Electrostatic Characterization of Enzyme Complexes: Evaluation of the Mechanism of Catalysis of Dihydrofolate Reductase
- 1 March 1997
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 119 (10) , 2386-2395
- https://doi.org/10.1021/ja962621r
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- 15N NMR studies of the conformation ofE. colidihydrofolate reductase in complex with folate or methotrexateFEBS Letters, 1991
- Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coliBiochemistry, 1991
- The kinetic mechanism of wild-type and mutant mouse dihydrofolate reductasesBiochemistry, 1990
- Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate .cntdot. NADP+ ternary complex. substrate binding and a model for the transition stateBiochemistry, 1990
- EPR and kinetic analysis of the interaction of halides and phosphate with nitrate reductaseBiochemistry, 1989
- Computational studies on pterins and speculations on the mechanism of action of dihydrofolate reductaseBiochemical and Biophysical Research Communications, 1989
- Mechanism of the reaction catalyzed by dihydrofolate reductase from Escherichia coli: pH and deuterium isotope effects with NADPH as the variable substrateBiochemistry, 1988
- Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coliBiochemistry, 1987
- Theoretical studies on the activation of the pterin cofactor in the catalytic mechanism of dihydrofolate reductaseBiochemistry, 1985
- Kinetics of substrate, coenzyme, and inhibitor binding to Escherichia coli dihydrofolate reductaseBiochemistry, 1981