Effect of secondary interaction on the enzymatic activity of subtilisin BPN′: Comparison with α-chymotrypsin, trypsin, and elastase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(73)80157-7/fullpdf
Reference14 articles.
1. Substrate binding site in bovine chymotrypsin Aγ. Crystallographic study using peptide chloromethyl ketones as site-specific inhibitors
2. X-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPN
3. A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsin
4. Comparison of α-chymotrypsin and subtilisin BPN1: Size and specificity of the active site
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