Literature summary for 2.7.2.3 extracted from

Tougard, P.; Le, T.H.; Minard, P.; Desmadril, M.; Yon, J.M.; Bizebard, T.; Lebras, G.; Dumas, C.
Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala (1996), Protein Eng., 9, 181-187.

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Protein Variants

Protein Variants	Comment	Organism
R203P	three-dimensional structure analysis, kcat is reduced by 10-20%, mostly unaltered kinetic parameter, decreased stability compared to the wild-type	Saccharomyces cerevisiae
R206P	naturally occuring mutant variant phosphoglycerate kinase-Uppsala, associated with chronic nonspherocytic hemolytic anemia, structure study via comparison to constructed mutant analogue in yeast	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	mutant pathological variant phosphoglycerate kinase-Uppsala with R206P	-
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

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

Cofactor

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

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Release 2023.1 (January 2023)