Mechanism of association of a specific aldehyde "transition-state analog" to the active site of .alpha.-chymotrypsin
- 23 January 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (2), 349-356
- https://doi.org/10.1021/bi00569a019
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- On the mechanism of action of methyl chymotrypsinBioorganic Chemistry, 1978
- Expression of functionality of alpha-chymotrypsin. An alternate binding mode in the substrate specificity siteJournal of Biological Chemistry, 1978
- Re-examination of the charge relay system in subtilisin comparison with other serine proteases.Journal of Biological Chemistry, 1977
- Thiohemiacetal formation by inhibitory aldehydes at the active site of papainBiochemistry, 1977
- Thermodynamics of binding to native α-chymotrypsin and to forms of α-chymotrypsin in which catalytically essential residues are modified; a study of "productive" and "nonproductive" associationsBiochemistry, 1977
- Binding rates, oxygen-sulfur substitution effects, and the pH dependence of chymotrypsin reactionsBiochemistry, 1977
- NMR evidence against covalent attachment of an aldehyde ‘transition-state’ analogue to α-chymotrypsinBiochemical and Biophysical Research Communications, 1976
- The binding of inhibitors to α-chymotrypsinBiochemical Journal, 1966
- The Reversible Hydration of Carbonyl CompoundsPublished by Elsevier ,1966
- The Mode of Action of the Crystalline Pancreatic Proteolytic Enzymes.Chemical Reviews, 1950