Active Centers of alpha-Chymotrypsin and of Streptomyces griseus Proteases 1 and 3. S2-P2 Enzyme-Substrate Interactions
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1980.tb04533.x/fullpdf
Reference33 articles.
1. The Disulfide Bridge Sequences of a Serine Protease of Wide Specificity from Streptomyces griseus
2. The active centers of Streptomyces griseus protease 3 and α-chymotrypsin: enzyme-substrate interactions remote from the scissile bond
3. Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases
4. Molecular structure of crystalline Streptomyces griseus protease A at 2.8 å resolution
5. Active centers of Streptomyces griseus protease 1, Streptomyces griseus protease 3, and α-chymotrypsin: enzyme-substrate interactions
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1. Streptogrisin B;Handbook of Proteolytic Enzymes;2013
2. Determination of the cleavage specificity of Streptomyces griseus protease B in the presence of guanidinium chloride;International Journal of Peptide and Protein Research;2009-01-12
3. Investigation of the Substrate-Binding Site of Trypsin by the Aid of Tripeptidyl-p-nitroanilide Substrates;European Journal of Biochemistry;2005-03-03
4. Active-site variants of Streptomyces griseus protease B with peptide-ligation activity;Chemistry & Biology;2000-03
5. Streptogrisin B;Enzyme Handbook 15;1998
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