Transition State Charge Distribution in Reactions of an Acetyltyrosylchymotrypsin Intermediate
Open Access
- 1 August 1973
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 248 (16) , 5887-5891
- https://doi.org/10.1016/s0021-9258(19)43586-2
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Concerning a reported change in rate-determining step in chymotrypsin catalysisJournal of the American Chemical Society, 1973
- One-proton catalysis in the deacetylation of acetyl-a-chymotrypsinJournal of the American Chemical Society, 1973
- Nitrogen isotope effects on the chymotrypsin-catalyzed hydrolysis of N-acetyl-L-tryptophanamideJournal of the American Chemical Society, 1972
- Chymotrypsin catalysis. Evidence for a new intermediate. IIJournal of the American Chemical Society, 1972
- Mechanism of the .alpha.-chymotrypsin-catalyzed hydrolysis of amides. pH dependence of kc and km. kinetic detection of an intermediateJournal of the American Chemical Society, 1971
- Free energies of acetyl transfer from ring-substituted acetanilidesJournal of the American Chemical Society, 1971
- Specificity of α‐chymotrypsin. Dipeptide substratesFEBS Letters, 1970
- Chymotrypsin catalysis. Evidence for a new intermediateJournal of the American Chemical Society, 1969
- The Kinetics of the α-Chymotrypsin Catalyzed Hydrolysis of Acetyl-L-tyrosinhydroxamide in Aqueous Solutions at 25° and pH 7.61Journal of the American Chemical Society, 1953
- The Kinetics of the α-Chymotrypsin Catalyzed Hydrolysis of Acetyl-L-tyrosinamide in Aqueous Solutions at 25° and pH 7.8-8.01Journal of the American Chemical Society, 1951