Reaction: Preferential cleavage of bonds with hydrophobic residues in P1'
Other names: pronase component; Streptomyces griseus neutral proteinase; actinase E; SGNPI
Comments: From Streptomyces griseus, S. naraensis, and S. cacaoi. Specificity similar to that of thermolysin, but much more sensitive to inhibition by mercaptoacetyl-Phe-Leu. Little structural similarity to other bacterial metalloendopeptidases. Type example of peptidase family M5.
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, CAS registry number: 153190-34-2
References:
1. Morihara, K., Tsuzuki, H. and Oka, T. Comparison of the specificities of various neutral proteinases from microorganisms. Arch. Biochem. Biophys. 123 (1968) 572-588. [PMID: 4967801]
2 Hiramatsu, A. and Ouchi, T. A neutral proteinase from Streptomyces naraensis. J. Biochem. (Tokyo) 71 (1972) 767-781. [PMID: 5073323]
3. Blumberg, S. and Tauber, Z. Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides. Eur. J. Biochem. 136 (1983) 151-154. [PMID: 6413206]
4. Chang, P.C., Kue, T-C., Tsugita, A. and Lee, Y.H.W. Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product. Gene 88 (1990) 87-95. [PMID: 2341042]