Aminomuconate-semialdehyde dehydrogenase
| aminomuconate-semialdehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 aminomuconate-semialdehyde dehydrogenase tetramer, Pseudomonas | |||||||||
| Identifiers | |||||||||
| EC no. | 1.2.1.32 | ||||||||
| CAS no. | 37250-95-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an aminomuconate-semialdehyde dehydrogenase (EC 1.2.1.32) is an enzyme that catalyzes the chemical reaction
- 2-aminomuconate 6-semialdehyde + NAD+ + H2O 2-aminomuconate + NADH + 2 H+
The 3 substrates of this enzyme are 2-aminomuconate 6-semialdehyde, NAD+, and H2O, whereas its 3 products are 2-aminomuconate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in 3 metabolic pathways: benzoic acid degradation via hydroxylation, tryptophan metabolism, and the degradation pathway for toluene and xylene.
Nomenclature
[edit]The systematic name of this enzyme class is 2-aminomuconate-6-semialdehyde:NAD+ 6-oxidoreductase. Other names in common use include 2-aminomuconate semialdehyde dehydrogenase, 2-hydroxymuconic acid semialdehyde dehydrogenase, 2-hydroxymuconate semialdehyde dehydrogenase, alpha-aminomuconic epsilon-semialdehyde dehydrogenase, alpha-hydroxymuconic epsilon-semialdehyde dehydrogenase, and 2-hydroxymuconic semialdehyde dehydrogenase.
References
[edit]Further reading
[edit]- Ichiyama A, Nakamura S, Kawai H, Honjo T, Nishizuka Y, Hayaishi O, Senoh S (February 1965). "Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues. II. enzymic formation of alpha-aminomuconic acid from 3-hydroxyanthranilic acid". The Journal of Biological Chemistry. 240: 740–9. PMID 14275130.
