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Link to original content: http://en.wikipedia.org/wiki/Mycolysin
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Mycolysin

From Wikipedia, the free encyclopedia
Mycolysin
Identifiers
EC no.3.4.24.31
CAS no.153190-34-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

Mycolysin (EC 3.4.24.31, pronase component, Streptomyces griseus neutral proteinase, actinase E, SGNPI) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Preferential cleavage of bonds with hydrophobic residues in P1'

This enzyme is present in Streptomyces griseus, S. naraensis, and S. cacaoi.

References

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  1. ^ Morihara K, Tsuzuki H, Oka T (March 1968). "Comparison of the specificities of various neutral proteinases from microorganisms". Archives of Biochemistry and Biophysics. 123 (3): 572–88. doi:10.1016/0003-9861(68)90179-3. PMID 4967801.
  2. ^ Hiramatsu A, Ouchi T (May 1972). "A neutral proteinase from Streptomyces naraensis. 3. An improved purification and some physiochemical properties". Journal of Biochemistry. 71 (5): 767–81. PMID 5073323.
  3. ^ Blumberg S, Tauber Z (October 1983). "Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides". European Journal of Biochemistry. 136 (1): 151–4. doi:10.1111/j.1432-1033.1983.tb07719.x. PMID 6413206.
  4. ^ Chang PC, Kuo TC, Tsugita A, Lee YH (March 1990). "Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product". Gene. 88 (1): 87–95. doi:10.1016/0378-1119(90)90063-w. PMID 2341042.
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