ExplorEnz: EC 3.4.21.66

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3.4.21.66

Accepted name:

thermitase

Reaction:

Hydrolysis of proteins, including collagen

Other name(s):

thermophilic Streptomyces serine proteinase; Thermoactinomyces vulgaris serine proteinase

Comments:

A peptidase of family S8 (subtilisin family) from Thermoactinomyces vulgaris containing a single Cys, near the active site His, and inhibited by p-mercuribenzoate. The N-terminal extension of the polypeptide chain relative to subtilisin contributes to Ca²⁺-binding and the high thermostability. The amino acid composition and properties of the thermostable enzyme from Streptomyces rectus var. proteolyticus (formerly included in EC 3.4.21.14) are closely similar [1,2].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 69772-87-8

References:

1.	Mizusawa, K. and Yoshida, F. Thermophilic Streptomyces alkaline proteinase. J. Biol. Chem. 247 (1972) 6978–6984. [PMID: 4711613]
2.	Borgia, P. and Campbell, L. Properties of two homologous alkaline proteases from Streptomyces rectus. J. Bacteriol. 123 (1974) 1109–1115. [PMID: 4373436]
3.	Kleine, R. Properties of thermitase, a thermostable serine protease from Thermoactinomyces vulgaris. Acta Biol. Med. Ger. 41 (1982) 89–102. [PMID: 7051706]
4.	Meloun, B., Baudyš, M., Kostka, V., Hausdorf, G., Frömmel, C. and Höhne, W.E. Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin-type proteinases. FEBS Lett. 183 (1985) 195–200.
5.	Teplyakov, A.V., Kuranova, I.P., Harutyunyan, E.H., Vainshtein, B.K., Frömmel, C., Höhne, W.E. and Wilson, K.S. Crystal structure of thermitase at 1.4 Å resolution. J. Mol. Biol. 214 (1990) 261–279. [DOI] [PMID: 2196375]

[EC 3.4.21.66 created 1992]