Thermitase
Thermitase | |||||||||
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Identifiers | |||||||||
EC number | 3.4.21.66 | ||||||||
CAS number | 69772-87-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Thermitase (EC 3.4.21.66, thermophilic Streptomyces serine proteinase, Thermoactinomyces vulgaris serine proteinase) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Hydrolysis of proteins, including collagen
This peptidase is isolated from Thermoactinomyces vulgaris.
References
- ↑ Mizusawa, K.; Yoshida, F. (1972). "Thermophilic Streptomyces alkaline proteinase". J. Biol. Chem. 247: 6978–6984. PMID 5082135.
- ↑ Borgia, P.; Campbell, L. (1974). "Properties of two homologous alkaline proteases from Streptomyces rectus". J. Bacteriol. 123: 1109–1115. PMID 4373436.
- ↑ Kleine, R. (1982). "Properties of thermitase, a thermostable serine protease from Thermoactinomyces vulgaris". Acta Biol. Med. Ger. 41: 89–102. PMID 7051706.
- ↑ Meloun, B.; Baudyš, M.; Kostka, V.; Hausdorf, G.; Frömmel, C.; Höhne, W.E. (1985). "Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin-type proteinases". FEBS Lett. 183: 195–200. doi:10.1016/0014-5793(85)80775-4.
- ↑ Teplyakov, A.V.; Kuranova, I.P.; Harutyunyan, E.H.; Vainshtein, B.K.; Frömmel, C.; Höhne, W.E.; Wilson, K.S. (1990). "Crystal structure of thermitase at 1.4 Å resolution". J. Mol. Biol. 214: 261–279. doi:10.1016/0022-2836(90)90160-n. PMID 2196375.
External links
- Thermitase at the US National Library of Medicine Medical Subject Headings (MeSH)
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