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Literature summary for 1.1.2.3 extracted from

  • Balme, A.; Brunt, C.E.; Pallister, R.L.; Chapman, S.K.; Reid, G.A.
    Isolation and characterization of the flavin-binding domain of flavocytochrome b2 expressed independently in Escherichia coli (1995), Biochem. J., 309, 601-605.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of flavocytochrome b2 flavin-binding domain in Escherichia coli Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic parameters and 2H kinetic isotope effects for the isolated flavin domain and intact, wild-type flavocytoochrome b2 Saccharomyces cerevisiae
0.01
-
ferricytochrome c pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae
0.023
-
ferricytochrome c pH 7.5, 25°C, recombinantly expressed flavocytochrome b2 flavin-binding domain Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
x * 47000, recombinantly expressed flavocytochrome b2 flavin-binding domain, SDS-PAGE Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinantly expressed flavocytochrome b2 flavin-binding domain Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactate + 2 ferricytochrome c kcat/KM is 24000 fold lower with the recombinantly expressed flavocytochrome b2 flavin-binding domain compared to wild-type enzyme Saccharomyces cerevisiae pyruvate + 2 ferrocytochrome c + 2 H+
-
?

Subunits

Subunits Comment Organism
? x * 47000, recombinantly expressed flavocytochrome b2 flavin-binding domain, SDS-PAGE Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
flavocytochrome b2
-
Saccharomyces cerevisiae
L-lactate:cytochrome c oxidoreductase
-
Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic parameters and 2H kinetic isotope effects for the isolated flavin domain and intact, wild-type flavocytoochrome b2 Saccharomyces cerevisiae
0.02
-
ferricytochrome c pH 7.5, 25°C, recombinantly expressed flavocytochrome b2 flavin-binding domain Saccharomyces cerevisiae
207
-
ferricytochrome c pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FMN the C-terminal domain of the enzyme contains FMN Saccharomyces cerevisiae
heme the N-terminal domain of the enzyme contains protohaem IX Saccharomyces cerevisiae