Slow step after bond-breaking by porcine pepsin identified using solvent deuterium isotope effects
- 15 April 1991
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 176 (1) , 65-69
- https://doi.org/10.1016/0006-291x(91)90890-j
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Substrate specificity of recombinant human renal renin: effect of histidine in the P2 subsite of pH dependenceBiochemistry, 1990
- Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active siteBiochemistry, 1988
- Energetics and mechanism of proline racemaseBiochemistry, 1986
- Cryoenzymology of porcine pepsinBiochemistry, 1984
- Metabolic resistance to tight-binding inhibitors of enzymes involved in the de novo pyrimidine pathway Simulation of time-dependent effects. Simulation of time-dependent effectsEuropean Journal of Biochemistry, 1984
- Regression analysis of nonlinear Arrhenius plots: An empirical model and a computer programComputers in Biology and Medicine, 1984
- Rate-limiting step: a quantitative definition. Application to steady-state enzymic systemsBiochemistry, 1983
- The Expression of Isotope Effects on Enzyme-Catalyzed ReactionsAnnual Review of Biochemistry, 1981
- Catalytic mechanism of pepsin using a new synthetic substrateBiochemistry, 1972