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show all sequences of 1.1.2.3

Potentiometric and further kinetic characterization of the flavin-binding domain of Saccharomyces cerevisiae flavocytochrome b2. Inhibition by anions binding in the active site

Cenas, N.; Le, K.H.; Terrier, M.; Lederer, F.; Biochemistry 46, 4661-4670 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant wild-type Fcb2 and its recombinant FMN-binding domain (FDH domain) are expressed in Escherichia coli
Saccharomyces cerevisiae
Engineering
Amino acid exchange
Commentary
Organism
R289K
kcat (1/sec) (substrate: L-lactate): 8.6 (in 200 mM phosphate: 9.2, in 400 mM potassium acetate: 8.8, in 400 mM KCl: 9.2, in 400 mM KBr: 7.8), Km (mM) (substrate: L-lactate): 7.0 (in 200 mM phosphate: 8.7, in 400 mM potassium acetate: 9.2, in 400 mM KCl: 6.5, in 400 mM KBr: 5.8). Mutant is not sensitive for excess lactate concentration. In contrast to the wild-type enzyme high concentrations of acetate, phosphate, chloride and bromide show no influence on the mutant enzyme
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetate
-
Saccharomyces cerevisiae
bromide
-
Saccharomyces cerevisiae
chloride
-
Saccharomyces cerevisiae
additional information
enzyme is inhibited by high substrate concentrations
Saccharomyces cerevisiae
phosphate
-
Saccharomyces cerevisiae
pyruvate
-
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.66
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 30°C; FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7.5, 25°C
Saccharomyces cerevisiae
0.86
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 10 mM Tris/HCl buffer, 0.1 M NaCl, pH 7.5, 25°C
Saccharomyces cerevisiae
0.89
-
L-lactate
stopped-flow kinetic parameters for flavin reduction by L-lactate using holo-enzyme, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide
Saccharomyces cerevisiae
0.9
-
L-lactate
influence of anions (200 mM phsophate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
0.94
-
L-lactate
influence of anions (400 mM KBr) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
1.03
-
L-lactate
stopped-flow kinetic parameters for flavin reduction by L-lactate using FDH domain, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide
Saccharomyces cerevisiae
1.18
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C
Saccharomyces cerevisiae
1.5
-
L-lactate
influence of anions (400 mM KCl) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
2.3
-
L-lactate
influence of anions (400 mM KCl) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
2.7
-
L-lactate
influence of anions (400 mM potassium acetate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
2.8
-
L-lactate
influence of anions (300 mM phsophate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
4
-
L-lactate
influence of anions (400 mM KBr) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
4.6
-
L-lactate
influence of anions (400 mM potassium acetate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
5.8
-
L-lactate
influence of anions (400 mM KBr) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
6.5
-
L-lactate
influence of anions (400 mM KCl) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
7
-
L-lactate
mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
8.7
-
L-lactate
influence of anions (200 mM phsophate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
9.2
-
L-lactate
influence of anions (400 mM potassium acetate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Storage Stability
Storage Stability
Organism
-70°C in 0.1 M phosphate buffer, 1 mM EDTA, pH 7, 10 mM DL-lactate is added to the Fcb2 preparations to keep the enzyme in the reduced state
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lactate + ferricyanide
-
685150
Saccharomyces cerevisiae
pyruvate + ferrocyanide + H+
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.8
-
L-lactate
influence of anions (400 mM KBr) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
8.6
-
L-lactate
mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
8.8
-
L-lactate
influence of anions (400 mM potassium acetate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
9.2
-
L-lactate
influence of anions (200 mM phsophate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration; influence of anions (400 mM KCl) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
45
-
L-lactate
influence of anions (400 mM KBr) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
60
-
L-lactate
influence of anions (400 mM KCl) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
61
-
L-lactate
influence of anions (400 mM KBr) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
71
-
L-lactate
influence of anions (200 mM phsophate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
75
-
L-lactate
influence of anions (400 mM KCl) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
86
-
L-lactate
influence of anions (400 mM potassium acetate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
101
-
L-lactate
influence of anions (300 mM phsophate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
113
-
L-lactate
influence of anions (400 mM potassium acetate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
117
-
L-lactate
holo-enzyme, reaction conditions: 1 or 2 mM ferricyanide, 100 mM phosphate buffer, 1mM EDTA, pH 7, 5°C
Saccharomyces cerevisiae
133
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C
Saccharomyces cerevisiae
144
-
L-lactate
stopped-flow kinetic parameters for flavin reduction by L-lactate using holo-enzyme, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide
Saccharomyces cerevisiae
149
-
L-lactate
stopped-flow kinetic parameters for flavin reduction by L-lactate using FDH domain, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide
Saccharomyces cerevisiae
214
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 10 mM Tris/HCl buffer, 0.1 M NaCl, pH 7.5, 25°C
Saccharomyces cerevisiae
240
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7.5, 25°C
Saccharomyces cerevisiae
259
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 30°C
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
-
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
6
-
pyruvate
using the FDH domain at varied ferrocyanide concentrations and a fixed L-lactate concentration pyruvate behaves as a mixed-type inhibitor toward ferrocyanide; using the FDH domain at varied L-lactate concentrations and a fixed ferrocyanide concentration pyruvate behaves as a mixed-type inhibitor toward L-lactate
Saccharomyces cerevisiae
9.7
-
pyruvate
in pre-steady-state kinetic studies of the FDH domain reduction and reoxidation, pyruvate acts as a competitive inhibitor of L-lactate
Saccharomyces cerevisiae
170
-
acetate
in pre-steady-state kinetic studies of the FDH domain reduction and reoxidation, acetate acts as a competitive inhibitor of L-lactate
Saccharomyces cerevisiae
450
-
chloride
in pre-steady-state kinetic studies of the FDH domain reduction and reoxidation, chloride acts as a competitive inhibitor of L-lactate
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant wild-type Fcb2 and its recombinant FMN-binding domain (FDH domain) are expressed in Escherichia coli
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
-
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
R289K
kcat (1/sec) (substrate: L-lactate): 8.6 (in 200 mM phosphate: 9.2, in 400 mM potassium acetate: 8.8, in 400 mM KCl: 9.2, in 400 mM KBr: 7.8), Km (mM) (substrate: L-lactate): 7.0 (in 200 mM phosphate: 8.7, in 400 mM potassium acetate: 9.2, in 400 mM KCl: 6.5, in 400 mM KBr: 5.8). Mutant is not sensitive for excess lactate concentration. In contrast to the wild-type enzyme high concentrations of acetate, phosphate, chloride and bromide show no influence on the mutant enzyme
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetate
-
Saccharomyces cerevisiae
bromide
-
Saccharomyces cerevisiae
chloride
-
Saccharomyces cerevisiae
additional information
enzyme is inhibited by high substrate concentrations
Saccharomyces cerevisiae
phosphate
-
Saccharomyces cerevisiae
pyruvate
-
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
6
-
pyruvate
using the FDH domain at varied ferrocyanide concentrations and a fixed L-lactate concentration pyruvate behaves as a mixed-type inhibitor toward ferrocyanide; using the FDH domain at varied L-lactate concentrations and a fixed ferrocyanide concentration pyruvate behaves as a mixed-type inhibitor toward L-lactate
Saccharomyces cerevisiae
9.7
-
pyruvate
in pre-steady-state kinetic studies of the FDH domain reduction and reoxidation, pyruvate acts as a competitive inhibitor of L-lactate
Saccharomyces cerevisiae
170
-
acetate
in pre-steady-state kinetic studies of the FDH domain reduction and reoxidation, acetate acts as a competitive inhibitor of L-lactate
Saccharomyces cerevisiae
450
-
chloride
in pre-steady-state kinetic studies of the FDH domain reduction and reoxidation, chloride acts as a competitive inhibitor of L-lactate
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.66
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 30°C; FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7.5, 25°C
Saccharomyces cerevisiae
0.86
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 10 mM Tris/HCl buffer, 0.1 M NaCl, pH 7.5, 25°C
Saccharomyces cerevisiae
0.89
-
L-lactate
stopped-flow kinetic parameters for flavin reduction by L-lactate using holo-enzyme, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide
Saccharomyces cerevisiae
0.9
-
L-lactate
influence of anions (200 mM phsophate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
0.94
-
L-lactate
influence of anions (400 mM KBr) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
1.03
-
L-lactate
stopped-flow kinetic parameters for flavin reduction by L-lactate using FDH domain, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide
Saccharomyces cerevisiae
1.18
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C
Saccharomyces cerevisiae
1.5
-
L-lactate
influence of anions (400 mM KCl) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
2.3
-
L-lactate
influence of anions (400 mM KCl) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
2.7
-
L-lactate
influence of anions (400 mM potassium acetate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
2.8
-
L-lactate
influence of anions (300 mM phsophate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
4
-
L-lactate
influence of anions (400 mM KBr) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
4.6
-
L-lactate
influence of anions (400 mM potassium acetate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
5.8
-
L-lactate
influence of anions (400 mM KBr) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
6.5
-
L-lactate
influence of anions (400 mM KCl) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
7
-
L-lactate
mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
8.7
-
L-lactate
influence of anions (200 mM phsophate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
9.2
-
L-lactate
influence of anions (400 mM potassium acetate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
Storage Stability (protein specific)
Storage Stability
Organism
-70°C in 0.1 M phosphate buffer, 1 mM EDTA, pH 7, 10 mM DL-lactate is added to the Fcb2 preparations to keep the enzyme in the reduced state
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lactate + ferricyanide
-
685150
Saccharomyces cerevisiae
pyruvate + ferrocyanide + H+
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.8
-
L-lactate
influence of anions (400 mM KBr) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
8.6
-
L-lactate
mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
8.8
-
L-lactate
influence of anions (400 mM potassium acetate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
9.2
-
L-lactate
influence of anions (200 mM phsophate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration; influence of anions (400 mM KCl) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
45
-
L-lactate
influence of anions (400 mM KBr) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
60
-
L-lactate
influence of anions (400 mM KCl) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
61
-
L-lactate
influence of anions (400 mM KBr) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
71
-
L-lactate
influence of anions (200 mM phsophate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
75
-
L-lactate
influence of anions (400 mM KCl) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
86
-
L-lactate
influence of anions (400 mM potassium acetate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
101
-
L-lactate
influence of anions (300 mM phsophate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
113
-
L-lactate
influence of anions (400 mM potassium acetate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration
Saccharomyces cerevisiae
117
-
L-lactate
holo-enzyme, reaction conditions: 1 or 2 mM ferricyanide, 100 mM phosphate buffer, 1mM EDTA, pH 7, 5°C
Saccharomyces cerevisiae
133
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C
Saccharomyces cerevisiae
144
-
L-lactate
stopped-flow kinetic parameters for flavin reduction by L-lactate using holo-enzyme, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide
Saccharomyces cerevisiae
149
-
L-lactate
stopped-flow kinetic parameters for flavin reduction by L-lactate using FDH domain, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide
Saccharomyces cerevisiae
214
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 10 mM Tris/HCl buffer, 0.1 M NaCl, pH 7.5, 25°C
Saccharomyces cerevisiae
240
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7.5, 25°C
Saccharomyces cerevisiae
259
-
L-lactate
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 30°C
Saccharomyces cerevisiae
Other publictions for EC 1.1.2.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743420
Gillet
QM/MM study of l-lactate oxid ...
Saccharomyces cerevisiae
Phys. Chem. Chem. Phys.
18
15609-15618
2016
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1
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1
1
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3
1
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5
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5
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3
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1
1
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1
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2
1
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Cunane
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1
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1
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348074
Daff
New insights into the catalyti ...
Saccharomyces cerevisiae
Biochemistry
35
6345-6350
1996
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3
1
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696188
Daff
Interaction of cytochrome c wi ...
Saccharomyces cerevisiae
Biochemistry
35
6351-6357
1996
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2
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2
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3
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1
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1
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348071
Gaume
Mutation to glutamine of histi ...
Saccharomyces cerevisiae
Biochimie
77
621-630
1995
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-
1
1
3
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2
4
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1
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2
4
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2
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348072
Tegoni
X-ray structure of two complex ...
Saccharomyces cerevisiae
Biochemistry
34
9840-9850
1995
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1
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1
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4
3
1
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3
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3
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1
4
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3
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696075
Balme
Isolation and characterization ...
Saccharomyces cerevisiae
Biochem. J.
309
601-605
1995
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1
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3
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1
1
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3
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348069
Balme
On the rate of proton exchange ...
Saccharomyces cerevisiae
Protein Sci.
3
109-117
1994
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1
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2
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4
-
1
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1
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1
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4
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1
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1
4
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3
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348070
Daff
-
Strategic manipulation of the ...
Saccharomyces cerevisiae
Biochem. J.
301
829-834
1994
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1
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3
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4
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1
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1
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1
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1
9
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5
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1
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1
1
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3
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4
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1
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1
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1
9
-
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-
5
-
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348068
Silvestrini
Expression in Escherichia coli ...
Wickerhamomyces anomalus
Biochem. J.
295
501-508
1993
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1
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1
1
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1
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3
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3
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1
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3
-
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348067
Brunt
Isolation and characterization ...
Saccharomyces cerevisiae
Biochem. J.
283
87-90
1992
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1
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1
1
1
1
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5
-
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1
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3
-
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1
1
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1
1
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1
1
1
1
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1
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-
3
-
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-
1
-
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348065
Lederer
-
On some aspects of the catalys ...
Saccharomyces cerevisiae
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
773-782
1991
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1
1
2
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4
-
1
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1
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1
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4
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1
3
1
2
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4
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1
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4
-
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4
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348064
Genet
The carbanion of nitroethane i ...
Saccharomyces cerevisiae
Biochem. J.
266
301-304
1990
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-
-
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3
1
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1
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1
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1
2
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3
2
1
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1
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1
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3
-
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348066
Tegoni
Inhibition of L-lactate: cytoc ...
Saccharomyces cerevisiae, Wickerhamomyces anomalus
Eur. J. Biochem.
190
329-342
1990
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-
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2
4
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2
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2
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3
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7
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2
1
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2
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2
1
4
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2
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2
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7
-
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699506
Xia
Molecular structure of flavocy ...
Saccharomyces cerevisiae
J. Mol. Biol.
212
837-863
1990
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1
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348063
Black
Structural basis for the kinet ...
Saccharomyces cerevisiae, Wickerhamomyces anomalus
Biochem. J.
263
973-976
1989
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-
2
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2
1
2
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5
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5
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2
2
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1
2
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5
-
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348062
Ghrir
Primary structure of flavocyto ...
Saccharomyces cerevisiae
Eur. J. Biochem.
139
59-74
1984
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-
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1
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1
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3
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1
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1
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3
-
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348060
Blazy
A standard high-yield purifica ...
Wickerhamomyces anomalus
Anal. Biochem.
88
624-633
1978
-
-
-
-
-
1
-
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1
1
1
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1
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1
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1
1
2
1
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1
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1
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-
1
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1
1
1
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1
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1
1
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348061
Labeyrie
Flavocytochrome b 2 or L-lacta ...
Saccharomyces cerevisiae, Wickerhamomyces anomalus
Methods Enzymol.
53
238-256
1978
-
-
-
1
-
1
6
4
-
2
5
2
-
3
-
-
2
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-
-
2
5
2
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-
-
1
-
-
6
7
-
-
-
-
-
6
1
-
1
-
6
7
4
-
2
5
2
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-
2
-
-
-
2
5
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
287801
Hatefi
-
Metal-containing flavoprotein ...
Saccharomyces cerevisiae, Wickerhamomyces anomalus
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
175-297
1976
-
-
-
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2
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2
3
2
-
2
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6
2
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8
-
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8
-
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2
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2
3
2
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-
-
6
2
-
-
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-
-
-
-
-
-
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-
-
-
-
348058
Jacq
Cytochrome b2 from bakers yeas ...
Saccharomyces cerevisiae
Eur. J. Biochem.
41
311-320
1974
-
-
-
-
-
-
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1
2
1
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2
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1
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1
3
1
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3
-
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3
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1
2
1
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1
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1
3
1
-
-
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-
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348057
Guiard
Yeast L-lactate dehydrogenase ...
Saccharomyces cerevisiae
Eur. J. Biochem.
34
241-247
1973
-
-
-
-
-
-
-
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-
1
1
1
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1
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1
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3
1
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2
-
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2
-
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-
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1
1
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1
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-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
348056
Pritchard
An NAD+-independent L-lactate ...
Rhizopus oryzae
Biochim. Biophys. Acta
250
25-34
1971
-
-
-
-
-
-
1
1
-
1
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1
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1
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1
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3
-
4
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1
1
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2
2
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2
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1
2
1
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1
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1
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1
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3
-
4
-
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1
1
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