Literature summary for 2.7.2.3 extracted from

Hurth, C.; Tassius, C.; Talbot, J.C.; Maali, A.; Moskalenko, C.; Minard, P.; Aime, J.P.; Argoul, F.
Enzymatic activity of immobilized yeast phosphoglycerate kinase (2007), Biosens. Bioelectron., 22, 2449-2455.

Search for more literature for 2.7.2.3

Application

Application	Comment	Organism
additional information	immobilizing PGK on solid supports like glass or muscovite mica does not strongly modify its enzymatic activity, guideline for biosensors made with the method of Tapping Mode atomic force microscopy whenever a rapid assessment of the remaining surface activity is needed	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.1	-	ADP	enzymatic activity of immobilized PGK on glass	Saccharomyces cerevisiae
0.18	-	ADP	enzymatic activity in bulk condition	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P00560	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + 3-phospho-D-glyceroyl phosphate	-	Saccharomyces cerevisiae	ATP + 3-phospho-D-glycerate	-	?

Synonyms

Synonyms	Comment	Organism
PGK	-	Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
963.1	-	ADP	enzymatic activity in bulk condition	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)