Literature summary for 2.7.2.3 extracted from

Ritco-Vonsovici, M.; Mouratou, B.; Minard, P.; Desmadril, M.; Yon, J.M.; Andrieux, M.; Leroy, E.; Guittet, E.
Role of the C-terminal helix in the folding and stability of yeast phosphoglycerate kinase (1995), Biochemistry, 34, 833-841.

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Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a deletion mutant lacking the 12 C-terminal amino acid residues, which normally form a C-terminal helix, mutant folds in a conformation similar to the wild-type, but exhibits 0.1% remaining activity compared to wild-type, addition of the missing peptide leads to 40fold increased activity	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate	C-terminal part is important for full activity	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

Cofactor

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

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Release 2023.1 (January 2023)