KEGG   ENZYME: 3.4.24.31Help
Entry
EC 3.4.24.31                Enzyme                                 

Name
mycolysin;
pronase component;
Streptomyces griseus neutral proteinase;
actinase E;
SGNPI
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage of bonds with hydrophobic residues in P1'
Comment
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. Formerly included in EC 3.4.24.4
History
EC 3.4.24.31 created 1972 as EC 3.4.24.4, part transferred 1992 to EC 3.4.24.31
Reference
1  [PMID:4967801]
  Authors
Morihara K, Tsuzuki H, Oka T.
  Title
Comparison of the specificities of various neutral proteinases from microorganisms.
  Journal
Arch. Biochem. Biophys. 123 (1968) 572-88.
Reference
2  [PMID:5073323]
  Authors
Hiramatsu A, Ouchi T.
  Title
A neutral proteinase from Streptomyces naraensis. 3. An improved purification and some physiochemical properties.
  Journal
J. Biochem. (Tokyo). 71 (1972) 767-81.
Reference
3  [PMID:6413206]
  Authors
Blumberg S, Tauber Z.
  Title
Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides.
  Journal
Eur. J. Biochem. 136 (1983) 151-4.
Reference
4  [PMID:2341042]
  Authors
Chang PC, Kuo TC, Tsugita A, Lee YH.
  Title
Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product.
  Journal
Gene. 88 (1990) 87-95.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
153190-34-2

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