Mycolysin
| Mycolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.31 | ||||||||
| CAS number | 153190-34-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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
- ↑ Morihara, K.; Tsuzuki, H.; Oka, T. (1968). "Comparison of the specificities of various neutral proteinases from microorganisms". Arch. Biochem. Biophys. 123: 572–588. PMID 4967801. doi:10.1016/0003-9861(68)90179-3.
- ↑ Hiramatsu, A.; Ouchi, T. (1972). "A neutral proteinase from Streptomyces naraensis". J. Biochem. (Tokyo). 71: 767–781. PMID 5073323.
- ↑ Blumberg, S.; Tauber, Z. (1983). "Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides". Eur. J. Biochem. 136: 151–154. PMID 6413206. doi:10.1111/j.1432-1033.1983.tb07719.x.
- ↑ Chang, P.C.; Kue, T-C.; Tsugita, A.; Lee, Y.H.W. (1990). "Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product". Gene. 88: 87–95. PMID 2341042. doi:10.1016/0378-1119(90)90063-w.
External links
- Mycolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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