Streptogrisin A

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Streptogrisin A (EC 3.4.21.80, Streptomyces griseus protease A, protease A, proteinase A, Streptomyces griseus proteinase A, Streptomyces griseus serine proteinase 3, Streptomyces griseus serine proteinase A) is an enzyme. This enzyme catalyses the following chemical reaction

Hydrolysis of proteins with specificity similar to chymotrypsin

This enzyme is isolated from Streptomyces griseus.

References

Johnson P, Smillie LB (May 1971). "The disulfide bridge sequences of a serine protease of wide specificity from Streptomyces griseus". Canadian Journal of Biochemistry. 49 (5): 548–62. doi:10.1139/o71-082. PMID 5575653.
Sielecki AR, Hendrickson WA, Broughton CG, Delbaere LT, Brayer GD, James MN (November 1979). "Protein structure refinement: Streptomyces griseus serine protease A at 1.8 A resolution". Journal of Molecular Biology. 134 (4): 781–804. doi:10.1016/0022-2836(79)90486-8. PMID 119870.
James MN, Sielecki AR, Brayer GD, Delbaere LT, Bauer CA (November 1980). "Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 A resolution. A model for serine protease catalysis". Journal of Molecular Biology. 144 (1): 43–88. doi:10.1016/0022-2836(80)90214-4. PMID 6783761.
Delbaere LT, Brayer GD (May 1985). "The 1.8 A structure of the complex between chymostatin and Streptomyces griseus protease A. A model for serine protease catalytic tetrahedral intermediates". Journal of Molecular Biology. 183 (1): 89–103. doi:10.1016/0022-2836(85)90283-9. PMID 3892018.
Henderson G, Krygsman P, Liu CJ, Davey CC, Malek LT (August 1987). "Characterization and structure of genes for proteases A and B from Streptomyces griseus". Journal of Bacteriology. 169 (8): 3778–84. PMC 212465. PMID 3112129.

External links

Streptogrisin+A at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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Biology

Category:

EC 3.4.21