Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: hydrolyses of thiono and oxygen esters
- 4 January 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (1) , 117-122
- https://doi.org/10.1021/bi00270a017
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 9 references indexed in Scilit:
- Isolation of highly active papaya peptidases A and B from commercial chymopapainBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- Stereochemical aspects of peptide hydrolysis catalyzed by serine proteases of the chymotrypsin typeBioorganic Chemistry, 1981
- Computation of peptide-protein interactions. Catalysis by chymotrypsin: prediction of relative substrate reactivitiesJournal of the American Chemical Society, 1981
- Catalysis and leaving group binding in anilide hydrolysis by chymotrypsinBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- The question of differential hydrogen bonding in the mechanism of catalysis by serine proteasesBioorganic Chemistry, 1978
- ENHANCED CATALYTIC ACTIVITY OF PAPAIN TOWARDS AMIDE SUBSTRATES1977
- Binding of chloromethyl ketone substrate analogs to crystalline papainBiochemistry, 1976
- The Amino Acid Sequence around the Reactive Thiol Group of Chymopapain BJournal of Biological Chemistry, 1966
- DIRECT EVIDENCE FOR AN ACYLATED THIOL AS AN INTERMEDIATE IN PAPAIN- AND FICIN-CATALYSED HYDROLYSESBiochemical Journal, 1965