Mycolysin

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
Search PMC articles PubMed articles NCBI proteins

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

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.

External links

• Mycolysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)