Literature summary extracted from

Varga, A.; Szabo, J.; Flachner, B.; Roy, B.; Konarev, P.; Svergun, D.; Zavodszky, P.; Perigaud, C.; Barman, T.; Lionne, C.; Vas, M.
Interaction of human 3-phosphoglycerate kinase with L-ADP, the mirror image of D-ADP (2008), Biochem. Biophys. Res. Commun., 366, 994-1000.

General Stability

EC Number	General Stability	Organism
2.7.2.3	L-MgADP binds to the specific adenosine-binding site and protects the conformation of hPGK molecule against heat denaturation	Homo sapiens

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.7.2.3	D-MgADP-	competitive inhibitor with respect to MgATP	Homo sapiens
2.7.2.3	L-MgADP-	competitive inhibitor with respect to MgATP	Homo sapiens

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.7.2.3	0.27	-	L-ADP	L-MgADP-	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.2.3	Homo sapiens	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.7.2.3	L-ADP + 3-phospho-D-glyceroyl phosphate	L-MgADP is almost as a good substrate for hPGK as the natural D-MgADP	Homo sapiens	ATP + 3-phospho-D-glycerate	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
2.7.2.3	hPGK	-	Homo sapiens

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
2.7.2.3	additional information	-	L-MgADP binds to the specific adenosine-binding site and protects the conformation of hPGK molecule against heat denaturation	Homo sapiens

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.7.2.3	685	-	L-ADP	L-MgADP-	Homo sapiens

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
2.7.2.3	0.035	-	D-MgADP-	-	Homo sapiens
2.7.2.3	0.063	-	L-MgADP-	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)