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0.0018 - 1100
(S)-lactate
0.6
2-oxobutyrate
-
pH 7.5
0.116
2-oxovalerate
-
pH 7.5
11.37
3,4-Dihydroxyphenylpyruvate
pH 6, 25°C
0.123 - 0.408
3-acetylpyridine adenine dinucleotide
0.0085
APAD+
pH 5.5, 25°C, recombinant enzyme
0.0166
APADH
pH 5.5, 25°C, recombinant enzyme
4.7
NADP+
25°C, pH 8, mutant enzyme F16Q/I37K/D38SC81S/N85R, activated by fructose 1,6-diphosphate
1.76 - 8.23
phenylpyruvate
additional information
additional information
-
0.0018
(S)-lactate
pH 5.5, 25°C, recombinant enzyme
0.0026
(S)-lactate
pH 8.5, 25°C, isozyme H4
0.0057
(S)-lactate
pH 8.5, 25°C, isozyme H2M2
0.0142
(S)-lactate
pH 8.5, 25°C, isozyme M4
0.515
(S)-lactate
-
15°C, pH 8
0.517
(S)-lactate
-
20°C, pH 8
0.537
(S)-lactate
-
20°C, pH 7.4
0.541
(S)-lactate
-
15°C, pH 8
0.567
(S)-lactate
-
15°C, pH 7.4
0.616
(S)-lactate
-
20°C, pH 8
0.62
(S)-lactate
-
15°C, pH 7.4
0.641
(S)-lactate
-
20°C, pH 7.4
0.735
(S)-lactate
-
15°C, pH 7
0.803
(S)-lactate
-
20°C, pH 7
0.822
(S)-lactate
-
30°C, pH 7
0.862
(S)-lactate
-
15°C, pH 7
0.909
(S)-lactate
-
30°C, pH 7
0.94
(S)-lactate
-
30°C, pH 7.4
0.966
(S)-lactate
-
20°C, pH 7
1.016
(S)-lactate
-
30°C, pH 7.4
1.191
(S)-lactate
-
30°C, pH 8
1.33
(S)-lactate
-
30°C, pH 7
2.5
(S)-lactate
Molinema dessetae
-
-
8.1
(S)-lactate
-
pH 7.5, 25°C
10.2
(S)-lactate
pH 9.2, 25°C
10.73
(S)-lactate
pH 8.0, temperature not specified in the publication, healthy breast tissue enzyme
11.3
(S)-lactate
-
pH 9.2, 25°C
12
(S)-lactate
pH 9.2, 25°C
17
(S)-lactate
-
pH 8.2, isoenzyme II
21.78
(S)-lactate
pH 8.0, temperature not specified in the publication, breast cancer tissue enzyme
22
(S)-lactate
-
pH 8.8, isoenzyme I
22
(S)-lactate
-
anoxic enzyme, pH 6.7, 25°C
32.9
(S)-lactate
-
aerobic control enzyme, pH 8.5, 25°C
34.2
(S)-lactate
-
anoxic enzyme, pH 8.5, 25°C
93
(S)-lactate
-
pH 9.2, 25°C
100
(S)-lactate
-
in presence of 1 mM fructose 1,6-diphosphate
158
(S)-lactate
-
pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate
0.123
3-acetylpyridine adenine dinucleotide
pH 9.2, 25°C
0.168
3-acetylpyridine adenine dinucleotide
-
pH 9.2, 25°C
0.182
3-acetylpyridine adenine dinucleotide
pH 9.2, 25°C
0.408
3-acetylpyridine adenine dinucleotide
-
pH 9.2, 25°C
0.047
L-lactate
-
pH 7.5
0.152
L-lactate
-
pH not specified in the publication, temperature not specified in the publication
60
L-lactate
pH 7.0, 70°C, recombinant enzyme
3.3
Lactate
-
-
47.4
Lactate
-
LDHB, in the presence of 3.75 mM NAD+
105.1
Lactate
-
LDHB, in the presence of 3.75 mM NAD+
0.0081
NAD+
25°C, pH 8, mutant enzyme F16Q/C81S/N85R, activated by fructose 1,6-diphosphate
0.0303
NAD+
pH 5.5, 25°C, recombinant enzyme
0.105
NAD+
25°C, pH 8, wild-type enzyme, activated by fructose 1,6-diphosphate
0.143
NAD+
-
pH 9.2, 25°C
0.18
NAD+
Molinema dessetae
-
-
0.311
NAD+
-
pH 9.2, 25°C
0.38
NAD+
-
pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate
0.5
NAD+
pH 8.0, temperature not specified in the publication, healthy breast tissue enzyme
0.95
NAD+
-
pH 8.2, isoenzyme II
0.99
NAD+
pH 8.0, temperature not specified in the publication, breast cancer tissue enzyme
1.96
NAD+
-
anoxic enzyme, pH 8.5, 25°C
2.18
NAD+
-
aerobic control enzyme, pH 8.5, 25°C
2.4
NAD+
-
in presence of 1 mM fructose 1,6-diphosphate
2.4
NAD+
-
in presence of 1.0 mM fructose 1,6-diphosphate
0.007
NADH
pH 7.5, 25°C
0.009
NADH
-
pH 7.5, 25°C
0.01
NADH
-
fructose 1,6-diphosphate has no effect
0.0125
NADH
-
pH 7.3, isoenzyme I and isoenzyme II
0.0127
NADH
pH 8.5, 25°C, isozyme H2M2
0.0137
NADH
pH 8.5, 25°C, isozyme H4
0.014
NADH
-
pH 7.5, 25°C
0.0156
NADH
pH 8.5, 25°C, isozyme M4
0.0169
NADH
pH 5.5, 25°C, recombinant enzyme
0.018
NADH
-
wild-type enzyme
0.05
NADH
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
0.054
NADH
pH 6.0, 30°C, isozyme LDH
0.058
NADH
pH 7.0, 30°C, isozyme LDH
0.065
NADH
-
mutant enzyme S163L
0.066
NADH
-
pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate
0.077
NADH
pH 6.0, 30°C, isozyme LDHB
0.08
NADH
-
pH 6.9, 90 mM Tris-maleate buffer, pH 6.9, 0.5 mM fructose 1,6-diphosphate
0.08
NADH
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.11
NADH
pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
0.15
NADH
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
0.18
NADH
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.18
NADH
pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
0.19
NADH
-
measured with D-fructose 1,6-bisphosphate
0.19
NADH
-
measured with D-fructose 1,6-bisphosphate
0.19
NADH
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
0.19
NADH
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
0.2
NADH
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
0.25
NADH
Molinema dessetae
-
-
0.26
NADH
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
0.364
NADH
pH 7.0, 30°C, isozyme LDHB
0.4
NADH
-
in presence of fructose 1,6-diphosphate
0.41
NADH
pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
0.9
NADH
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate
0.93
NADH
pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
8
NADH
-
without fructose 1,6-diphosphate
44
NADH
-
in absence of fructose 1,6-diphosphate
1.76
phenylpyruvate
-
pH 6.5, 30°C, purified enzyme
1.86
phenylpyruvate
mutant Q88R, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
2.5 - 5
phenylpyruvate
mutant I229A, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
3.5
phenylpyruvate
wild-type, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
5.75
phenylpyruvate
mutant I229A, pH 5.5, 30°C
6.82
phenylpyruvate
mutant Q88R, pH 5.5, 30°C
8.23
phenylpyruvate
wild-type, pH 5.5, 30°C
0.016
pyruvate
-
-
0.016
pyruvate
-
20°C, pH 7
0.017
pyruvate
pH 7.5, 25°C
0.018
pyruvate
-
15°C, pH 7
0.018
pyruvate
-
octameric enzyme form
0.019
pyruvate
-
tetrameric enzyme form
0.02
pyruvate
-
pH 7.5, 25°C
0.02
pyruvate
pH 8.0, 25°C
0.025
pyruvate
-
15°C, pH 7.4
0.027
pyruvate
-
15°C, pH 7
0.03
pyruvate
pH 7.5, 25°C
0.033
pyruvate
-
20°C, pH 7
0.039
pyruvate
-
20°C, pH 7.4
0.044
pyruvate
-
15°C, pH 7.4
0.0468
pyruvate
pH 8.5, 25°C, isozyme H4
0.054
pyruvate
-
20°C, pH 7.4
0.057
pyruvate
-
15°C, pH 8
0.06
pyruvate
pH 6.0, 25°C, recombinant wild-type enzyme
0.061
pyruvate
-
30°C, pH 7
0.061
pyruvate
-
30°C, pH 7
0.0653
pyruvate
pH 8.5, 25°C, isozyme H2M2
0.07
pyruvate
-
pH 7.2, 25°C, isoenzyme LDH-A2B2
0.071
pyruvate
-
pH 7.5, 25°C
0.078
pyruvate
-
20°C, pH 8
0.08
pyruvate
-
at 0°C and at 5°C
0.086
pyruvate
-
30°C, pH 7.4
0.09
pyruvate
-
pH 7.6, 25°C, isoenzyme LDH-B4
0.11
pyruvate
-
15°C, pH 8
0.113
pyruvate
-
pH 7.0, 4°C
0.117
pyruvate
-
30°C, pH 7.4
0.123
pyruvate
-
aerobic control enzyme, pH 6.7, 25°C
0.13
pyruvate
pH 8.5, 25°C, isozyme M4
0.13
pyruvate
-
soluble recombinant enzyme, pH 7.0, 25°C
0.133
pyruvate
-
immobilized recombinant enzyme, pH 7.0, 25°C
0.14
pyruvate
-
pH 7.5, 25°C
0.145
pyruvate
-
30°C, pH 8
0.16
pyruvate
pH 7.0, 0°C, recombinant enzyme
0.16
pyruvate
pH 7.0, 0°C, recombinant enzyme
0.171
pyruvate
-
20°C, pH 8
0.18
pyruvate
pH 5.8, 60°C, recombinant enzyme
0.19
pyruvate
-
anoxic enzyme, pH 6.7, 25°C
0.1973
pyruvate
pH 5.5, 25°C, recombinant enzyme
0.2
pyruvate
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.21
pyruvate
pH 7.0, 0°C, recombinant enzyme
0.22
pyruvate
-
pH 7.1, 25°C, isoenzyme LDH-A4
0.25
pyruvate
-
with 1.0 mM fructose 1,6-diphosphate
0.312
pyruvate
-
30°C, pH 7.4
0.32
pyruvate
-
pH 6.5, 30°C, purified enzyme
0.34
pyruvate
Molinema dessetae
-
-
0.34
pyruvate
-
pH 7.3, isoenzyme I
0.353
pyruvate
-
anoxic enzyme, pH 7.2, 25°C
0.36
pyruvate
-
aerobic control enzyme, pH 7.2, 25°C
0.42
pyruvate
-
pH 7.3, isoenzyme II
0.5
pyruvate
-
pH 6.5, isoenzyme II
0.67
pyruvate
-
pH 8.0, 25°C, in absence of aldolase
0.8
pyruvate
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.93
pyruvate
pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
1
pyruvate
-
in presence of 0.02 mM fructose 1,6-diphosphate
1.15
pyruvate
-
in absence of fructose 1,6-diphosphate
1.3
pyruvate
pH 6.0, 30°C, isozyme LDHB
1.3
pyruvate
-
LDHB, in the presence of 0.25 mM NADH
1.5
pyruvate
-
pH 6.9, 90 mM Tris-maleate buffer, pH 6.9, 0.5 mM fructose 1,6-diphosphate
1.5
pyruvate
pH 6.0, 30°C, isozyme LDH
1.7
pyruvate
pH 7.0, 30°C, isozyme LDH
1.9
pyruvate
-
LDHB, in the presence of 0.2 mM NADH
1.91
pyruvate
recombinant enzyme, pH 6.5, 55°C
1.95
pyruvate
-
pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate
2.2
pyruvate
-
in absence of fructose 1,6-diphosphate
2.2
pyruvate
pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
2.3
pyruvate
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
2.7
pyruvate
pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
2.76
pyruvate
-
pH 6.0, 25°C, recombinant wild-type enzyme in presence of fructose 1,6-bisphosphate
2.8
pyruvate
-
LDHB, in the presence of 0.15 mM NADH
2.9
pyruvate
pH 7.0, 30°C, isozyme LDHB
3
pyruvate
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
3.7
pyruvate
-
pH 6.0, 25°C, recombinant mutant D38R in presence of fructose 1,6-bisphosphate
3.8
pyruvate
pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
4.1
pyruvate
-
isoform LDHL1, pH 7, 45°C
4.8
pyruvate
-
LDHB, in the presence of 0.125 mM NADH
5
pyruvate
-
LDHB, in the presence of 0.25 mM NADH
6.8
pyruvate
-
measured with D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
6.8
pyruvate
-
measured with D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
6.8
pyruvate
-
isoform LDHL2, pH 7, 40°C
7
pyruvate
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
7
pyruvate
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
7.7
pyruvate
-
in presence of fructose 1,6-diphosphate
7.7
pyruvate
-
LDHB, in the presence of 0.2 mM NADH
8.4
pyruvate
-
LDHB, in the presence of 0.15 mM NADH
13
pyruvate
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
13.3
pyruvate
-
pH 7.5, 25°C, recombinant mutant I12V/R81Q/M85E/G210A/V214I
15
pyruvate
-
LDHB, in the presence of 0.125 mM NADH
15
pyruvate
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate
19.3
pyruvate
-
pH 6.0, 25°C, recombinant mutant D38R in absence of fructose 1,6-bisphosphate
32
pyruvate
-
pH 6.0, 25°C, recombinant wild-type enzyme in absence of fructose 1,6-bisphosphate
34
pyruvate
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values for mutant enzymes with enlarged loop
-
additional information
additional information
-
influence of pH
-
additional information
additional information
-
influence of pH
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
an allosteric enzyme
-
additional information
additional information
-
an allosteric enzyme
-
additional information
additional information
isozymes LDH and LDHB, kinetic analysis, NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH does not change with pH
-
additional information
additional information
-
isozymes LDH and LDHB, kinetic analysis, NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH does not change with pH
-
additional information
additional information
-
kinetics analysis
-
additional information
additional information
-
steady-state and transient kinetics, rapid kinetics of the multiple-turnover reaction, overview
-
additional information
additional information
-
stopped-flow kinetics, steady-state kinetics, and thermodynamics of free and NADH-bound enzyme, overview
-
additional information
additional information
kinetics, the enzyme is allosteric in presence of D-fructose 1,6-bisphosphate, overview
-
additional information
additional information
-
alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, kinetic analysis of the recombinant enzyme, overview
-
additional information
additional information
alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, kinetic analysis of the recombinant enzyme, overview
-
additional information
additional information
-
enzyme kinetics, ordered bibi kinetic mechanism of nLDH with the coenzyme binding first
-
additional information
additional information
LDH has different kinetic characteristics in breast tumors compared to normal breast tissues. Tumor LDH affinity in the pyruvate reduction reaction is the same as for normal LDH but Vmax of cancerous LDH is higher relative to normal LDH. In the lactate oxidation reaction, affinity of tumor LDH for lactate and NAD+ is lower than for normal LDH, also the enzyme efficiency for lactate and NAD+ is higher in normal samples. The activation energy for the pyruvate reduction reaction is higher in cancerous tissues. The enzyme in forward reaction in both tissues displays sigmoidal kinetics with respect to pyruvate and NADH
-
additional information
additional information
-
LDH has different kinetic characteristics in breast tumors compared to normal breast tissues. Tumor LDH affinity in the pyruvate reduction reaction is the same as for normal LDH but Vmax of cancerous LDH is higher relative to normal LDH. In the lactate oxidation reaction, affinity of tumor LDH for lactate and NAD+ is lower than for normal LDH, also the enzyme efficiency for lactate and NAD+ is higher in normal samples. The activation energy for the pyruvate reduction reaction is higher in cancerous tissues. The enzyme in forward reaction in both tissues displays sigmoidal kinetics with respect to pyruvate and NADH
-
additional information
additional information
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
additional information
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
additional information
-
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
additional information
Michaelis-Menten kinetic modelling, detailed overview. NADH can bind only to the open-loop apoenzyme, substrate analogue oxamate can bind only to the bsLDH·NADH binary complex in the open-loop conformation, and oxamate binding is followed by closing of the active site loop preventing oxamate unbinding. The open and closed states of the loop are in dynamic equilibrium and interconvert on the submillisecond time scale. This interconversion strongly accelerates with an increase in temperature because of significant enthalpy barriers. Binding of NADH to bsLDH results in minor changes of the loop dynamics and does not shift the open-closed equilibrium, but binding of the oxamate substrate mimic shifts this equilibrium to the closed state. At high excess oxamate concentrations where all active sites are nearly saturated with the substrate mimic, all active site mobile loops are mainly closed, kinetic analysis, overview
-
additional information
additional information
-
Michaelis-Menten kinetic modelling, detailed overview. NADH can bind only to the open-loop apoenzyme, substrate analogue oxamate can bind only to the bsLDH·NADH binary complex in the open-loop conformation, and oxamate binding is followed by closing of the active site loop preventing oxamate unbinding. The open and closed states of the loop are in dynamic equilibrium and interconvert on the submillisecond time scale. This interconversion strongly accelerates with an increase in temperature because of significant enthalpy barriers. Binding of NADH to bsLDH results in minor changes of the loop dynamics and does not shift the open-closed equilibrium, but binding of the oxamate substrate mimic shifts this equilibrium to the closed state. At high excess oxamate concentrations where all active sites are nearly saturated with the substrate mimic, all active site mobile loops are mainly closed, kinetic analysis, overview
-
additional information
additional information
-
Vmax in the pyruvate-reducing direction is significantly higher for the enzyme from anoxic crayfish whereas in the lactate-oxidizing direction the Vmax is significantly higher for the aerobic control enzyme
-
additional information
additional information
-
Km values for pyruvate, NADH, (S)-lactate and NAD+ are measured in the solubilized mirochondrial Hep G2 fractions. They differ from the values measured in the cytosolic fractions
-
additional information
pyruvate
-
the enzyme shows hyperbolic dependence on the substrate concentration