| EC |
3.4.24.31 |
| Accepted name: |
mycolysin |
| Reaction: |
Preferential cleavage of bonds with hydrophobic residues in P1′ |
| Other name(s): |
pronase component; Streptomyces griseus neutral proteinase; actinase E; SGNPI |
| Comments: |
The enzyme has been characterized from the bacteria Streptomyces griseus, Streptomyces naraensis, and Streptomyces cacaoi. Specificity is similar to that of thermolysin, but the enzyme is much more sensitive to inhibition by sulfanylacetyl-Phe-Leu. Little structural similarity to other bacterial metalloendopeptidases. Type example of peptidase family M5. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 2341042] |
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| [EC 3.4.24.31 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.31] |
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