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Literature summary for 1.1.1.8 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.
    View publication on PubMed

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
isoforms Gdp1, Gut2
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae