Phosphoglycerate mutases: stereochemical course of the phosphoryl group transfers catalyzed by the cofactor-dependent enzyme from rabbit muscle and the cofactor-independent enzyme from wheat germ
- 19 February 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 19 (4), 738-743
- https://doi.org/10.1021/bi00545a020
Abstract
2-[(R)-16O,17O,18O]Phospho-D-glycerate was synthesized and used to determine the stereochemical course of each of the 2 mechanistic classes of phosphoglycerate mutases. The enzyme from rabbit muscle requires 2,3-bis-phospho-D-glycerate as a cofactor and catalyzes an intermolecular phosphoryl group transfer reaction. The enzyme from wheat germ requires no cofactor and catalyzes an intramolecular transfer of the phosphoryl group. The reaction catalyzed by each of these enzymes proceeds with overall retention of the configuration at phosphorus. This stereochemical result is consistent with a double-displacement pathway involving a single phosphorylenzyme, for each of the catalyzed reactions.This publication has 8 references indexed in Scilit:
- Stereochemical course of phosphokinases. The use of adenosine [.gamma.-(S)-16O,17O,18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinaseBiochemistry, 1979
- Active site phosphohistidine peptides from red cell bisphosphoglycerate synthase and yeast phosphoglycerate mutase.Journal of Biological Chemistry, 1979
- Chiral[16O, 17O, 18O]phosphate monoesters. Asymmetric synthesis and stereochemical analysis of [1(R)-16O, 17O, 18O]phospho-(S)-propane-1,2-diolJournal of the American Chemical Society, 1979
- Phosphoglycerate mutase. Kinetics and effects of salts on the mutase and bisphosphoglycerate phosphatase activities of the enzyme from chicken breast muscle.Journal of Biological Chemistry, 1978
- Adenosine 5'-O-([gamma-18O]gamma-thio)triphosphate chiral at the gamma-phosphorus: stereochemical consequences of reactions catalyzed by pyruvate kinase, glycerol kinase, and hexokinase.Proceedings of the National Academy of Sciences, 1978
- Phosphoglycerate mutase from wheat germ: studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular. Appendix: Phosphoglycerate mutase from wheat germ: isolation, crystallization, and propertiesBiochemistry, 1977
- Phosphoglycerate mutase from wheat germ: studies with oxygen-18-labeled substrate, investigations of the phosphatase and phosphoryl transfer activities, and evidence for a phosphoryl-enzyme intermediateBiochemistry, 1977
- Rates of phosphorylation and dephosphorylation of phosphoglycerate mutase and bisphosphoglycerate synthase.Journal of Biological Chemistry, 1976