THE CHEMICAL MODIFICATION OF CHYMOTRYPSIN
- 1 June 1964
- journal article
- abstracts
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 42 (6) , 695-714
- https://doi.org/10.1139/o64-083
Abstract
Chemical modification of chymotrypsin has led to the identification of several amino acid side-chains which are probably constituents of the active site of the enzyme. A single seryl and a single histidyl residue appear to cooperate in catalyzing the bond-breaking process while one or more tryptophanyl residues may be involved in the specific binding of substrate. Neither of the two methionyl residues is essential for enzyme activity although changes in kinetic properties occur when they are modified by oxidation or alkylation.Keywords
This publication has 31 references indexed in Scilit:
- Partial structure of chymotrypsinogenBiochimica et Biophysica Acta, 1962
- Steric Course and Specificity of α-Chymotrypsin-catalyzed Reactions. IJournal of the American Chemical Society, 1962
- Identification of the methionine involved in the active center of chymotrypsinBiochemical and Biophysical Research Communications, 1962
- The Mechanism of α-Chymotrypsin-catalyzed Hydrolyses1-3Journal of the American Chemical Society, 1962
- The pH Dependence of Some α-Chymotrypsin-catalyzed Hydrolyses1-3Journal of the American Chemical Society, 1962
- MECHANISM OF ENZYME ACTIONAnnual Review of Biochemistry, 1960
- Reactivity of Nucleophilic Reagents toward EstersJournal of the American Chemical Society, 1960
- Isolation of acetyl peptides from acetylchymotrypsinBiochimica et Biophysica Acta, 1958
- The active centre of chymotrypsin II. Reaction with fluorodinitrobenzeBiochimica et Biophysica Acta, 1956
- Concerted Displacement Reactions. VIII. Polyfunctional Catalysis1Journal of the American Chemical Society, 1952