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Literature summary extracted from

  • Watson, H.C.; Bryant, T.N.; Walker, N.P.C.; Shaw, P.J.; Wendell, P.L.
    The active site of yeast phosphoglycerate kinase (1977), Biochem. Soc. Trans., 5, 652-654.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.3 divalent cation
-
 Equus caballus
2.7.2.3 divalent cation Mg2+ or Mn2+ Saccharomyces cerevisiae
2.7.2.3 Mg2+
-
 Saccharomyces cerevisiae
2.7.2.3 Mg2+
-
 Equus caballus
2.7.2.3 Mn2+ can partially replace Mg2+ in activation Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.3 Equus caballus
-
-
-
2.7.2.3 Saccharomyces cerevisiae
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.2.3 ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate active site structure containing 2 tryptophan residues, substrate binding Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.3 ATP + 3-phospho-D-glycerate
-
 Saccharomyces cerevisiae ADP + 1,3-diphosphoglycerate
-
 r
2.7.2.3 ATP + 3-phospho-D-glycerate
-
 Equus caballus ADP + 1,3-diphosphoglycerate
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.2.3 ADP
-
 Saccharomyces cerevisiae
2.7.2.3 ADP
-
 Equus caballus
2.7.2.3 ATP required as phosphate donor Saccharomyces cerevisiae
2.7.2.3 ATP required as phosphate donor Equus caballus