Thermitase
| Thermitase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.66 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
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
[edit]- ^ Mizusawa K, Yoshida F (November 1972). "Thermophilic Streptomyces alkaline proteinase. I. Isolation, crystallization, and physicochemical properties". The Journal of Biological Chemistry. 247 (21): 6978–84. PMID 5082135.
- ^ Borgia P, Campbell LL (December 1974). "Properties of two homologous alkaline proteases from Streptomyces rectus". Journal of Bacteriology. 120 (3): 1109–15. PMC 245889. PMID 4373436.
- ^ Kleine R (1982). "Properties of thermitase, a thermostable serine protease from Thermoactinomyces vulgaris". Acta Biologica et Medica Germanica. 41 (1): 89–102. PMID 7051706.
- ^ Meloun B, Baudyš M, Kostka V, Hausdorf G, Frömmel C, Höhne WE (1985). "Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin-type proteinases". FEBS Lett. 183 (2): 195–200. doi:10.1016/0014-5793(85)80775-4.
- ^ Teplyakov AV, Kuranova IP, Harutyunyan EH, Vainshtein BK, Frömmel C, Höhne WE, Wilson KS (July 1990). "Crystal structure of thermitase at 1.4 A resolution". Journal of Molecular Biology. 214 (1): 261–79. doi:10.1016/0022-2836(90)90160-n. PMID 2196375.
External links
[edit]- Thermitase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
