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Literature summary extracted from

  • Gillet, N.; Ruiz-Pernia, J.J.; de la Lande, A.; Levy, B.; Lederer, F.; Demachy, I.; Moliner, V.
    QM/MM study of l-lactate oxidation by flavocytochrome b2 (2016), Phys. Chem. Chem. Phys., 18, 15609-15618 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.2.3 D282N site-directed mutagenesis, while the wild-type mutant has residue R289 in a distal or a proximal conformation, the mutant shows R289 only in a distal conformation Saccharomyces cerevisiae
1.1.2.3 additional information active site structures of wild-type and mutant enzymes, detailed overview Saccharomyces cerevisiae
1.1.2.3 Y254L site-directed mutagenesis, while the wild-type mutant has residue R289 in a distal or a proximal conformation, the mutant shows R289 only in a distal conformation Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.2.3 additional information
-
 additional information steady-state kinetics Saccharomyces cerevisiae

Localization

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

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 the first step of the catalytic cycle consists of the oxidation of L-lactate by the FMN prosthetic group. FMN is later reoxidized by transferring its electrons one by one to the ferric heme. The final electron acceptor is cytochrome c pyruvate + 2 ferrocytochrome c + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.3 Saccharomyces cerevisiae P00175
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.2.3 (S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+ the hydride transfer mechanism involves the transfer of the lactate hydroxyl proton to H373 while the substrate aH atom is transferred as a hydride to the flavin mononucleotide (FMN) prosthetic group anchored in the active site Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.3 (S)-lactate + 2 ferricytochrome c the first step of the catalytic cycle consists of the oxidation of L-lactate by the FMN prosthetic group. FMN is later reoxidized by transferring its electrons one by one to the ferric heme. The final electron acceptor is cytochrome c Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
 ?
1.1.2.3 (S)-lactate + 2 flavocytochrome b2
-
 Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.2.3 homotetramer
-
 Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
1.1.2.3 Fcb2
-
 Saccharomyces cerevisiae
1.1.2.3 L-lactate cytochrome c oxidoreductase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.2.3 30
-
 assay at 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 0.51
-
 (S)-lactate mutant Y254L with R289 distal, pH 7.0, 30°C Saccharomyces cerevisiae
1.1.2.3 3.9
-
 (S)-lactate mutant D282N with R289 distal, pH 7.0, 30°C Saccharomyces cerevisiae
1.1.2.3 270
-
 (S)-lactate wild-type enzyme with R289 distal, pH 7.0, 30°C Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.2.3 7
-
 assay at Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.3 ferricytochrome c
-
 Saccharomyces cerevisiae
1.1.2.3 flavocytochrome b2
-
 Saccharomyces cerevisiae
1.1.2.3 FMN each of the four subunits contains a flavin mononucleotide prosthetic group Saccharomyces cerevisiae
1.1.2.3 heme each of the four subunits contains a beta-type heme Saccharomyces cerevisiae
1.1.2.3 additional information FMN and heme groups are localized in two different domains Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
1.1.2.3 additional information molecular dynamics simulations using a hybrid quantum mechanics/molecular mechanics (QM/MM) scheme to study the mechanism of L-lactate oxidation by flavocytochrome b2. Simulation results highlight the influence of the environment on the catalytic mechanism by describing a step-wise process in the wild-type enzyme with R289 in a distal position and a concerted mechanism for the other systems. Structure analysis of pyruvate in the Fcb2 active site pocket with R289 in the distal conformation. Residue Y254 plays a role in the catalytic process by stabilizing the product of the first proton transfer from substrate to H373, while residue D282 is expected to stabilize the imidazolium ion in transition and product states by electrostatic interactions and hydrogen bonding with the Hdelta of H373. Active site structures of wild-type and mutant enzymes, detailed overview Saccharomyces cerevisiae