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Literature summary for 1.1.99.40 extracted from

  • Becker-Kettern, J.; Paczia, N.; Conrotte, J.F.; Kay, D.P.; Guignard, C.; Jung, P.P.; Linster, C.L.
    Saccharomyces cerevisiae forms D-2-hydroxyglutarate and couples its degradation to D-lactate formation via a cytosolic transhydrogenase (2016), J. Biol. Chem., 291, 6036-6058.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.111
-
D-2-hydroxyglutarate pH 9.5, 30°C Saccharomyces cerevisiae
0.45
-
pyruvate pH 9.5, 30°C Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Saccharomyces cerevisiae 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 0.005 mM, about 3fold stimulation Saccharomyces cerevisiae
Zn2+ 0.005 mM, about 3fold stimulation Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P39976
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein. Purified fractions show a yellow color Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + D-lactate
-
Saccharomyces cerevisiae D-2-hydroxyglutarate + pyruvate
-
r
D-2-hydroxyglutarate + oxaloacetate
-
Saccharomyces cerevisiae 2-oxoglutarate + malate
-
r
D-2-hydroxyglutarate + pyruvate
-
Saccharomyces cerevisiae 2-oxoglutarate + D-lactate
-
r
additional information no substrate: L-lactate. The enzyme displays dehydrogenase activity with artificial acceptor dichlorophenolindophenol Saccharomyces cerevisiae ?
-
?

Synonyms

Synonyms Comment Organism
D-2-hydroxyglutarate-pyruvate transhydrogenase
-
Saccharomyces cerevisiae
DLD3
-
Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4
-
D-2-hydroxyglutarate pH 9.5, 30°C Saccharomyces cerevisiae
4.9
-
pyruvate pH 9.5, 30°C Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FAD enzyme is a FAD-dependent transhydrogenase using pyruvate as a hydrogen acceptor Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function a mutant strain lacking cytosolic transhydrogenase Dld3 activity accumulates millimolar levels of D-2-hydroxyglutarate Saccharomyces cerevisiae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
12
-
pyruvate pH 9.5, 30°C Saccharomyces cerevisiae
36
-
D-2-hydroxyglutarate pH 9.5, 30°C Saccharomyces cerevisiae