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Literature summary extracted from

  • Mowat, C.G.; Beaudoin, I.; Durley, R.C.; Barton, J.D.; Pike, A.D.; Chen, Z.W.; Reid, G.A.; Chapman, S.K.; Mathews, F.S.; Lederer, F.
    Kinetic and crystallographic studies on the active site Arg289Lys mutant of flavocytochrome b2 (yeast L-lactate dehydrogenase) (2000), Biochemistry, 39, 3266-3275.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.2.3 in Escherichia coli AR120 Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.2.3 crystallization of Y143F mutant, vapor diffusion technique in presence of PEG 4000 Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.1.2.3 A289K mutant Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.2.3 D-lactate
-
 Saccharomyces cerevisiae
1.1.2.3 L-Mandelate competitive Saccharomyces cerevisiae
1.1.2.3 oxalate
-
 Saccharomyces cerevisiae
1.1.2.3 pyruvate competitive at low concentrations, non-competitve at high concentrations Saccharomyces cerevisiae
1.1.2.3 sulfite competitive Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.2.3 0.03
-
 ferricyanide Y254L mutant Saccharomyces cerevisiae
1.1.2.3 0.04
-
 ferricyanide Y254F mutant Saccharomyces cerevisiae
1.1.2.3 0.07
-
 ferricyanide wild type enzyme Saccharomyces cerevisiae
1.1.2.3 0.22
-
 L-Phenyllactate wild type enzyme Saccharomyces cerevisiae
1.1.2.3 0.29
-
 L-lactate wild type enzyme Saccharomyces cerevisiae
1.1.2.3 0.34
-
 L-lactate Y254F mutant Saccharomyces cerevisiae
1.1.2.3 0.53
-
 L-lactate Y254L mutant Saccharomyces cerevisiae
1.1.2.3 0.7
-
 cytochrome c Y254L mutant Saccharomyces cerevisiae
1.1.2.3 1.43
-
 L-Phenyllactate R289K mutant enzyme Saccharomyces cerevisiae
1.1.2.3 2.4
-
 cytochrome c Y254F mutant Saccharomyces cerevisiae
1.1.2.3 131
-
 cytochrome c wild type enzyme Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.3 mitochondrial intermembrane space soluble Saccharomyces cerevisiae 5758
-

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.2.3 57500
-
 4 * 57500, SDS-PAGE 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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.2.3
-
 Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
1.1.2.3 -180°C, long term storage Saccharomyces cerevisiae
1.1.2.3 -80°C, 0.1 M phosphate buffer, 1 mM EDTA, 1 mM PMSF Saccharomyces cerevisiae
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)-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 (S)-lactate + cytochrome c
-
 Saccharomyces cerevisiae pyruvate + oxidized cytochrome c
-
 ?
1.1.2.3 (S)-mandelate + ferricytochrome c
-
 Saccharomyces cerevisiae hydroxy(phenyl)acetate + ferrocytochrome c
-
 ?
1.1.2.3 (S)-phenyllactate + ferricytochrome c
-
 Saccharomyces cerevisiae phenylpyruvate + ferrocytochrome c
-
 ?
1.1.2.3 L-lactate + ferricyanide
-
 Saccharomyces cerevisiae pyruvate + ferrocyanide + H+
-
 ?
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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.2.3 tetramer 4 * 57500, SDS-PAGE 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 0.42
-
 L-lactate Y254L mutant Saccharomyces cerevisiae
1.1.2.3 7.5
-
 L-lactate Y254F mutant Saccharomyces cerevisiae
1.1.2.3 155
-
 L-lactate wild type enzyme Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.3 cytochrome c
-
 Saccharomyces cerevisiae
1.1.2.3 FMN one FMN per subunit Saccharomyces cerevisiae
1.1.2.3 heme one heme per subunit Saccharomyces cerevisiae
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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.2.3 0.0014
-
 sulfite
-
 Saccharomyces cerevisiae
1.1.2.3 0.0026
-
 L-Mandelate
-
 Saccharomyces cerevisiae
1.1.2.3 0.3
-
 oxalate
-
 Saccharomyces cerevisiae
1.1.2.3 1.4
-
 D-lactate
-
 Saccharomyces cerevisiae
1.1.2.3 3
-
 pyruvate competitive Saccharomyces cerevisiae
1.1.2.3 30
-
 pyruvate non-competitive Saccharomyces cerevisiae