The binding of a non-specific ‘transition state analogue’ to α-chymotrypsin
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(75)81037-4/fullpdf
Reference19 articles.
1. Enzymatic Catalysis and Transition-State Theory
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3. Use of peptide aldehydes to generate transition-state analogs of elastase
4. Aldehydes as Inhibitors of Papain
5. Re-evaluation of the Inhibition Constants of Previously Investigated Competitive Inhibitors of α-Chymotrypsin. II. Mono-, Bi- and Trifunctional Inhibitors Evaluated under Zone A Conditions1
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1. Inhibition of bacterial cell division protein FtsZ by cinnamaldehyde;Biochemical Pharmacology;2007-09
2. Backbone amide linker (BAL) strategy forNα-9-fluorenylmethoxycarbonyl (Fmoc) solid-phase synthesis of peptide aldehydes;Journal of Peptide Science;2005
3. Inhibition of Oleamide Hydrolase Catalyzed Hydrolysis of the Endogenous Sleep-Inducing Lipid cis-9-Octadecenamide;Journal of the American Chemical Society;1996-01-01
4. Active and Inactive Forms of the Transition-state Analog Protease Inhibitor Leupeptin: Explanation of the Observed Slow Binding of Leupeptin to Cathepsin B and Papain;Journal of Biological Chemistry;1989-01
5. Mechanism of slow-binding inhibition of human leukocyte elastase by trifluoromethyl ketones;Biochemistry;1987-05-19
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