Literature summary extracted from

Pahlman, I.L.; Larsson, C.; Averet, N.; Bunoust, O.; Boubekeur, S.; Gustafsson, L.; Rigoulet, M.
Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae (2002), J. Biol. Chem., 277, 27991-27995.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.1.1.8	34	-	glycerol-3-phosphate	isoform Gut2, pH 6.8	Saccharomyces cerevisiae

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.8	Saccharomyces cerevisiae	-	isoforms Gdp1, Gut2	-

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.1.1.8	2396	-	isoform Gut2, pH 6.8	Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.8	glycerol-3-phosphate + NAD+	-	Saccharomyces cerevisiae	glycerone phosphate + NADH	-	?

Subunits

EC Number	Subunits	Comment	Organism
1.1.1.8	More	kinetic interaction between NADH dehydrogenases Nde1/Nde2 and enzyme isoform Gut2 at inner mitochondrial membrane	Saccharomyces cerevisiae

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.1.1.8	NAD+	-	Saccharomyces cerevisiae
1.1.1.8	NADH	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)