histamine
CoA + N-propionylhistamine
Substrates: -
Products: -
?
propionyl-CoA + histamine
CoA + N-propionylhistamine
Substrates: -
Products: -
?
propionyl-CoA + histamine
CoA + N-propionylhistamine
Substrates: -
Products: -
?
propionyl-CoA + tyramine
CoA + N-propionyltyramine
Substrates: -
Products: -
?
propionyl-CoA + tyramine
CoA + N-propionyltyramine
Substrates: -
Products: -
?
propionyl-CoA + tyramine
CoA + N-propionyltyramine
-
Substrates: -
Products: -
?
additional information
?
-
Substrates: aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
Products: -
?
additional information
?
-
-
Substrates: aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, aaNAT1 and aaNAT2 show a broad substrate specificity and their affinity and catalytic efficiency to each of the seven arylalkylamines tested. The affinity between aaNAT1 and aaNAT2 to most of the arylalkylamines is similar except that aaNAT2 has less affinity than aaNAT1 to norepinephrine. Also aaNAT1 is more efficient in catalyzing all the tested substrates than that of aaNAT2
Products: -
?
additional information
?
-
Substrates: no substrate: sulfamethazine
Products: -
?
additional information
?
-
-
Substrates: no substrate: sulfamethazine
Products: -
?
additional information
?
-
-
Substrates: ordered sequential mechanism, with acetyl-CoA binding first followed by histamine to generate an AANATL7-acetyl-CoA-histamine ternary complex prior to catalysis. An ionizable group with a pKa of 7.1 is assigned to Glu-26 as a general base and a second with a pKa of 9.5 is assigned to the protonation of the thiolate of the coenzyme A product
Products: -
?
additional information
?
-
-
Substrates: enzyme activity in cultured cells is suppressed by light, as it is in vivo. The ability to express circadian regulation of the enzyme activity is an intrinsic property of retinal cells that can develop in vitro
Products: -
?
additional information
?
-
-
Substrates: further substrates: selected synthetic amines
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the rate-limiting step in melatonin synthesis
Products: -
?
additional information
?
-
Substrates: no activity with 2-(4-aminophenyl)-ethylamine, 3,4-(dibenzyloxy)phenethylamine, 5-hydroxydopamine, 4-(2-aminoethyl)-benzenesulfonamide or 2-(p-chlorophenoxy)-2-methylpropionic acid
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-(4-aminophenyl)-ethylamine, 3,4-(dibenzyloxy)phenethylamine, 5-hydroxydopamine, 4-(2-aminoethyl)-benzenesulfonamide or 2-(p-chlorophenoxy)-2-methylpropionic acid
Products: -
?
additional information
?
-
-
Substrates: enzyme light and diurnal regulation involves phosphorylation on key AANAT Ser and Thr residues, which results in 14-3-3 protein recruitment and changes in catalytic activity and protein stability
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the limiting step for melatonin synthesis
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the limiting step for melatonin synthesis
Products: -
?
additional information
?
-
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: arylamines, such as aniline or p-phenetidine are very poor substrates
Products: -
?
additional information
?
-
-
Substrates: arylamines, such as aniline or p-phenetidine are very poor substrates
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-(4-aminophenyl)-ethylamine, 3,4-(dibenzyloxy)phenethylamine or 2-(p-chlorophenoxy)-2-methylpropionic acid
Products: -
?
additional information
?
-
-
Substrates: NAT could be a clock-controlled gene functioning as an output regulator of the circadian clock
Products: -
?
additional information
?
-
-
Substrates: no substrates are phenylethanolamine derivatives with a beta-hydroxy group
Products: -
?
additional information
?
-
-
Substrates: arylamines, such as aniline or p-phenetidine are very poor substrates
Products: -
?
additional information
?
-
-
Substrates: arylamines, such as aniline or p-phenetidine are very poor substrates
Products: -
?
additional information
?
-
Substrates: overexpression of inducible cAMP early repressor can suppress the norepinephrine induction of aa-nat
Products: -
?
additional information
?
-
Substrates: AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
Products: -
?
additional information
?
-
Substrates: AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
Products: -
?
additional information
?
-
-
Substrates: AANAT1 may carry out an as yet unknown function that involves acetylation of arylalkylamines other than serotonin
Products: -
?
additional information
?
-
Substrates: AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
Products: -
?
additional information
?
-
Substrates: AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
Products: -
?
additional information
?
-
-
Substrates: AANAT2 is responsible for the production of large amounts of melatonin that is released into the circulation and exerts an endocrine role
Products: -
?
additional information
?
-
Substrates: insignificant activity in presence of phenylethylamine or tyramine
Products: -
?
additional information
?
-
Substrates: insignificant activity in presence of phenylethylamine or tyramine
Products: -
?
additional information
?
-
-
Substrates: insignificant activity in presence of phenylethylamine or tyramine
Products: -
?
additional information
?
-
-
Substrates: AANAT is a key regulatory enzyme in the melatonin biosynthetic pathway
Products: -
?
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Acidosis
Acidosis-sensing glutamine pump SNAT2 determines amino acid levels and mammalian target of rapamycin signalling to protein synthesis in L6 muscle cells.
Acidosis
Inhibition of SNAT2 by metabolic acidosis enhances proteolysis in skeletal muscle.
Acquired Immunodeficiency Syndrome
Cell Surface Proteomic Map of HIV Infection Reveals Antagonism of Amino Acid Metabolism by Vpu and Nef.
aralkylamine n-acetyltransferase deficiency
Inhibition of the glutamine transporter SNAT1 confers neuroprotection in mice by modulating the mTOR-autophagy system.
aralkylamine n-acetyltransferase deficiency
Prolonged swim-test immobility of serotonin N-acetyltransferase (AANAT)-mutant mice.
Arthus Reaction
Serotonin metabolism in the arthus reaction.
Asthma
N-acetyltransferases as markers for asthma and allergic/atopic disorders.
Astrocytoma
Increased expression of a glutamine transporter SNAT3 is a marker of malignant gliomas.
Brain Injuries
Up-regulation of miR-325-3p suppresses pineal aralkylamine N-acetyltransferase (Aanat) after neonatal hypoxia-ischemia brain injury in rats.
Brain Neoplasms
Increased expression of a glutamine transporter SNAT3 is a marker of malignant gliomas.
Breast Neoplasms
Activation of SNAT1/SLC38A1 in human breast cancer: correlation with p-Akt overexpression.
Breast Neoplasms
Altered Umbilical Cord Blood Nutrient Levels, Placental Cell Turnover and Transporter Expression in Human Term Pregnancies Conceived by Intracytoplasmic Sperm Injection (ICSI).
Breast Neoplasms
Hypoxia-induced switch in SNAT2/SLC38A2 regulation generates endocrine resistance in breast cancer.
Breast Neoplasms
Melatonin pathway genes and breast cancer risk among Chinese women.
Breast Neoplasms
Polymorphisms in circadian genes, night work and breast cancer: results from the GENICA study.
Breast Neoplasms
SNAT2 transceptor signalling via mTOR: a role in cell growth and proliferation?
Carcinogenesis
Activation of SNAT1/SLC38A1 in human breast cancer: correlation with p-Akt overexpression.
Carcinogenesis
O-GlcNAcylation of YY1 stimulates tumorigenesis in colorectal cancer cells by targeting SLC22A15 and AANAT.
Carcinoma, Hepatocellular
Characterization of the amino acid response element within the human sodium-coupled neutral amino acid transporter 2 (SNAT2) System A transporter gene.
Carcinoma, Hepatocellular
Despite Increased ATF4 Binding at the C/EBP-ATF Composite Site following Activation of the Unfolded Protein Response, System A Transporter 2 (SNAT2) Transcription Activity Is Repressed in HepG2 Cells.
Choriocarcinoma
Human placental trophoblasts synthesize melatonin and express its receptors.
Chronobiology Disorders
The flavonoid myricetin reduces nocturnal melatonin levels in the blood through the inhibition of serotonin N-acetyltransferase.
Colorectal Neoplasms
AA-NAT, MT1 and MT2 Correlates with Cancer Stem-Like Cell Markers in Colorectal Cancer: Study of the Influence of Stage and p53 Status of Tumors.
Colorectal Neoplasms
Melatonin reduces endothelin-1 expression and secretion in colon cancer cells through the inactivation of FoxO-1 and NF-??
Colorectal Neoplasms
O-GlcNAcylation of YY1 stimulates tumorigenesis in colorectal cancer cells by targeting SLC22A15 and AANAT.
Endometrial Neoplasms
ASCT2 regulates glutamine uptake and cell growth in endometrial carcinoma.
Epilepsy
Modulation of epileptiform activity by glutamine and system A transport in a model of post-traumatic epilepsy.
Glioma
Increased expression of a glutamine transporter SNAT3 is a marker of malignant gliomas.
Infections
Attacking the Supply Lines: HIV-1 Restricts Alanine Uptake to Prevent T Cell Activation.
Infections
Expression of Melatonin Synthesizing Enzymes in Helicobacter pylori Infected Gastric Mucosa.
Infections
Structure of Mycobacterium smegmatis Eis in complex with paromomycin.
Infections
The Amino Acid-mTORC1 Pathway Mediates APEC TW-XM-Induced Inflammation in bEnd.3 Cells.
Insulin Resistance
Chronic treatment with dexamethasone alters clock gene expression and melatonin synthesis in rat pineal gland at night.
Insulin Resistance
Inhibition of SNAT2 by metabolic acidosis enhances proteolysis in skeletal muscle.
Intestinal Volvulus
Characterization of the arylalkylamine N-acetyltransferase in Onchocerca volvulus.
Ischemic Attack, Transient
Arylalkylamine N-acetyltransferase (AANAT) is expressed in astrocytes and melatonin treatment maintains AANAT in the gerbil hippocampus induced by transient cerebral ischemia.
Klatskin Tumor
Overexpression of Prdx1 in hilar cholangiocarcinoma: a predictor for recurrence and prognosis.
Liver Cirrhosis
Pinealectomy or light exposure exacerbates biliary damage and liver fibrosis in cholestatic rats through decreased melatonin synthesis.
Liver Cirrhosis
Prolonged exposure of cholestatic rats to complete dark inhibits biliary hyperplasia and liver fibrosis.
Melanoma
Gender-specific associations between polymorphisms of the circadian gene RORA and cutaneous melanoma susceptibility.
Melanoma
Running for time: circadian rhythms and melanoma.
Melanoma
Serotoninergic and melatoninergic systems are fully expressed in human skin.
Melanoma
Serotoninergic system in hamster skin.
Melanosis
A New Arylalkylamine N-Acetyltransferase in Silkworm (Bombyx mori) Affects Integument Pigmentation.
Melanosis
Mutations of an arylalkylamine-n-acetyl transferase, BM-IAANAT, are responsible for the silkworm melanism mutant.
Neoplasm Metastasis
Increased SNAT1 is a marker of human osteosarcoma and potential therapeutic target.
Neoplasms
AA-NAT, MT1 and MT2 Correlates with Cancer Stem-Like Cell Markers in Colorectal Cancer: Study of the Influence of Stage and p53 Status of Tumors.
Neoplasms
Activation of SNAT1/SLC38A1 in human breast cancer: correlation with p-Akt overexpression.
Neoplasms
Adiponectin Inhibits Nutrient Transporters and Promotes Apoptosis in Human Villous Cytotrophoblasts: Involvement in the Control of Fetal Growth.
Neoplasms
ASCT2 regulates glutamine uptake and cell growth in endometrial carcinoma.
Neoplasms
Deletion of Amino Acid Transporter ASCT2 (SLC1A5) Reveals an Essential Role for Transporters SNAT1 (SLC38A1) and SNAT2 (SLC38A2) to Sustain Glutaminolysis in Cancer Cells.
Neoplasms
Effect of TNF-alpha on the melatonin synthetic pathway in the rat pineal gland: basis for a 'feedback' of the immune response on circadian timing.
Neoplasms
Histological features and expression of enzymes implicated in melatonin synthesis in pineal parenchymal tumours and in cultured tumoural pineal cells.
Neoplasms
STAT1-NF?B crosstalk triggered by interferon gamma regulates noradrenaline-induced pineal hormonal production.
Neoplasms
The transport of glutamine into mammalian cells.
Neoplasms
TLR4 and CD14 receptors expressed in rat pineal gland trigger NFKB pathway.
Nervous System Diseases
Selective tonicity-induced expression of the neutral amino-acid transporter SNAT2 in oligodendrocytes in rat brain following systemic hypertonicity.
Obesity
Design, synthesis and in vitro evaluation of novel benzo[b]thiophene derivatives as serotonin N-acetyltransferase (AANAT) inhibitors.
Osteosarcoma
Deletion of Amino Acid Transporter ASCT2 (SLC1A5) Reveals an Essential Role for Transporters SNAT1 (SLC38A1) and SNAT2 (SLC38A2) to Sustain Glutaminolysis in Cancer Cells.
Osteosarcoma
Increased SNAT1 is a marker of human osteosarcoma and potential therapeutic target.
Paraproteinemias
Dependence on glutamine uptake and glutamine addiction characterize myeloma cells: a new attractive target.
Peritonitis
Pineal arylalkylamine N-acetyl-transferase (Aanat) gene expression as a target of inflammatory mediators in the chicken.
Pulmonary Edema
Sodium coupled neutral amino acid transporter SNAT2 counteracts cardiogenic pulmonary edema by driving alveolar fluid clearance.
Retinoblastoma
Regulation of AA-NAT and HIOMT gene expression by butyrate and cyclic AMP in Y79 human retinoblastoma cells.
Retinoblastoma
The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression.
Rett Syndrome
Dysregulation of Glutamine Transporter SNAT1 in Rett Syndrome Microglia: A Mechanism for Mitochondrial Dysfunction and Neurotoxicity.
Sarcopenia
Skeletal muscle: from birth to old age, routes to mechanical and metabolic failure.
Scoliosis
Association study of tryptophan hydroxylase 1 and arylalkylamine N-acetyltransferase polymorphisms with adolescent idiopathic scoliosis in Han Chinese.
Seizures
Differential molecular regulation of glutamate in kindling resistant rats.
Seizures
Modulation of epileptiform activity by glutamine and system A transport in a model of post-traumatic epilepsy.
Sepsis
Sepsis-induced changes in amino acid transporters and leucine signaling via mTOR in skeletal muscle.
Sleep Deprivation
AANAT1 functions in astrocytes to regulate sleep homeostasis.
Sleep Disorders, Circadian Rhythm
Arylalkylamine N-acetyltransferase (AANAT) genotype as a personal trait in melatonin synthesis.
Sleep Disorders, Circadian Rhythm
Significant association of the arylalkylamine N-acetyltransferase ( AA-NAT) gene with delayed sleep phase syndrome.
Sleep Disorders, Circadian Rhythm
The G619A Aa-nat gene polymorphism does not contribute to sleep time variation in the Brazilian population.
Sleep Wake Disorders
Computational Analysis of N-acetyl transferase in Tribolium castaneum.
Sleep Wake Disorders
Crystal structure of the dopamine N-acetyltransferase-acetyl-CoA complex provides insights into the catalytic mechanism.
Squamous Cell Carcinoma of Head and Neck
ASCT2 (SLC1A5)-dependent glutamine uptake is involved in the progression of head and neck squamous cell carcinoma.
Starvation
Amino acid starvation induces the SNAT2 neutral amino acid transporter by a mechanism that involves eukaryotic initiation factor 2alpha phosphorylation and cap-independent translation.
Starvation
Characterization and Regulation of the Amino Acid Transporter SNAT2 in the Small Intestine of Piglets.
Starvation
Deletion of Amino Acid Transporter ASCT2 (SLC1A5) Reveals an Essential Role for Transporters SNAT1 (SLC38A1) and SNAT2 (SLC38A2) to Sustain Glutaminolysis in Cancer Cells.
Starvation
Effects of starvation, re-feeding and timing of food supply on daily rhythm features of gut melatonin in carp (Catla catla).
Starvation
Enhanced small neutral but not branched chain amino acid transport after epigenetic sodium coupled neutral amino acid transporter-2 (SNAT2) cDNA expression in myoblasts.
Starvation
Proteasomal modulation of cellular SNAT2 (SLC38A2) abundance and function by unsaturated fatty acid availability.
Starvation
Specificity of amino acid regulated gene expression: analysis of genes subjected to either complete or single amino acid deprivation.
Starvation
The synthesis of SNAT2 transporters is required for the hypertonic stimulation of system A transport activity.
Stroke
Inhibition of the glutamine transporter SNAT1 confers neuroprotection in mice by modulating the mTOR-autophagy system.
Tuberculosis
Structure of Mycobacterium smegmatis Eis in complex with paromomycin.
Uterine Cervical Neoplasms
Deletion of Amino Acid Transporter ASCT2 (SLC1A5) Reveals an Essential Role for Transporters SNAT1 (SLC38A1) and SNAT2 (SLC38A2) to Sustain Glutaminolysis in Cancer Cells.
Vitamin A Deficiency
Regulation of the expression of serotonin N-acetyltransferase gene in Japanese quail (Coturnix japonica): II. Effect of vitamin A deficiency.
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0.47
2,5-dimethoxyphenylethylamine
-
pH 6.8, 37°C
0.34 - 3.46
2-(2,3-dichlorophenyl)-ethylamine
0.9 - 2.74
2-(2-chlorophenyl)-ethylamine
1.76
2-(3,4-dihydroxyphenyl)-ethylamine
-
pH 6.8, 37°C
0.62 - 1.31
2-(3-chlorophenyl)-ethylamine
1.1 - 1.65
2-(3-fluorophenyl)-ethylamine
0.75 - 1.55
2-(4-bromophenyl)-ethylamine
2.33
2-(4-chlorophenyl)ethylamine
-
pH 6.8, 37°C
1.28 - 2.2
2-(4-fluorophenyl)-ethylamine
0.98 - 1.91
2-(p-fluorophenyl)-ethylamine
1.405
2-(p-nitrophenyl)-ethylamine
-
pH 6.8, 37°C
1.17 - 1.58
2-(p-tolyl)-ethylamine
1.37
2-fluorophenylethylamine
0.49 - 1.3
2-methoxyphenylethylamine
0.17 - 9.5
2-Phenylethylamine
0.18
3-(trifluoromethyl)phenethylamine
-
wild-type, pH 8.0, 22°C
2.07
3-methoxy-2-phenylethylamine
-
pH 6.8, 37°C
0.061
3-methoxyphenethylamine
-
wild-type, pH 8.0, 22°C
1.815
3-methoxytyramine
-
pH 6.8, 37°C
0.009
5-benzyloxytryptamine
-
wild-type, pH 8.0, 22°C
0.024
5-hydroxytryptamine
-
-
0.042 - 0.63
5-methoxytryptamine
1.9
6-Hydroxydopamine
pH 6.8, 37°C
0.00031 - 1.11
acetyl-CoA
0.0019
Arachidonoyl-CoA
pH 8.0, temperature not specified in the publication
0.26
beta-methylphenethylamine
-
wild-type, pH 8.0, 22°C
0.009 - 0.173
beta-phenylethylamine
0.0018 - 0.006
butanoyl-CoA
0.04
hexanoyl-CoA
-
wild-type, pH 8.0, 22°C
0.18 - 0.23
methoxytryptamine
0.05 - 0.17
norepinephrine
0.0036
oleoyl-CoA
pH 8.0, temperature not specified in the publication
0.0099
palmitoyl-CoA
pH 8.0, temperature not specified in the publication
0.32
phenethylamine
-
wild-type, pH 8.0, 22°C
0.34 - 11
Phenylethylamine
0.066 - 0.47
propionyl-CoA
0.006
stearoyl-CoA
pH 8.0, temperature not specified in the publication
additional information
additional information
-
0.34
2-(2,3-dichlorophenyl)-ethylamine
pH 6.8, 37°C
3.46
2-(2,3-dichlorophenyl)-ethylamine
-
pH 6.8, 37°C
0.9
2-(2-chlorophenyl)-ethylamine
-
pH 6.8, 37°C
2.74
2-(2-chlorophenyl)-ethylamine
pH 6.8, 37°C
0.62
2-(3-chlorophenyl)-ethylamine
pH 6.8, 37°C
1.31
2-(3-chlorophenyl)-ethylamine
-
pH 6.8, 37°C
1.1
2-(3-fluorophenyl)-ethylamine
pH 6.8, 37°C
1.65
2-(3-fluorophenyl)-ethylamine
-
pH 6.8, 37°C
0.75
2-(4-bromophenyl)-ethylamine
pH 6.8, 37°C
1.55
2-(4-bromophenyl)-ethylamine
-
pH 6.8, 37°C
1.28
2-(4-fluorophenyl)-ethylamine
-
pH 6.8, 37°C
2.2
2-(4-fluorophenyl)-ethylamine
pH 6.8, 37°C
0.98
2-(p-fluorophenyl)-ethylamine
pH 6.8, 37°C
1.91
2-(p-fluorophenyl)-ethylamine
-
pH 6.8, 37°C
1.17
2-(p-tolyl)-ethylamine
pH 6.8, 37°C
1.58
2-(p-tolyl)-ethylamine
-
pH 6.8, 37°C
1.37
2-fluorophenylethylamine
-
pH 6.8, 37°C
1.37
2-fluorophenylethylamine
pH 6.8, 37°C
0.49
2-methoxyphenylethylamine
-
pH 6.8, 37°C
1.3
2-methoxyphenylethylamine
pH 6.8, 37°C
0.17
2-Phenylethylamine
pH 6.8, 37°C
1.8
2-Phenylethylamine
-
pH 6.8, 37°C
9.5
2-Phenylethylamine
pH 6.8, 37°C
0.042
5-methoxytryptamine
-
wild-type, pH 8.0, 22°C
0.2
5-methoxytryptamine
-
-
0.63
5-methoxytryptamine
-
pH 7.8, 45°C
0.00031
acetyl-CoA
-
-
0.00142
acetyl-CoA
pH 7.4, 37°C
0.0061
acetyl-CoA
pH 8.0, temperature not specified in the publication
0.013
acetyl-CoA
-
mutant E26A, pH 8.0, 22°C
0.019
acetyl-CoA
-
mutant S171A, pH 8.0, 22°C
0.0287
acetyl-CoA
-
cosubstrate tryptamine
0.029
acetyl-CoA
-
wild-type, pH 8.0, 22°C
0.029
acetyl-CoA
-
mutant T167A/S171A, pH 8.0, 22°C
0.05
acetyl-CoA
-
cosubstrate tryptamine, pineal gland
0.12
acetyl-CoA
cosubstrate histamine, pH 7.0, 25°C
0.125
acetyl-CoA
-
cosubstrate tryptamine, liver
0.14
acetyl-CoA
-
mutant T167A, pH 8.0, 22°C
0.21
acetyl-CoA
-
mutant H206A, pH 8.0, 22°C
0.265
acetyl-CoA
-
pH 6.8, 37°C
0.27
acetyl-CoA
cosubstrate tyramine, pH 7.0, 25°C
0.48
acetyl-CoA
-
cosubstrate octopamine, pH 7.0, 25°C
0.53
acetyl-CoA
pH 6.8, 37°C
0.55
acetyl-CoA
-
mutant R138A, pH 8.0, 22°C
0.65
acetyl-CoA
pH 6.8, 37°C
1.11
acetyl-CoA
pH 6.8, 27°C
0.009
beta-phenylethylamine
-
-
0.173
beta-phenylethylamine
-
-
0.0018
butanoyl-CoA
pH 8.0, temperature not specified in the publication
0.006
butanoyl-CoA
-
wild-type, pH 8.0, 22°C
0.11
dopamine
pH not specified in the publication, temperature not specified in the publication
0.17
dopamine
-
wild-type, pH 8.0, 22°C
0.19
dopamine
-
pH 7.3, 22°C, recombinant aaNAT1
0.27
dopamine
-
pH 7.3, 22°C, recombinant aaNAT2
11
dopamine
-
cosubstrate acetyl-CoA, pH 7.0, 25°C
0.0023
histamine
-
mutant H206A, pH 8.0, 22°C
0.0034
histamine
-
mutant S171A, pH 8.0, 22°C
0.0049
histamine
-
mutant R138A, pH 8.0, 22°C
0.0067
histamine
-
mutant T167A, pH 8.0, 22°C
0.013
histamine
-
mutant T167A/S171A, pH 8.0, 22°C
0.016
histamine
-
mutant E26A, pH 8.0, 22°C
0.52
histamine
-
cosubstrate acetyl-CoA, wild-type, pH 8.0, 22°C
1.92
histamine
-
pH 7.5, 22°C
2.8
histamine
cosubstrate acetyl-CoA, pH 7.0, 25°C
2.9
histamine
-
cosubstrate butanoyl-CoA, wild-type, pH 8.0, 22°C
15
histamine
-
cosubstrate hexanoyl-CoA, wild-type, pH 8.0, 22°C
16
histamine
cosubstrate acetyl-CoA, pH 7.0, 25°C
0.18
methoxytryptamine
-
pH 7.3, 22°C, recombinant aaNAT1
0.23
methoxytryptamine
-
pH 7.3, 22°C, recombinant aaNAT2
0.05
norepinephrine
pH not specified in the publication, temperature not specified in the publication
0.16
norepinephrine
-
pH 7.3, 22°C, recombinant aaNAT1
0.17
norepinephrine
-
pH 7.3, 22°C, recombinant aaNAT2
0.002
octopamine
-
-
0.07
octopamine
pH not specified in the publication, temperature not specified in the publication
0.12
octopamine
-
wild-type, pH 8.0, 22°C
0.13
octopamine
-
pH 7.3, 22°C, recombinant aaNAT2
0.14
octopamine
-
pH 7.3, 22°C, recombinant aaNAT1
0.94
octopamine
-
cosubstrate acetyl-CoA, pH 7.0, 25°C
6.2
octopamine
cosubstrate acetyl-CoA, pH 7.0, 25°C
30
octopamine
cosubstrate acetyl-CoA, pH 7.0, 25°C
0.34
Phenylethylamine
-
11
Phenylethylamine
-
cosubstrate acetyl-CoA, pH 7.0, 25°C
0.066
propionyl-CoA
-
cosubstrate octopamine, pH 7.0, 25°C
0.098
propionyl-CoA
cosubstrate tyramine, pH 7.0, 25°C
0.47
propionyl-CoA
cosubstrate histamine, pH 7.0, 25°C
0.05
serotonin
-
0.06
serotonin
-
wild-type enzyme
0.096
serotonin
-
wild-type enzyme with 14-3-3 protein
0.106
serotonin
-
wild-type enzyme with protein kinase A
0.16
serotonin
-
wild-type, pH 8.0, 22°C
0.23
serotonin
-
pH 7.3, 22°C, recombinant aaNAT1
0.232
serotonin
-
pH 7.8, 45°C
0.371
serotonin
pH 8.8, 45°C
0.42
serotonin
-
pH 7.3, 22°C, recombinant aaNAT2
0.467
serotonin
-
pH 8.8, 55°C
0.64
serotonin
-
pH 6.8, 37°C
1.35
serotonin
pH 6.8, 37°C
1.7
serotonin
pH 6.8, 37°C
2.05
serotonin
pH 6.8, 27°C
13
serotonin
-
cosubstrate acetyl-CoA, pH 7.0, 25°C
0.0017
tryptamine
-
0.00331
tryptamine
pH 7.4, 37°C
0.026
tryptamine
-
wild-type, pH 8.0, 22°C
0.1
tryptamine
pH not specified in the publication, temperature not specified in the publication
0.16
tryptamine
-
pH 7.3, 22°C, recombinant aaNAT1
0.17
tryptamine
-
pH 6.8, 30°C, phosphorylated T31, unphosphorylated S205
0.17
tryptamine
-
pH 7.3, 22°C, recombinant aaNAT2
0.18
tryptamine
-
pH 6.8, 30°C, unphosphorylated enzyme
0.25
tryptamine
-
pH 6.8, 30°C, mutant enzyme S205A, phosphorylated T31
0.28
tryptamine
-
pH 6.8, 30°C, mutant enzyme S205A, unphosphorylated
0.291
tryptamine
-
pH 6.8, 37°C, mutant enzyme S192V
0.3
tryptamine
-
pH 6.8, 30°C, mutant enzyme T31A, phosphorylated S205
0.31
tryptamine
-
pH 6.8, 30°C, mutant enzyme T31A, unphosphorylated
0.317
tryptamine
-
pH 6.8, 37°C, mutant enzyme T29V/S203G
0.33
tryptamine
pH 6.8, 37°C, recombinant wild-type enzyme
0.344
tryptamine
-
pH 6.8, 37°C, mutant enzyme T127V
0.361
tryptamine
-
pH 6.8, 37°C, wild-type enzyme
0.413
tryptamine
-
pH 6.8, 37°C, mutant enzyme T29V
0.417
tryptamine
-
pH 6.8, 37°C, mutant enzyme S203G
0.53
tryptamine
-
pineal gland
1.4
tryptamine
pH 6.8, 27°C
2.3
tryptamine
pH 6.8, 37°C, recombinant mutant I57A/V59A
4
tryptamine
above, pH 6.8, 37°C, recombinant mutants P64A, P64G, P64W, and recombinant truncation mutants
4.3
tryptamine
-
cosubstrate acetyl-CoA, pH 7.0, 25°C
0.0015
tyramine
-
-
0.042
tyramine
-
wild-type, pH 8.0, 22°C
0.17
tyramine
-
pH 7.3, 22°C, recombinant aaNAT1
0.23
tyramine
-
pH 7.3, 22°C, recombinant aaNAT2
0.56
tyramine
pH not specified in the publication, temperature not specified in the publication
57
tyramine
-
cosubstrate acetyl-CoA, pH 7.0, 25°C
additional information
additional information
-
apparent Km-values
-
additional information
additional information
-
apparent Km-values
-
additional information
additional information
formation and cleavage of a disulfide bond produce active/inactive states of enzyme
-
additional information
additional information
-
exposing chickens to light in the middle of the night increased the apparent Km of AANAT for tryptamine by about 10fold. The Km began to increase within 5 min of exposure to light and reached a maximum at about 30 min
-
additional information
additional information
-
kinetics of recombinant partially phosphorylated wild-type and mutant enzymes, overview
-
additional information
additional information
kinetics of recombinant wild-type and mutant enzymes, substrate tryptamine, overview
-
additional information
additional information
-
AANAT2 kinetic constants as a function of temperature, overview
-
additional information
additional information
-
AANAT2 kinetic constants as a function of temperature, overview
-
additional information
additional information
-
AANAT2 kinetic constants as a function of temperature, overview
-
additional information
additional information
-
AANAT2 kinetics in relation to temperature, overview
-
additional information
additional information
-
AANAT2 kinetics in relation to temperature, overview
-
additional information
additional information
-
Michaelis-Menten kinetic analysis
-
additional information
additional information
both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b
-
additional information
additional information
both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b
-
additional information
additional information
both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b
-
additional information
additional information
-
both isoforms Aanat1a and Aanat1b display 2- to 3fold lower KM values for indolethylamines compared to phenylethylamines. KM for phenylethylamines is around two times lower for Aanat1a than for Aanat1b
-
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malfunction
the abnormal Bm-iAANAT is responsible for the mln mutant, phenotype, overview. The content of dopamine in the mln mutant is about 2times higher than in the wild-type. A greater accumulation of dopamine results from the functional deficiency of Bm-iAANAT in the mutant and that the excessive dopamine is converted into dopamine melanin, causing the darker color pattern of the sclerified regions in the mln mutant compared with the wild-type
evolution
-
AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature
evolution
-
AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature
evolution
-
AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature
evolution
-
AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature
evolution
-
AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature
evolution
-
AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature
evolution
-
AANAT2 evolution is mainly driven by phylogenetic relationships although catalytic properties (enzyme turnover and substrate affinity) are also under the influence of the respective species normal habitat temperature
evolution
evolution of insect arylalkylamine N-acetyltransferases, structural evidence from the yellow fever mosquito, Aedes aegypti, overview
metabolism
-
the enzyme catalyzes the first step in melatonin biosynthesis, melatonin biosynthesis follows a 24 h day and night rhythm, which is different in fasted, fed, and refed fish, overview
metabolism
-
the enzyme catalyzes the first step in melatonin biosynthesis, melatonin biosynthesis follows a 24 h day and night rhythm, which is different in fasted, fed, and refed fish, overview
metabolism
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis
metabolism
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis
metabolism
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis, melatonin biosynthesis pathway overview
metabolism
-
arylalkylamine N-acetyltransferase is the rate-limiting enzyme of the melatonin biosynthesis pathway
metabolism
-
serotonin N-acetyltransferase is a rate-limiting enzyme in melatonin biosynthesis in vertebrates
metabolism
N-terminally acetylated Ac-AANAT is degraded through the recognition of its N-terminally acetylated N-terminal Met residue by the Ac/N-end rule pathway, whereas the non-N-terminally acetylated AANAT is targeted by the Arg/N-end rule pathway, which recognizes the unacetylated N-terminal Met-Leu sequence of rat AANAT. Degradation of Lys8Arg mutants of rat AANAT is mediated by polyubiquitylation of its Lys residue(s)
metabolism
the N-terminal sequence of human AANAT differs from that of rodent AANATs. The human enzyme is longer-lived than its rat counterpart and appears to be refractory to degradation by the N-end rule pathway
physiological function
-
AANAT is a key circadian rhythm enzyme that drives the nocturnal production of melatonin in the pineal
physiological function
-
Aanat2 is the main enzyme responsible of the plasma nocturnal melatonin increase in the fish
physiological function
-
the enzyme catalyzes the rate-limiting step in melatonin synthesis, melatonin is a hormone acting as a synchronizer for the circadian system, overview. Evolution of the pineal gland and the circadian system involving melatonin, overview
physiological function
-
the melatonin synthetic enzyme arylalkylamine N-acetyltransferase is a significant element in a possible reactive oxygen species removal system. UV signals initiate melatonin synthesis for reactive oxgene species removal in mites
physiological function
aaNATs are involved in sclerotization and neurotransmitter inactivation in insects
physiological function
-
arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature
physiological function
-
arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature
physiological function
-
arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature
physiological function
-
arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature
physiological function
-
arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature
physiological function
-
arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature
physiological function
-
arylalkylamine N-acetyltransferase-2 is the enzyme responsible for the rhythmic production of the time-keeping hormone melatonin. It plays a crucial role in the synchronization of biological functions with changes in the environment. Annual and daily fluctuations in light are known to be key environmental factors involved in such synchronization. AANAT2 activity is also markedly influenced by temperature
physiological function
arylalkylamine-N-acetyltransferases play a role in color pattern mutation in Lepidoptera, the BmiAANAT gene plays an essential role in the pigment metabolism in silkworm
physiological function
melatonin influences circadian rhythms and seasonal behavioral changes in vertebrates, it is synthesized from serotonin by N-acetylation by arylalkylamine N-acetyltransferase and O-methylation by N-acetylserotonin methyltransferase, EC 2.1.1.4
physiological function
-
serotonin N-acetyltransferase is responsible for the production of N-acetylserotonin, an intermediate of melatonin biosynthesis. Melatonin, i.e. N-acetyl-5-methoxytryptamine, has multiple functions in vertebrates, including the regulation of circadian rhythms and photoperiodism. Plant melatonin is involved in cold stress
physiological function
Aanat1 isoforms have a broad range of functions including melatonin synthesis in the retina, and catabolism of serotonin and dopamine in the retina and other tissues
physiological function
isoform AANAT1 is an important enzyme in the regulation of dopamine and N-acetyldopamine content in liver
physiological function
isoform Aanat2 is a pineal enzyme involved in melatonin production
physiological function
isoform AANATL2 has a role in the biosynthetic formation of long-chain N-acylserotonins and N-acydopamines
physiological function
suppression of gene expression leads to melanin deposition in the head and integument. An increase in dopamine levels affects melanism patterns on the heads of transgenic worms. A reduction in the enzyme activity of AANAT leads to changes in dopamine levels
physiological function
-
a knockout mutant exhibits delayed flowering. Melatonin levels are 50% lower in flowers of the mutant than in those of the wild-type, but the melatonin levels of leaves do not differ
physiological function
-
a significant negative correlation exists between plasma levels of the thyroid hormones T3 and T4 and AANAT activity. A direct relationship exists between water temperature/daylength and plasma levels of thyroid hormones, and an inverse relationship between water temperature/daylength and AANAT activity. The acrophase (peak) of the circadian rhythm of both T3 and T4 occurs around midday, while the acrophase of AANAT activity rhythm is recorded during midnight
physiological function
AANAT levels and melatonin synthesis increase after TRPV4 channel stimulation in ciliary body epithelium
physiological function
-
CoA and acetyl-CoA alter the conformation of the substrate binding site of arylalkylamine N-acetyltransferase to facilitate interaction with acceptor substrates. It is the presence of the acetyl group within the catalytic funnel that triggers high affinity binding. Acetyl group occupancy is relayed through a conserved salt bridge between the P-loop and the acceptor binding site, and is manifested as differential dynamics in the CoA and acetyl-CoA-bound states
physiological function
loss of function of AANAT1 caused by RNAi has no effect on larval and pupal development. The tanning of pupal setae, gin traps and urogomphi proceeds normally. About 70% of the resulting adults exhibit a roughened exoskeletal surface, separated elytra and improperly folded hindwings. The body wall, elytra and veins of the hindwing of the mature adults are significantly darker than those of control insects probably due to the accumulation of dopamine melanin
physiological function
suppression of both isoforms SNAT1 and SNAT2 leads to retarded seedling growths in conjunction with severe decreases in melatonin compared to wild-types and single-suppression rice plants. The laminar angle is decreased in the SNAT1/SNAT2 suppression rice compared to that of the wild-types and SNAT1 suppression, but is comparable to that of SNAT2 suppression strain. The reduced germination speed in the SNAT1/SNAT2 suppression strain is comparable to that of SNAT2 suppression lines. The SNAT1 suppression strain is the most severely deteriorated, followed by SNAT1/SNAT2 suppression and SNAT2 suppression strains
physiological function
transgenic rice plants overexpressing rice SNAT1 do not show enhanced seedling growth. SNAT1-overexpressing rice plants show significant resistance to cadmium and senescence stresses relative to wild-type controls. Melatonin synthesis in rice seedlings is not induced by selenium and SNAT1 transgenic rice plants do not show tolerance to selenium. T2 homozygous SNAT1 transgenic rice plants exhibit increased grain yield due to increased panicle number per plant under paddy field conditions
physiological function
-
melatonin influences circadian rhythms and seasonal behavioral changes in vertebrates, it is synthesized from serotonin by N-acetylation by arylalkylamine N-acetyltransferase and O-methylation by N-acetylserotonin methyltransferase, EC 2.1.1.4
-
additional information
three clusters of aaNAT-like sequences in insects: typical insect aaNAT, polyamine NAT-like aaNAT, and mosquito unique putative aaNAT, paaNAT. aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
additional information
-
three clusters of aaNAT-like sequences in insects: typical insect aaNAT, polyamine NAT-like aaNAT, and mosquito unique putative aaNAT, paaNAT. aaNAT2, a protein from the typical insect aaNAT cluster, uses histamine as a substrate as well as arylalkylamines
additional information
under light-dark conditions, a rhythmic pattern of melatonin levels occurs with higher levels toward the middle of the night, peaking at zeitgeber time ZT18, and with a minimum value around ZT0-6. AA-NAT activity shows a diurnal and circadian fluctuation with higher levels of activity during the early night, both under light-dark conditions and constant darkness conditions. A peak is found around ZT12 and circadian time CT12. Light acts on AA-NAT through a well-known phototransduction mechanism that originates in the retina, is mediated by the retinohypothalamic tract, and processed in the hypothalamic suprachiasmatic nuclei, SCN, the site of the master circadian clock. From the SCN, the photic message is transduced through the sympathetic nervous system to the pineal, where noradrenergic receptors, among others, control the activity of AA-NAT
additional information
-
under light-dark conditions, a rhythmic pattern of melatonin levels occurs with higher levels toward the middle of the night, peaking at zeitgeber time ZT18, and with a minimum value around ZT0-6. AA-NAT activity shows a diurnal and circadian fluctuation with higher levels of activity during the early night, both under light-dark conditions and constant darkness conditions. A peak is found around ZT12 and circadian time CT12. Light acts on AA-NAT through a well-known phototransduction mechanism that originates in the retina, is mediated by the retinohypothalamic tract, and processed in the hypothalamic suprachiasmatic nuclei, SCN, the site of the master circadian clock. From the SCN, the photic message is transduced through the sympathetic nervous system to the pineal, where noradrenergic receptors, among others, control the activity of AA-NAT
additional information
-
under light-dark conditions, a rhythmic pattern of melatonin levels occurs with higher levels toward the middle of the night, peaking at zeitgeber time ZT18, and with a minimum value around ZT0-6. AA-NAT activity shows a diurnal and circadian fluctuation with higher levels of activity during the early night, both under light-dark conditions and constant darkness conditions. A peak is found around ZT12 and circadian time CT12. Light acts on AA-NAT through a well-known phototransduction mechanism that originates in the retina, is mediated by the retinohypothalamic tract, and processed in the hypothalamic suprachiasmatic nuclei, SCN, the site of the master circadian clock. From the SCN, the photic message is transduced through the sympathetic nervous system to the pineal, where noradrenergic receptors, among others, control the activity of AA-NAT
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Fajardo, N.; Abreu, P.; Alonso, R.
Determination of kinetic properties of serotonin-N-acetyltransferase in bovine pineal gland using HPLC with fluorimetric detection
J. Pineal Res.
13
80-84
1992
Bos taurus, Rattus norvegicus
brenda
Morrissey, J.J.; Edwards, S.B.; Lovenberg, W.
Comparison of rat pineal gland and rat liver serotonin-N-acetyltransferase
Biochem. Biophys. Res. Commun.
77
118-123
1977
Rattus norvegicus
brenda
Ohtomi, M.; Sasaki, M.; Deguchi, T.
Two arylamine N-acetyltransferases from chicken pineal gland as identified by cDNA cloning
Eur. J. Biochem.
185
253-261
1989
Gallus gallus
brenda
Namboodiri, M.A.A.; Dubbels, R.; Klein, D.C.
Arylalkylamine N-acetyltransferase from mammalian pineal gland
Methods Enzymol.
142
583-590
1987
Ovis aries, Rattus norvegicus
brenda
Voisin, P.; Namboodiri, M.A.A.; Klein, D.C.
Arylamine N-acetyltransferase and arylalkylamine N-acetyltransferase in the mammalian pineal gland
J. Biol. Chem.
259
10913-10918
1984
Ovis aries, Rattus norvegicus
brenda
Withyachumnarnkul, B.; Pongsa-Asawapaiboon, A.; Poolsanguan, B.
Characteristics of the enzyme N-acetyltransferase in the optic lobe of the giant freshwater prawn, Macrobrrachium rosenbergii
Comp. Biochem. Physiol. B
104
449-454
1993
Macrobrachium rosenbergii
-
brenda
Namboodiri, M.A.A.; Brownstein, M.J.; Voisin, P.; Weller, J.L.; Klein, D.C.
A simple and rapid method for the purification of ovine pineal arylalkylamine N-acetyltransferase
J. Neurochem.
48
580-585
1987
Ovis aries, Rattus norvegicus
brenda
Rodriguez-Cabello, J.C.; Agapito, M.T.; Garcia-Herrero, I.; Recio, J.M.
Effects of EGTA and calmodulin, neutral thiol proteinases and protein kinase C inhibitors on loss of chicken pineal serotonin N-acetyltransferase activity
J. Comp. Physiol. B
159
583-588
1989
Gallus gallus
brenda
Namboodiri, M.A.A.; Brownstein, M.J.; Weller, J.L.; Voisin, P.; Klein, D.C.
Multiple forms of arylalkylamine N-acetyltransferases in the rat pineal gland: purification of one molecular form
J. Pineal Res.
4
235-246
1987
Rattus norvegicus
brenda
Deguchi, T.
Characteristics of serotonin-acetyl coenzyme A N-acetyltransferase in pineal gland of rat
J. Neurochem.
24
1083-1085
1975
Rattus norvegicus
brenda
Fleming, J.V.; Barrett, P.; Coon, S.L.; Klein, D.C.; Morgan, P.J.
Ovine arylalkylamine N-acetyltransferase in the pineal and pituitary glands: differences in function and regulation
Endocrinology
140
972-978
1999
Ovis aries
brenda
Falcon, J.; Galarneau, K.M.; Weller, J.L.; Ron, B.; Chen, G.; Coon, S.L.; Klein, D.C.
Regulation of arylalkylamine N-acetyltransferase-2 (AANAT2, EC 2.3.1.87) in the fish pineal organ: evidence for a role of proteasomal proteolysis
Endocrinology
142
1804-1813
2001
Esox sp., Sparus aurata, trout
brenda
Coon, S.L.; Del Olmo, E.; Young, W.S.; Klein, D.C.
Melatonin synthesis enzymes in Macaca mulatta: focus on arylalkylamine N-acetyltransferase (EC 2.3.1.87)
J. Clin. Endocrinol. Metab.
87
4699-4706
2002
Macaca mulatta (O97756), Macaca mulatta
brenda
Aisien, S.O.; Hellmund, C.; Walter, R.D.
Characterization of the arylalkylamine N-acetyltransferase in Onchocerca volvulus
Parasitol. Res.
82
369-371
1996
Onchocerca volvulus
brenda
Obsil, T.; Ghirlando, R.; Klein, D.C.; Ganguly, S.; Dyda, F.
Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex: a role for scaffolding in enzyme regulation
Cell
105
257-267
2001
Ovis aries
brenda
Hamada, T.; Ootomi, M.; Horikawa, K.; Niki, T.; Wakamatu, H.; Ishida, N.
The expression of the melatonin synthesis enzyme: arylalkylamine N-acetyltransferase in the suprachiasmatic nucleus of rat brain
Biochem. Biophys. Res. Commun.
258
772-777
1999
Rattus norvegicus
brenda
Amherd, R.; Hintermann, E.; Walz, D.; Affolter, M.; Meyer, U.A.
Purification, cloning, and characterization of a second arylalkylamine N-acetyltransferase from Drosophila melanogaster
DNA Cell Biol.
19
697-705
2000
Drosophila melanogaster, Drosophila melanogaster AANAT2
brenda
Alonso-Gomez, A.L.; Valenciano, A.I.; Alonso-Bedate, M.; Delgado, M.J.
Differential characteristics and regulation of arylamine and arylalkylamine N-acetyltransferases in the frog retina (Rana perezi)
Neurochem. Int.
26
223-231
1995
Pelophylax perezi
brenda
Ivanova, T.N.; Michael Iuvone, P.
Melatonin synthesis in retina: circadian regulation of arylalkylamine N-acetyltransferase activity in cultured photoreceptor cells of embryonic chicken retina
Brain Res.
973
56-63
2003
Gallus gallus
brenda
De Angelis, J.; Gastel, J.; Klein, D.C.; Cole, P.A.
Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87)
J. Biol. Chem.
273
3045-3050
1998
Ovis aries
brenda
Tsuboi, S.; Kotani, Y.; Ogawa, K.i.; Hatanaka, T.; Yatsushiro, S.; Otsuka, M.; Moriyama, Y.
An Intramolecular Disulfide Bridge as a Catalytic Switch for Serotonin N-Acetyltransferase
J. Biol. Chem.
277
44229-44235
2002
Rattus norvegicus (Q64666)
brenda
Scheibner, K.A.; De Angelis, J.; Burley, S.K.; Cole, P.A.
Investigation of the roles of catalytic residues in serotonin N-acetyltransferase
J. Biol. Chem.
277
18118-18126
2002
Ovis aries (Q29495)
brenda
Khalil, E.M.; De Angelis, J.; Cole, P.A.
Indoleamine analogs as probes of the substrate selectivity and catalytic mechanism of serotonin N-acetyltransferase
J. Biol. Chem.
273
30321-30327
1998
Ovis aries
brenda
Ferry, G.; Loynel, A.; Kucharczyk, N.; Bertin, S.; Rodriguez, M.; Delagrange, P.; Galizzi, J.P.; Jacoby, E.; Volland, J.P.; Lesieur, D.; Renard, P.; Canet, E.; Fauchere, J.L.; Boutin, J.A.
Substrate specificity and inhibition studies of human serotonin N-acetyltransferase
J. Biol. Chem.
275
8794-8805
2000
Ovis aries, Homo sapiens
brenda
Ichihara, N.; Okada, M.; Takeda, M.
Characterization and purification of polymorphic arylalkylamine N-acetyltransferase from the American cockroach, Periplaneta americana
Insect Biochem. Mol. Biol.
32
15-22
2001
Periplaneta americana
brenda
Ichihara, N.; Okada, M.; Nakagawa, H.; Takeda, M.
Purification and characterization of arylalkylamine N-acetyltransferase from cockroach testicular organs
Insect Biochem. Mol. Biol.
27
241-246
1997
Periplaneta americana
brenda
Asano, H.; Bembenek, J.; Takeda, M.
Multiple forms of arylalkylamine N-acetyltransferase (NAT) from cockroach female colleterial glands and activity changes during oocyte maturation
Comp. Biochem. Physiol. A
134A
795-803
2003
Periplaneta americana
-
brenda
Bembenek, J.; Sehadova, H.; Ichihara, N.; Takeda, M.
Day/night fluctuations in melatonin content, arylalkylamine N-acetyltransferase activity and NAT mRNA expression in the CNS, peripheral tissues and hemolymph of the cockroach, Periplaneta americana
Comp. Biochem. Physiol. B
140
27-36
2005
Periplaneta americana
brenda
Ferry, G.; Ubeaud, C.; Mozo, J.; Pean, C.; Hennig, P.; Rodriguez, M.; Scoul, C.; Bonnaud, A.; Nosjean, O.; Galizzi, J.P.; Delagrange, P.; Renard, P.; Volland, J.P.; Yous, S.; Lesieur, D.; Boutin, J.A.
New substrate analogues of human serotonin N-acetyltransferase produce in situ specific and potent inhibitors
Eur. J. Biochem.
271
418-428
2004
Homo sapiens
brenda
Zilberman-Peled, B.; Benhar, I.; Coon, S.L.; Ron, B.; Gothilf, Y.
Duality of serotonin-N-acetyltransferase in the gilthead seabream (Sparus aurata): molecular cloning and characterization of recombinant enzymes
Gen. Comp. Endocrinol.
138
139-147
2004
Sparus aurata (Q68SL6), Sparus aurata (Q68SL7), Sparus aurata
brenda
Choi, B.H.; Chae, H.D.; Park, T.J.; Oh, J.; Lim, J.; Kang, S.S.; Ha, H.; Kim, K.T.
Protein kinase C regulates the activity and stability of serotonin N-acetyltransferase
J. Neurochem.
90
442-454
2004
Rattus norvegicus
brenda
Schomerus, C.; Laedtke, E.; Korf, H.W.
Activation of arylalkylamine N-acetyltransferase by phorbol esters in bovine pinealocytes suggests a novel regulatory pathway in melatonin synthesis
J. Neuroendocrinol.
16
741-749
2004
Bos taurus
brenda
Ganguly, S.; Weller, J.L.; Ho, A.; Chemineau, P.; Malpaux, B.; Klein, D.C.
Melatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205
Proc. Natl. Acad. Sci. USA
102
1222-1227
2005
Ovis aries
brenda
Ferry, G.; Ubeaud, C.; Dauly, C.; Mozo, J.; Guillard, S.; Berger, S.; Jimenez, S.; Scoul, C.; Leclerc, G.; Yous, S.; Delagrange, P.; Boutin, J.A.
Purification of the recombinant human serotonin N-acetyltransferase (EC 2.3.1.87): further characterization of and comparison with AANAT from other species
Protein Expr. Purif.
38
84-98
2004
Ovis aries, Homo sapiens (Q16613), Homo sapiens, Rattus norvegicus (Q64666)
brenda
Bembenek, J.; Sakamoto, K.; Takeda, M.
Molecular cloning of a cDNA encoding arylalkylamine N-acetyltransferase from the testicular system of Periplaneta americana: primary protein structure and expression analysis
Arch. Insect Biochem. Physiol.
59
219-229
2005
Periplaneta americana (Q76EI8), Periplaneta americana
brenda
Zilberman-Peled, B.; Ron, B.; Gross, A.; Finberg, J.P.; Gothilf, Y.
A possible new role for fish retinal serotonin-N-acetyltransferase-1 (AANAT1): Dopamine metabolism
Brain Res.
1073-1074
220-228
2006
Sparus aurata (Q68SL7), Danio rerio (Q6V7J8), Danio rerio
brenda
Tosini, G.; Chaurasia, S.S.; Michael Iuvone, P.
Regulation of arylalkylamine N-acetyltransferase (AANAT) in the retina
Chronobiol. Int.
23
381-391
2006
Macaca mulatta (O97756), Gallus gallus (P79774), Rattus norvegicus (Q64666), Rattus norvegicus Fischer (Q64666)
brenda
Tsugehara, T.; Iwai, S.; Fujiwara, Y.; Mita, K.; Takeda, M.
Cloning and characterization of insect arylalkylamine N-acetyltransferase from Bombyx mori
Comp. Biochem. Physiol. B Biochem. Mol. Biol.
147
358-366
2007
Bombyx mori (A0EM56), Bombyx mori
brenda
Ho, A.K.; Terriff, D.L.; Price, D.M.; Wloka, M.T.; Chik, C.L.
The role of inducible repressor proteins in the adrenergic induction of arylalkylamine-N-acetyltransferase and mitogen-activated protein kinase phosphatase-1 in rat pinealocytes
Endocrinology
148
743-751
2007
Rattus norvegicus (Q64666)
brenda
Fernandez-Duran, B.; Ruibal, C.; Polakof, S.; Ceinos, R.M.; Soengas, J.L.; Miguez, J.M.
Evidence for arylalkylamine N-acetyltransferase (AANAT2) expression in rainbow trout peripheral tissues with emphasis in the gastrointestinal tract
Gen. Comp. Endocrinol.
152
289-294
2006
Oncorhynchus mykiss (Q9PT39), Oncorhynchus mykiss
brenda
Zheng, W.; Schwarzer, D.; Lebeau, A.; Weller, J.L.; Klein, D.C.; Cole, P.A.
Cellular stability of serotonin N-acetyltransferase conferred by phosphonodifluoromethylene alanine (Pfa) substitution for Ser-205
J. Biol. Chem.
280
10462-10467
2005
Ovis aries (Q29495)
brenda
Han, S.; Kim, T.D.; Ha, D.C.; Kim, K.T.
Rhythmic expression of adenylyl cyclase VI contributes to the differential regulation of serotonin N-acetyltransferase by bradykinin in rat pineal glands
J. Biol. Chem.
280
38228-38234
2005
Rattus norvegicus (Q64666)
brenda
Koch, M.; Dehghani, F.; Habazettl, I.; Schomerus, C.; Korf, H.W.
Cannabinoids attenuate norepinephrine-induced melatonin biosynthesis in the rat pineal gland by reducing arylalkylamine N-acetyltransferase activity without involvement of cannabinoid receptors
J. Neurochem.
98
267-278
2006
Rattus norvegicus (Q64666)
brenda
Pozdeyev, N.; Taylor, C.; Haque, R.; Chaurasia, S.S.; Visser, A.; Thazyeen, A.; Du, Y.; Fu, H.; Weller, J.; Klein, D.C.; Iuvone, P.M.
Photic regulation of arylalkylamine N-acetyltransferase binding to 14-3-3 proteins in retinal photoreceptor cells
J. Neurosci.
26
9153-9161
2006
Gallus gallus
brenda
Huang, Z.; Deng, J.; Borjigin, J.
A novel H28Y mutation in LEC rats leads to decreased NAT protein stability in vivo and in vitro
J. Pineal Res.
39
84-90
2005
Rattus norvegicus (Q64666)
brenda
Coon, S.L.; Klein, D.C.
Evolution of arylalkylamine N-acetyltransferase: emergence and divergence
Mol. Cell. Endocrinol.
252
2-10
2006
Pelophylax perezi
brenda
Rosiak, J.; Zawilska, J.B.
Near-ultraviolet light perceived by the retina generates the signal suppressing melatonin synthesis in the chick pineal gland-an involvement of NMDA glutamate receptors
Neurosci. Lett.
379
214-217
2005
Gallus gallus (P79774), Gallus gallus
brenda
Iuvone, P.M.; Tosini, G.; Pozdeyev, N.; Haque, R.; Klein, D.C.; Chaurasia, S.S.
Circadian clocks, clock networks, arylalkylamine N-acetyltransferase, and melatonin in the retina
Prog. Retin. Eye Res.
24
433-456
2005
Gallus gallus, Rattus norvegicus, Xenopus laevis
brenda
Tsugehara, T.; Iwai, S.; Fujiwara, Y.; Mita, K.; Takeda, M.
Cloning and characterization of insect arylalkylamine N-acetyltransferase from Bombyx mori
Comp. Biochem. Physiol. B
147B
358-366
2007
Bombyx mori
brenda
Falcon, J.; Besseau, L.; Fuentes, M.; Sauzet, S.; Magnanou, E.; Boeuf, G.
Structural and functional evolution of the pineal melatonin system in vertebrates
Ann. N. Y. Acad. Sci.
1163
101-111
2009
vertebrata
brenda
Szewczuk, L.M.; Tarrant, M.K.; Sample, V.; Drury, W.J.; Zhang, J.; Cole, P.A.
Analysis of serotonin N-acetyltransferase regulation in vitro and in live cells using protein semisynthesis
Biochemistry
47
10407-10419
2008
Homo sapiens
brenda
Ceinos, R.M.; Polakof, S.; Illamola, A.R.; Soengas, J.L.; Miguez, J.M.
Food deprivation and refeeding effects on pineal indoles metabolism and melatonin synthesis in the rainbow trout Oncorhynchus mykiss
Gen. Comp. Endocrinol.
156
410-417
2008
Oncorhynchus mykiss
brenda
Isorna, E.; El Mrabet, A.; Confente, F.; Falcon, J.; Munoz-Cueto, J.A.
Cloning and expression of arylalkylamine N-acetyltranferase-2 during early development and metamorphosis in the sole Solea senegalensis
Gen. Comp. Endocrinol.
161
97-102
2009
Solea senegalensis
brenda
Pavlicek, J.; Coon, S.L.; Ganguly, S.; Weller, J.L.; Hassan, S.A.; Sackett, D.L.; Klein, D.C.
Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87)
J. Biol. Chem.
283
14552-14558
2008
Ovis aries (Q29495)
brenda
Suzuki, T.; Takashima, T.; Izawa, N.; Watanabe, M.; Takeda, M.
UV radiation elevates arylalkylamine N-acetyltransferase activity and melatonin content in the two-spotted spider mite, Tetranychus urticae
J. Insect Physiol.
54
1168-1174
2008
Tetranychus urticae
brenda
Okazaki, M.; Higuchi, K.; Hanawa, Y.; Shiraiwa, Y.; Ezura, H.
Cloning and characterization of a Chlamydomonas reinhardtii cDNA arylalkylamine N-acetyltransferase and its use in the genetic engineering of melatonin content in the Micro-Tom tomato
J. Pineal Res.
46
373-382
2009
Chlamydomonas reinhardtii
brenda
Bloemeke, B.; Golka, K.; Griefahn, B.; Roemer, H.C.
Arylalkylamine N-acetyltransferase (AANAT) genotype as a personal trait in melatonin synthesis
J. Toxicol. Environ. Health
71
874-876
2008
Homo sapiens
brenda
Gupta, B.B.; Yanthan, L.; Singh, K.M.
In vitro effects of 5-hydroxytryptophan, indoleamines and leptin on arylalkylamine N-acetyltransferase (AA-NAT) activity in pineal organ of the fish, Clarias gariepinus (Burchell, 1822) during different phases of the breeding cycle
Indian J. Exp. Biol.
48
786-792
2010
Clarias gariepinus
brenda
Mehere, P.; Han, Q.; Christensen, B.M.; Li, J.
Identification and characterization of two arylalkylamine N-acetyltransferases in the yellow fever mosquito, Aedes aegypti
Insect Biochem. Mol. Biol.
41
707-714
2011
Aedes aegypti
brenda
Dai, F.Y.; Qiao, L.; Tong, X.L.; Cao, C.; Chen, P.; Chen, J.; Lu, C.; Xiang, Z.H.
Mutations of an arylalkylamine-N-acetyltransferase, Bm-iAANAT, are responsible for silkworm melanism mutant
J. Biol. Chem.
285
19553-19560
2010
Bombyx mori (A0EM56), Bombyx mori (D6MKR1), Bombyx mori (D6MKR2), Bombyx mori
brenda
Kang, K.; Lee, K.; Park, S.; Kim, Y.S.; Back, K.
Enhanced production of melatonin by ectopic overexpression of human serotonin N-acetyltransferase plays a role in cold resistance in transgenic rice seedlings
J. Pineal Res.
49
176-182
2010
Homo sapiens
brenda
Migliori, M.L.; Romanowski, A.; Simonetta, S.H.; Valdez, D.; Guido, M.; Golombek, D.A.
Daily variation in melatonin synthesis and arylalkylamine N-acetyltransferase activity in the nematode Caenorhabditis elegans
J. Pineal Res.
53
38-46
2012
Caenorhabditis elegans (G5EDH7), Caenorhabditis elegans, Caenorhabditis elegans TJ1060 (G5EDH7)
brenda
Cazamea-Catalan, D.; Magnanou, E.; Helland, R.; Vanegas, G.; Besseau, L.; Boeuf, G.; Paulin, C.H.; Joergensen, E.H.; Falcon, J.
Functional diversity of Teleost arylalkylamine N-acetyltransferase-2: is the timezyme evolution driven by habitat temperature?
Mol. Ecol.
21
5027-5041
2012
Danio rerio, Esox lucius, Oncorhynchus mykiss, Thunnus thynnus, Salvelinus alpinus, Arctogadus glacialis, Oxydoras sifontesi
brenda
Han, Q.; Robinson, H.; Ding, H.; Christensen, B.M.; Li, J.
Evolution of insect arylalkylamine N-acetyltransferases: structural evidence from the yellow fever mosquito, Aedes aegypti
Proc. Natl. Acad. Sci. USA
109
11669-11674
2012
Aedes aegypti (Q16KL9), Aedes aegypti
brenda
Long, Y.; Li, J.; Zhao, T.; Li, G.; Zhu, Y.
A new arylalkylamine N-acetyltransferase in silkworm (Bombyx mori) affects integument pigmentation
Appl. Biochem. Biotechnol.
175
3447-3457
2015
Bombyx mori (A0A0F6PL61), Bombyx mori
brenda
Dempsey, D.R.; Jeffries, K.A.; Bond, J.D.; Carpenter, A.M.; Rodriguez-Ospina, S.; Breydo, L.; Caswell, K.K.; Merkler, D.J.
Mechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases
Biochemistry
53
7777-7793
2014
Drosophila melanogaster
brenda
Prashant, K.; Kumar, H.; Prasad, C.V.
In-silico study of arylalkylamine-nacetyltransferase enzyme to regulate circadian rhythmicity
Bioinformation
9
771-776
2013
Homo sapiens (Q16613), Homo sapiens
brenda
Leng, P.Q.; Zhao, F.L.; Yin, B.C.; Ye, B.C.
A novel, colorimetric method for biogenic amine detection based on arylalkylamine N-acetyltransferase
Chem. Commun. (Camb. )
51
8712-8714
2015
Aedes aegypti
brenda
Tsugehara, T.; Imai, T.; Takeda, M.
Characterization of arylalkylamine N-acetyltransferase from silkmoth (Antheraea pernyi) and pesticidal drug design based on the baculovirus-expressed enzyme
Comp. Biochem. Physiol. C
157
93-102
2013
Antheraea pernyi (A2SZ52), Antheraea pernyi
brenda
Dempsey, D.R.; Jeffries, K.A.; Anderson, R.L.; Carpenter, A.M.; Rodriquez Opsina, S.; Merkler, D.J.
Identification of an arylalkylamine N-acyltransferase from Drosophila melanogaster that catalyzes the formation of long-chain N-acylserotonins
FEBS Lett.
588
594-599
2014
Drosophila melanogaster (Q9VMG0)
brenda
Byeon, Y.; Yool Lee, H.; Choi, D.W.; Back, K.
Chloroplast-encoded serotonin N-acetyltransferase in the red alga Pyropia yezoensis: gene transition to the nucleus from chloroplasts
J. Exp. Bot.
66
709-717
2015
Neopyropia yezoensis
brenda
Paulin, C.H.; Cazamea-Catalan, D.; Zilberman-Peled, B.; Herrera-Perez, P.; Sauzet, S.; Magnanou, E.; Fuentes, M.; Gothilf, Y.; Munoz-Cueto, J.A.; Falcon, J.; Besseau, L.
Subfunctionalization of arylalkylamine N-acetyltransferases in the sea bass Dicentrarchus labrax: two-ones for one two
J. Pineal Res.
59
354-364
2015
Dicentrarchus labrax (A0A0K1H4R1), Dicentrarchus labrax (B9TU30), Dicentrarchus labrax (B9TU31), Dicentrarchus labrax
brenda
Lee, H.R.; Kim, T.D.; Kim, H.J.; Jung, Y.; Lee, D.; Lee, K.H.; Kim, D.Y.; Woo, K.C.; Kim, K.T.
Heterogeneous ribonucleoprotein R regulates arylalkylamine N-acetyltransferase synthesis via internal ribosomal entry site-mediated translation in a circadian manner
J. Pineal Res.
59
518-529
2015
Rattus norvegicus (Q64666)
brenda
Ahn, J.H.; Park, J.H.; Kim, I.H.; Lee, J.C.; Yan, B.C.; Yong, M.S.; Lee, C.H.; CHoi, J.H.; Yoo, K.Y.; Hwang, I.K.; Moon, S.M.; Shin, H.C.; Won, M.H.
Comparison of arylalkylamine N-acetyltransferase and melatonin receptor type 1B immunoreactivity between young adult and aged canine spinal cord
J. Vet. Sci.
15
335-342
2014
Canis lupus familiaris
brenda
Nisembaum, L.G.; Tinoco, A.B.; Moure, A.L.; Alonso Gomez, A.L.; Delgado, M.J.; Valenciano, A.I.
The arylalkylamine-N-acetyltransferase (AANAT) acetylates dopamine in the digestive tract of goldfish: a role in intestinal motility
Neurochem. Int.
62
873-880
2013
Carassius auratus (G1CSA9), Carassius auratus
brenda
Byeon, Y.; Back, K.
Melatonin production in Escherichia coli by dual expression of serotonin N-acetyltransferase and caffeic acid O-methyltransferase
Appl. Microbiol. Biotechnol.
100
6683-6691
2016
Ovis aries (Q29495)
brenda
Shin, S.; Choe, J.
Crystal structure of Pseudomonas aeruginosa N-acetyltransferase PA4534
Biochem. Biophys. Res. Commun.
487
236-240
2017
Pseudomonas aeruginosa (Q9HVP3), Pseudomonas aeruginosa DSM 22644 (Q9HVP3)
brenda
Premabati, Y.; Singh, K.; Gupta, B.
Inverse relationship between diurnal rhythms in plasma levels of thyroid hormones and pineal arylalkylamine-N-acetyltransferase (AANAT) activity in an air-breathing fish, Clarias gariepinus
Biol. Rhythm. Res.
49
201-214
2018
Clarias gariepinus
-
brenda
Aboalroub, A.A.; Zhang, Z.; Keramisanou, D.; Gelis, I.
Backbone resonance assignment of an insect arylalkylamine N-acetyltransferase from Bombyx mori reveals conformational heterogeneity
Biomol. NMR Assign.
11
105-109
2017
Bombyx mori
brenda
Hwang, O.J.; Back, K.
Hwang, O.; Back, K. Simultaneous suppression of two distinct serotonin N-Acetyltransferase isogenes by RNA interference leads to severe decreases in melatonin and accelerated seed deterioration in rice
Biomolecules
10
141
2020
Oryza sativa Japonica Group (Q5KQI6), Oryza sativa Japonica Group (Q6Z1Y6)
brenda
Lee, H.; Lee, K.; Back, K.
Knockout of Arabidopsis serotonin N-acetyltransferase-2 reduces melatonin levels and delays flowering
Biomolecules
9
712
2019
Arabidopsis thaliana
brenda
Noh, M.Y.; Koo, B.; Kramer, K.J.; Muthukrishnan, S.; Arakane, Y.
Arylalkylamine N-acetyltransferase 1 gene (TcAANAT1) is required for cuticle morphology and pigmentation of the adult red flour beetle, Tribolium castaneum
Insect Biochem. Mol. Biol.
79
119-129
2016
Tribolium castaneum (A0A1J0AHX8), Tribolium castaneum
brenda
Alkozi, H.; de Lara, M.; Sanchez-Naves, J.; Pintor, J.
TRPV4 stimulation induced melatonin secretion by increasing arylalkymine N-acetyltransferase (AANAT) protein level
Int. J. Mol. Sci.
18
746
2017
Homo sapiens (Q16613), Homo sapiens
brenda
Wadas, B.; Borjigin, J.; Huang, Z.; Oh, J.H.; Hwang, C.S.; Varshavsky, A.
Degradation of serotonin N-acetyltransferase, a circadian regulator, by the N-end rule pathway
J. Biol. Chem.
291
17178-17196
2016
Homo sapiens (Q16613), Homo sapiens, Rattus norvegicus (Q64666)
brenda
Byeon, Y.; Lee, H.; Back, K.
Cloning and characterization of the serotonin N-acetyltransferase-2 gene (SNAT2) in rice (Oryza sativa)
J. Pineal Res.
61
198-207
2016
Oryza sativa (Q6Z1Y6)
brenda
Lee, K.; Back, K.
Overexpression of rice serotonin N-acetyltransferase 1 in transgenic rice plants confers resistance to cadmium and senescence and increases grain yield
J. Pineal Res.
62
e12392
2017
Oryza sativa Japonica Group (Q5KQI6)
brenda
Lee, K.; Hwang, O.J.; Reiter, R.J.; Back, K.
Flavonoids inhibit both rice and sheep serotonin N-acetyltransferases and reduce melatonin levels in plants
J. Pineal Res.
65
e12512
2018
Oryza sativa, Ovis aries (Q29495), Ovis aries
brenda
Aboalroub, A.A.; Bachman, A.B.; Zhang, Z.; Keramisanou, D.; Merkler, D.J.; Gelis, I.
Acetyl group coordinated progression through the catalytic cycle of an arylalkylamine N-acetyltransferase
PLoS ONE
12
e0177270
2017
Bombyx mori
brenda
Pan, Q.; Zhao, F.; Ye, B.
Eis, a novel family of arylalkylamine N-acetyltransferase (EC 2.3.1.87)
Sci. Rep.
8
2435
2018
Saccharopolyspora erythraea, Mycolicibacterium smegmatis (A0QY29), Mycolicibacterium smegmatis, Mycobacterium tuberculosis (P9WFK7), Mycobacterium tuberculosis, Mycolicibacterium smegmatis ATCC 700084 (A0QY29), Mycobacterium tuberculosis ATCC 25618 (P9WFK7)
brenda
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 
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