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Literature summary extracted from

  • Gaume, B.; Sharp, R.E.; Manson, F.D.C.; Chapman, S.K.; Reid, G.A.; Lederer, F.
    Mutation to glutamine of histidine 373, the catalytic base of flavocytochrome b2 (L-lactate dehydrogenase) (1995), Biochimie, 77, 621-630.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.2.3 in Escherichia coli MM294 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 H373Q mutant Saccharomyces cerevisiae
1.1.2.3 Y143F turnover reduced to 15% Saccharomyces cerevisiae
1.1.2.3 Y254L only traces of activity Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.2.3 Fluoropyruvate
-
 Saccharomyces cerevisiae
1.1.2.3 pyruvate competitive at low concentrations, non-competitve at high concentrations Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.2.3 0.0001
-
 L-lactate Y254L mutant enzyme with 2,6-dichloroindophenol as electron acceptor Saccharomyces cerevisiae
1.1.2.3 0.037
-
 L-lactate wild type enzyme with 2,6-dichloroindophenol as electron acceptor Saccharomyces cerevisiae
1.1.2.3 0.04
-
 L-lactate Y143F mutant enzyme with 2,6-dichloroindophenol as electron acceptor Saccharomyces cerevisiae
1.1.2.3 0.13
-
 L-lactate H373Q mutant enzyme with 2,6-dichloroindophenol as electron acceptor 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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.2.3 wild type and mutant enzymes Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
1.1.2.3 -80°C as saturated solution 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 additional information 2,6-dichlorophenolindophenol used as electron acceptor, 10times more sensitive than ferricyanide 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 0.39
-
 L-lactate Y254L mutant enzyme Saccharomyces cerevisiae
1.1.2.3 60
-
 L-lactate Y143F mutant enzyme Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.3 additional information electron acceptors other than ferricytochrome c used Saccharomyces cerevisiae
1.1.2.3 additional information 2,6-dichlorophenolindophenol used as electron acceptor, 10-fold more sensitive than ferricyanide Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.2.3 3
-
 pyruvate competitive Saccharomyces cerevisiae
1.1.2.3 30
-
 pyruvate non-competitive Saccharomyces cerevisiae