Mycolysin
From Wikipedia the free encyclopedia
| Mycolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.31 | ||||||||
| CAS no. | 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[edit]
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
External links[edit]
- Mycolysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
