PhosphoglyceRate kinase (EC 126.96.36.199) (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglyceRate (1,3-BPG) to ADP producing 3-phosphoglyceRate (3-PG) and ATP. Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-geneRating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, geneRating ADP and 1,3-BPG.
3-PGK, Native (Baker's Yeast (S. cerevisiae))
Baker's yeast (S. cerevisiae)
3-Phosphoglyceric Phosphokinase generates ATP by catalyzing the transfer of a phosphate group from 1,3-diphosphoglycerate to ADP. 3-Phosphoglycerate Phosphokinase is used to study glycolysis and gluconeogenesis. It has also been used to study low molecular weight GTP-binding proteins and mechanisms of inhibition of glyceraldehyde-3-phosphate dehydrogenase. The enzyme has been used in the assay of glyceraldehyde-3-phosphate dehydrogenase.
ammonium sulfate suspension
Enzyme Commission Number
> 1000 units/mg protein
One unit will convert 1.0 μmole of 1,3-diphosphoglycerate to 3-phosphoglycerate per min at pH 6.9 at 25°C.
PGK; 3-PGK; ATP-3-phospho-D-glyceRate-1-phosphotransferase; ATP:D-3-phosphoglyceRate 1-phosphotransferase; 3-phosphoglyceRate kinase; 3-phosphoglyceRate phosphokinase; 3-phosphoglyceric acid kinase; 3-phosphoglyceric acid phosphokinase; 3-phosphoglyceric kinase; glyceRate 3-phosphate kinase; glycerophosphate kinase; phosphoglyceric acid kinase; phosphoglyceric kinase; phosphoglycerokinase; EC 188.8.131.52