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Literature summary for 1.1.2.3 extracted from

  • Sobrado, P.; Fitzpatrick, P.F.
    Solvent and primary deuterium isotope effects show that lactate CH and OH bond cleavages are concerted in Y254F flavocytochrome b2, consistent with a hydride transfer mechanism (2003), Biochemistry, 42, 15208-15214.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
Y254F increase in Km-value, 4fold decrease of vmax Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.16
-
 (S)-lactate pH 7.0, 25°C, wild type Saccharomyces cerevisiae
0.28
-
 (S)-lactate pH 7.0, 25°C, mutant Y254F Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+ hydride transfer mechanism Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + 2 ferricytochrome c
-
 Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.2
-
 (S)-lactate pH 7.0, 25°C, mutant Y254F Saccharomyces cerevisiae
372
-
 (S)-lactate pH 7.0, 25°C, wild type Saccharomyces cerevisiae