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 properties.
The isomerization of 3-phospho-D-glycerate and 2-phospho-D-glycerate catalyzed by the cofactor-independent phosphoglycerate mutase from wheat germ (the isolation and crystallization of which is described in the Appendix) has been shown to be intramolecular by two methods. Mass-spectrometric analysis of the products from the isomerization of a mixture of 3-phospho-D-[2(-2)H]glycerate and 3-[18O]phospho-D-glycerate shows that there is no exchange of labeled phosphoryl group between carbon skeletons in the mutase-catalyzed reaction. Analysis of the products from the isomerization of a mixture of 3-phospho-D-[2(-2)H]glycerate and 3-[32p]phospho-D-glycerate by a method involving the kinetic discrimination between 2(-2)H and 2(-1)H species using the enolase isotope effect similarly shows that the wheat germ phosphoglycerate mutase mediates an intramolecular transfer of the phosphoryl group.
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013058:Mass Spectrometry; D008970:Molecular Weight; D010736:Phosphoglycerate Mutase / Q000302:isolation & purification / Q000378:metabolism*; D010751:Phosphopyruvate Hydratase; D010770:Phosphotransferases / Q000378:metabolism*; D011770:Pyruvate Kinase; D013438:Sulfhydryl Compounds / Q000032:analysis; D014908:Triticum
D013438:Sulfhydryl Compounds; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D011770:Pyruvate Kinase; D010751:Phosphopyruvate Hydratase; D010736:Phosphoglycerate Mutase