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0.0015 - 0.131
ferricytochrome c
0.22 - 1.43
L-Phenyllactate
0.084 - 0.4
Phenyllactate
6
potassium ferricyanide
-
pH 9.5, temperature not specified in the publication
additional information
additional information
-
0.015
(S)-lactate
-
pH and temperature not specified in the publication
0.153
(S)-lactate
-
pH 7.5, 25°C
0.16
(S)-lactate
-
pH 7.0, 25°C, wild type
0.19
(S)-lactate
-
pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F, with heme
0.28
(S)-lactate
-
pH 7.0, 25°C, mutant Y254F
0.4
(S)-lactate
-
pH 7.0, 5°C, phosphate buffer, mutant Y143F, with heme
0.53
(S)-lactate
-
pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme, with heme
0.54
(S)-lactate
-
pH 7.0, 5°C, phosphate buffer, wild-type enzyme, with heme
0.84
(S)-lactate
-
pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme, with FMN
0.89
(S)-lactate
-
pH 7.0, 5°C, phosphate buffer, wild-type enzyme, with FMN
2.09
(S)-lactate
-
pH 7.0, 20°C
2.5 - 5
(S)-lactate
-
pH 7.0, 5°C, phosphate buffer, mutant Y143F, with FMN
2.6
(S)-lactate
-
pH 8.0, temperature not specified in the publication
2.81
(S)-lactate
-
pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F, with FMN
0.02
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant P44A
0.032
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant A67Q
0.051
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant L65A
0.061
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant P64R
0.065
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant F39A
0.069
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant P64Q
0.085
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant A67L
0.092
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant N69K
0.097
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant D72A
0.105
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant V70M
0.109
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant K73A
0.113
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant F39A
0.119
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant E63K
0.131
cytochrome c
pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, wild-type enzyme
0.7
cytochrome c
-
Y254L mutant
2.4
cytochrome c
-
Y254F mutant
131
cytochrome c
-
wild type enzyme
0.03
ferricyanide
-
Y254L mutant
0.04
ferricyanide
-
Y254F mutant
0.07
ferricyanide
-
wild type enzyme
0.07
ferricyanide
-
pH 5.5, isoform with activity maximum at pH 5.5
0.138
ferricyanide
-
pH 7.5, isoform with activity maximum at pH 7.5
0.27
ferricyanide
-
pH 9.5, isoform with activity maximum at pH 9.5
0.0015
ferricytochrome c
-
pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F
0.01
ferricytochrome c
-
pH 7.5, 25°C, wild-type enzyme
0.01
ferricytochrome c
-
pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme
0.023
ferricytochrome c
-
pH 7.5, 25°C, recombinantly expressed flavocytochrome b2 flavin-binding domain
0.045
ferricytochrome c
-
pH 7.0, 5°C, phosphate buffer, wild-type enzyme
0.121
ferricytochrome c
-
pH 7.0, 30°C, phosphate buffer, mutant Y143F
0.131
ferricytochrome c
-
pH 7.0, 30°C, phosphate buffer, wild-type enzyme
0.131
ferricytochrome c
-
pH 7.0, 5°C, phosphate buffer, mutant Y143F
0.0001
L-lactate
-
Y254L mutant enzyme with 2,6-dichloroindophenol as electron acceptor
0.037
L-lactate
-
wild type enzyme with 2,6-dichloroindophenol as electron acceptor
0.04
L-lactate
-
Y143F mutant enzyme with 2,6-dichloroindophenol as electron acceptor
0.13
L-lactate
-
H373Q mutant enzyme with 2,6-dichloroindophenol as electron acceptor
0.16
L-lactate
wild-type, intact protein
0.23
L-lactate
-
Y143F mutant with cytochrome c as electron acceptor
0.24
L-lactate
-
native enzyme with cytochrome c as electron acceptor
0.25
L-lactate
mutant H373Q, using flavin domain only
0.29
L-lactate
-
wild type enzyme
0.33
L-lactate
-
sensor based on the inital Hansenula polymorpha C-105 cells
0.336
L-lactate
pH 7.4, temperature not specified in the publication
0.34
L-lactate
-
Y254F mutant
0.35
L-lactate
-
Y254F mutant
0.36
L-lactate
wild-type, using flavin domain only
0.4
L-lactate
-
intact enzyme
0.4
L-lactate
-
A198G mutant enzyme
0.49
L-lactate
-
wild type enzyme
0.49
L-lactate
-
native enzyme mutant with ferricyanide as electron acceptor
0.5
L-lactate
-
wild type enzyme
0.53
L-lactate
-
Y254L mutant
0.6
L-lactate
-
L230A mutant enzyme
0.65
L-lactate
mutant H373Q, intact protein
0.66
L-lactate
-
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 30°C
0.66
L-lactate
-
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7.5, 25°C
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
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
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
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
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
1.102
L-lactate
pH 7.4, temperature not specified in the publication
1.18
L-lactate
-
FDH domain, reaction conditions: 13 mM ferricyanide, 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C
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
1.6
L-lactate
-
cleaved enzyme
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
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
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
2.9
L-lactate
-
Y143F mutant with ferricyanide as electron acceptor
3
L-lactate
-
with ferricyanide as electron acceptor
3.02
L-lactate
-
biosensor based on recombinant yeast FCb2cells
3.85
L-lactate
-
2,6-dichlorophenolindopenol as electron acceptor
3.9
L-lactate
-
Y254F mutant
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
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
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
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
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
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
8.9
L-lactate
-
wild type enzyme
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
38
L-lactate
-
A198G/L230A mutant enzyme
38
L-lactate
-
A198G/L230G mutant enzyme
0.22
L-Phenyllactate
-
wild type enzyme
1.43
L-Phenyllactate
-
R289K mutant enzyme
0.084
Phenyllactate
-
Y254F mutant
0.4
Phenyllactate
-
wild type enzyme
7.4
pyruvate
-
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
steady-state kinetic parameters and 2H kinetic isotope effects for the isolated flavin domain and intact, wild-type flavocytoochrome b2
-
additional information
additional information
stopped-flow, pre-steady-state and steady-state kinetics measuring electron transfer in artificial systems, redox potentials, overview
-