Streptogrisin B

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Streptogrisin B (EC 3.4.21.81, Streptomyces griseus protease B, pronase B, serine proteinase B, Streptomyces griseus proteinase B, Streptomyces griseus proteinase 1, Streptomyces griseus serine proteinase B) is an enzyme.^[1]^[2]^[3]^[4]^[5] This enzyme catalyses the following chemical reaction

Hydrolysis of proteins with trypsin-like specificity

This enzyme is isolated from Streptomyces griseus.

References

↑ Jurasek, L., Fackre, D. and Smillie, L.B. (1969). "Remarkable homology about the disulfide bridges of a trypsin-like enzyme from Streptomyces griseus". Biochem. Biophys. Res. Commun. 37: 99–105. doi:10.1016/0006-291x(69)90885-7. PMID 4899581.
↑ Fujinaga, M., Read, R.J., Sielecki, A., Ardelt, W., Laskowski, M., Jr. and James, M.N.G. (1982). "Refined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey". Proc. Natl. Acad. Sci. USA 79: 4868–4872. doi:10.1073/pnas.79.16.4868. PMID 6750612.
↑ Read, R.J., Fujinaga, M., Sielecki, A.R. and James, M.N.G. (1983). "Structure of the complex of Streptomyces griseus protease B and the third domain of turkey ovomucoid inhibitor at 1.8-Å resolution". Biochemistry 22: 4420–4433. doi:10.1021/bi00288a012. PMID 6414511.
↑ Henderson, G., Krygsman, P., Liu, C.J., Davey, C.C. and Malek, L.T. (1987). "Characterization and structure of genes for proteases A and B from Streptomyces griseus". J. Bacteriol. 169: 3778–3784. PMID 3112129.
↑ Greenblatt, H.M., Ryan, C.A. and James, M.N.G. (1989). "Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 Å resolution". J. Mol. Biol. 205: 201–228. doi:10.1016/0022-2836(89)90376-8. PMID 2494344.

External links

Streptogrisin B at the US National Library of Medicine Medical Subject Headings (MeSH)

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 Streptokinase S1P Cathepsin A G

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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