Transient kinetic and deuterium isotope effect studies on the catalytic mechanism of phosphoglycerate dehydrogenase.
Open Access
- 1 March 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (5) , 1539-1551
- https://doi.org/10.1016/s0021-9258(17)40584-9
Abstract
No abstract availableThis publication has 33 references indexed in Scilit:
- Divalent cation and pH-dependent primary isotope effects in the enolase reactionBiochemistry, 1973
- Approaches to the study of enzyme mechanisms lactate dehydrogenaseFEBS Letters, 1973
- Reaction Mechanism of l‐Glutamate DehydrogenaseEuropean Journal of Biochemistry, 1972
- Transients and Relaxation Kinetics of Enzyme ReactionsAnnual Review of Biochemistry, 1971
- Transients in the reactions of liver alcohol dehydrogenaseBiochemistry, 1970
- Rates of binding of reduced nicotinamide adenine dinucleotide analogs to liver alcohol dehydrogenaseBiochemistry, 1969
- Factors controlling the Interconversion of Enzyme–Substrate Compounds of Pig Heart Lactate DehydrogenaseNature, 1968
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- Inhibition of dehydrogenase reactions by a substance formed from reduced diphosphopyridine nucleotideBiochimica et Biophysica Acta, 1961
- The Synthesis and Properties of Hydroxypyruvic Acid PhosphateJournal of the American Chemical Society, 1956