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Literature summary extracted from

  • Daff, S.; Manson, F.D.C.; Reid, G.A.; Chapman, S.K.
    Strategic manipulation of the substrate specificity of Saccharomyces cerevisiae flavocytochrome b2 (1994), Biochem. J., 301, 829-834.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.2.3
-
 Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.1.2.3 A198G turnover reduced to 50% Saccharomyces cerevisiae
1.1.2.3 A198G/L230A double mutant, turnover reduced to less than 10% Saccharomyces cerevisiae
1.1.2.3 L230A turnover reduced to less than 10% Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.2.3 0.4
-
 L-lactate A198G mutant enzyme Saccharomyces cerevisiae
1.1.2.3 0.5
-
 L-lactate wild type enzyme Saccharomyces cerevisiae
1.1.2.3 0.6
-
 L-lactate L230A mutant enzyme Saccharomyces cerevisiae
1.1.2.3 38
-
 L-lactate A198G/L230A mutant enzyme Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.2.3 Fe2+ bound to enzyme Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.2.3 (S)-lactate + 2 ferricytochrome c Saccharomyces cerevisiae can feed electrons to respiratory chain at the level of cytochrome c pyruvate + 2 ferrocytochrome c + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.3 Saccharomyces cerevisiae
-
-
-

Storage Stability

EC Number Storage Stability Organism
1.1.2.3 4°C, precipitate from 70% saturated ammonium sulfate, under nitrogen, stable for several weeks Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.3 (S)-2-hydroxybutyrate + ferricytochrome c
-
 Saccharomyces cerevisiae 2-oxobutyrate + ferrocytochrome c
-
 ?
1.1.2.3 (S)-2-hydroxyhexanoate + ferricytochrome c
-
 Saccharomyces cerevisiae 2-oxohexanoate + ferrocytochrome c
-
 ?
1.1.2.3 (S)-2-hydroxyoctanoate + ferricytochrome c
-
 Saccharomyces cerevisiae 2-oxooctanoate + ferrocytochrome c
-
 ?
1.1.2.3 (S)-2-hydroxyvalerate + ferricytochrome c
-
 Saccharomyces cerevisiae 2-oxovalerate + ferrocytochrome c
-
 ?
1.1.2.3 (S)-lactate + 2 ferricytochrome c
-
 Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
 ?
1.1.2.3 (S)-lactate + 2 ferricytochrome c can feed electrons to respiratory chain at the level of cytochrome c Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
 ?
1.1.2.3 glycolate + ferricytochrome c very poor substrate Saccharomyces cerevisiae glyoxylate + ferrocytochrome c
-
 ?
1.1.2.3 additional information ferricyanide used as electron acceptor Saccharomyces cerevisiae ?
-
 ?
1.1.2.3 additional information electron acceptors other than ferricytochrome c used Saccharomyces cerevisiae ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.2.3 additional information
-
 additional information systematic determination of substrates with different chain length Saccharomyces cerevisiae
1.1.2.3 30
-
 L-lactate L230A mutant enzyme Saccharomyces cerevisiae
1.1.2.3 41
-
 L-lactate A198G/L230A mutant enzyme Saccharomyces cerevisiae
1.1.2.3 185
-
 L-lactate A198G mutant enzyme Saccharomyces cerevisiae
1.1.2.3 400
-
 L-lactate wild type enzyme Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.3 additional information ferricyanide used as electron acceptor Saccharomyces cerevisiae
1.1.2.3 additional information electron acceptors other than ferricytochrome c used Saccharomyces cerevisiae