Biology:Thermitase
From HandWiki
| 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
- ↑ "Thermophilic Streptomyces alkaline proteinase. I. Isolation, crystallization, and physicochemical properties". The Journal of Biological Chemistry 247 (21): 6978–84. November 1972. PMID 5082135. http://www.jbc.org/content/247/21/6978.long.
- ↑ "Properties of two homologous alkaline proteases from Streptomyces rectus". Journal of Bacteriology 120 (3): 1109–15. December 1974. PMID 4373436.
- ↑ "Properties of thermitase, a thermostable serine protease from Thermoactinomyces vulgaris". Acta Biologica et Medica Germanica 41 (1): 89–102. 1982. PMID 7051706.
- ↑ "Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin-type proteinases". FEBS Lett. 183 (2): 195–200. 1985. doi:10.1016/0014-5793(85)80775-4.
- ↑ "Crystal structure of thermitase at 1.4 A resolution". Journal of Molecular Biology 214 (1): 261–79. July 1990. 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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