Literature summary for 2.7.2.3 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.

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Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Equus caballus	-	-	-
Saccharomyces cerevisiae	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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)

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

Cofactor

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

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Release 2023.1 (January 2023)