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Thermitase

From Wikipedia, the free encyclopedia
Thermitase
Identifiers
EC no.3.4.21.66
CAS no.69772-87-8
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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

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  1. 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. doi:10.1016/S0021-9258(19)44682-6. PMID 5082135.
  2. Borgia P, Campbell LL (December 1974). "Properties of two homologous alkaline proteases from Streptomyces rectus". Journal of Bacteriology. 120 (3): 1109–15. doi:10.1128/jb.120.3.1109-1115.1974. PMC 245889. PMID 4373436.
  3. Kleine R (1982). "Properties of thermitase, a thermostable serine protease from Thermoactinomyces vulgaris". Acta Biologica et Medica Germanica. 41 (1): 89–102. PMID 7051706.
  4. 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. Bibcode:1985FEBSL.183..195M. doi:10.1016/0014-5793(85)80775-4.
  5. 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.
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