The Enzyme Database

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EC 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, 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. [PMID: 2196375]
[EC 3.4.21.66 created 1992]
 
 


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