The basic difference in catalyses by serine and cysteine proteinases resides in charge stabilization in the transition state
- 1 August 1986
- journal article
- research article
- Published by Elsevier in Journal of Theoretical Biology
- Vol. 121 (3), 323-326
- https://doi.org/10.1016/s0022-5193(86)80111-4
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Genetic engineering: Better enzymes by designNature, 1985
- Mechanism of action of cysteine proteinases: oxyanion binding site is not essential in the hydrolysis of specific substratesBiochemistry, 1985
- Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: hydrolyses of thiono and oxygen estersBiochemistry, 1983
- Determination of a low pK for histidine-159 in the S-methylthio derivative of papain by proton nuclear magnetic resonance spectroscopyBiochemistry, 1981
- Structure of actinidin, after refinement at 1.7 Å resolutionJournal of Molecular Biology, 1980
- Is the thiolate-imidazolium ion pair the catalytically important form of papain?FEBS Letters, 1980
- The α-helix dipole and the properties of proteinsNature, 1978
- Serine Proteases: Structure and Mechanism of CatalysisAnnual Review of Biochemistry, 1977
- Binding of chloromethyl ketone substrate analogs to crystalline papainBiochemistry, 1976
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969