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(R,S)-2-hydroxy-3-butenoic acid + acceptor
2-oxo-3-butenoic acid + reduced acceptor
(R,S)-2-hydroxybutyrate + acceptor
2-oxobutyrate + reduced acceptor
Substrates: slow substrate
Products: -
?
(R,S)-2-hydroxybutyric acid + acceptor
2-oxo-3-butynoic acid + reduced acceptor
Substrates: very low binding affinity for MDH
Products: -
?
(R,S)-2-hydroxyhexanoate + acceptor
2-oxohexanoate + reduced acceptor
Substrates: -
Products: -
?
(R,S)-2-hydroxyisocaproate + acceptor
2-oxoisocaproate + reduced acceptor
Substrates: -
Products: -
?
(R,S)-2-hydroxyisovalerate + acceptor
2-oxo-isovalerate + reduced acceptor
(R,S)-2-hydroxyoctanoate + acceptor
2-oxooctanoate + reduced acceptor
Substrates: slow substrate
Products: -
?
(R,S)-2-hydroxyvalerate + acceptor
2-oxovalerate + reduced acceptor
Substrates: -
Products: -
?
(R,S)-3-indolelactate + acceptor
3-(1H-indol-2-yl)-2-oxopropanoate + reduced acceptor
Substrates: -
Products: -
?
(R,S)-3-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
Substrates: slow substrate
Products: -
?
(R,S)-indoleglycolate + acceptor
indol-2-yl(oxo)acetate + reduced acceptor
Substrates: -
Products: -
?
(R,S)-mandelate + 2,6-dichlorophenolindophenol
2-oxo-2-phenylacetate + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
?
(R,S)-mandelate + ferricyanide
2-oxo-2-phenylacetate + ferrocyanide
Substrates: -
Products: -
?
(R,S)-p-chloromandelate + acceptor
?
-
Substrates: -
Products: -
?
(S)-2-hydroxy-2-phenylacetate + O2
2-oxo-2-phenylacetate + H2O2
-
Substrates: in absence of any other electron acceptor, oxygen is used by the wild-type enzyme for reoxidation of the reduced flavin, at a rather slow rate. Ping-pong kinetics
Products: -
?
(S)-3-phenyllactate + acceptor
?
-
Substrates: -
Products: -
?
(S)-mandelate + 2 ferricyanide
2-oxo-2-phenylacetate + 2 ferrocyanide + 2 H+
(S)-mandelate + 2 ferricyanide
benzoylformic acid + 2 ferrocyanide + 2 H+
-
Substrates: -
Products: -
?
(S)-mandelate + 2,6-dichloroindophenol
2-oxo-2-phenylacetate + ?
-
Substrates: -
Products: -
?
(S)-mandelate + 2,6-dichlorophenolindophenol
2-oxo-2-phenylacetate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
?
(S)-mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
(S)-mandelate + acceptor
benzoylformate + reduced acceptor
Substrates: -
Products: -
?
(S)-mandelate + acceptor
phenylglyoxylate + reduced acceptor
Substrates: -
Products: -
?
(S)-mandelate + cytochrome c
2-oxo-2-phenylacetate + ?
-
Substrates: -
Products: -
?
(S)-mandelate + FMN
benzoylformic acid + FMNH2
-
Substrates: -
Products: -
?
(S)-mandelate + FMN
phenylglyoxylate + FMNH2
(S)-phenyllactate + 2,6-dichlorophenolindophenol
?
-
Substrates: -
Products: -
?
2-hydroxy-3-butynoate + acceptor
2-oxo-3-butynoate + reduced acceptor
2-hydroxybutyrate + acceptor
2-oxobutyrate + reduced acceptor
-
Substrates: -
Products: -
?
2-hydroxyhexanoate + acceptor
2-oxohexanoate + reduced acceptor
-
Substrates: -
Products: -
?
2-hydroxyisocaproate + acceptor
2-oxoisocaproate + reduced acceptor
-
Substrates: -
Products: -
?
2-hydroxyoctanoate + acceptor
2-oxooctanoate + reduced acceptor
-
Substrates: -
Products: -
?
2-hydroxyoctanoate + acceptor
? + reduced acceptor
Substrates: -
Products: -
?
2-hydroxyvalerate + acceptor
2-oxovalerate + reduced acceptor
-
Substrates: -
Products: -
?
3-hydroxy-DL-mandelate + ferricyanide
2-oxo-2-(3-hydroxyphenyl)acetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
3-indolelactate + acceptor
3-(1H-indol-2-yl)-2-oxopropanoate + reduced acceptor
-
Substrates: -
Products: -
?
3-indolelactate + acceptor
? + reduced acceptor
Substrates: -
Products: -
?
3-methoxy-DL-mandelate + ferricyanide
2-oxo-2-(3-methoxyphenyl)acetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
3-phenyllactate + acceptor
2-oxo-3-phenylpropanoate + reduced acceptor
-
Substrates: -
Products: -
?
4-bromo-DL-mandelate + ferricyanide
2-oxo-2-(4-bromophenyl)acetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
4-chloro-DL-mandelate + ferricyanide
2-oxo-2-(4-chlorophenyl)acetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
4-chloromandelate + acceptor
2-oxo-2-(4-chlorophenyl)acetate + reduced acceptor
-
Substrates: -
Products: -
?
4-fluoro-D,L-mandelate + ferricyanide
2-oxo-2-(4-fluorophenyl)acetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
4-hydroxy-DL-mandelate + ferricyanide
2-oxo-2-(4-hydroxyphenyl)acetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
4-methoxy-DL-mandelate + ferricyanide
2-oxo-2-(4-methoxyphenyl)acetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
4-methyl-DL-mandelate + ferricyanide
2-oxo-2-(4-methylphenyl)acetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
DL-mandelate + ferricyanide
2-oxo-2-phenylacetate + ferrocyanide + H2O
-
Substrates: -
Products: -
?
ethyl-(S)-mandelate + acceptor
?
Substrates: -
Products: -
?
indoleglycolate + acceptor
indol-2-yl(oxo)acetate + reduced acceptor
-
Substrates: -
Products: -
?
L-mandelate + ferricyanide
2-oxo-2-phenylacetate + ferrocyanide
-
Substrates: -
Products: -
?
mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
methyl-(S)-mandelate + acceptor
?
Substrates: -
Products: -
?
additional information
?
-
(R,S)-2-hydroxy-3-butenoic acid + acceptor
2-oxo-3-butenoic acid + reduced acceptor
-
Substrates: -
Products: -
?
(R,S)-2-hydroxy-3-butenoic acid + acceptor
2-oxo-3-butenoic acid + reduced acceptor
Substrates: very low binding affinity for MDH
Products: -
?
(R,S)-2-hydroxyisovalerate + acceptor
2-oxo-isovalerate + reduced acceptor
-
Substrates: -
Products: -
?
(R,S)-2-hydroxyisovalerate + acceptor
2-oxo-isovalerate + reduced acceptor
Substrates: -
Products: -
?
(S)-mandelate + 2 ferricyanide
2-oxo-2-phenylacetate + 2 ferrocyanide + 2 H+
Substrates: -
Products: -
?
(S)-mandelate + 2 ferricyanide
2-oxo-2-phenylacetate + 2 ferrocyanide + 2 H+
-
Substrates: -
Products: -
?
(S)-mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
-
Substrates: reduction of 2,6-dichloroindophenol in presence of N-methylphenazonium methosulfate
Products: -
?
(S)-mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
-
Substrates: -
Products: -
?
(S)-mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
-
Substrates: -
Products: -
r
(S)-mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
-
Substrates: acceptor: 2,6-dichloroindophenol plus phenazine methosulfate. The MDH reaction has two rate-limiting step of similar activation energies: the formation and breakdown of a distinct intermediate, with the latter step being slightly more rate limiting. MDH is capable of catalyzing the reverse reaction, the reoxidation of reduced MDH by the product ketoacid, benzoylformate. The transient intermediate is observed during the reverse reaction as well
Products: -
r
(S)-mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
-
Substrates: phenazine methosulfate and 2,6-dichloroindophenol as acceptor. In absence of any other electron acceptor, oxygen is used by the wild-type enzyme for reoxidation of the reduced flavin, at a rather slow rate
Products: -
?
(S)-mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
-
Substrates: reduction of 2,6-dichloroindophenol in presence of N-methylphenazonium methosulfate
Products: -
?
(S)-mandelate + FMN
phenylglyoxylate + FMNH2
-
Substrates: -
Products: -
?
(S)-mandelate + FMN
phenylglyoxylate + FMNH2
-
Substrates: -
Products: -
?
2-hydroxy-3-butynoate + acceptor
2-oxo-3-butynoate + reduced acceptor
-
Substrates: -
Products: -
?
2-hydroxy-3-butynoate + acceptor
2-oxo-3-butynoate + reduced acceptor
Substrates: -
Products: -
?
mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
-
Substrates: -
Products: -
?
mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
Substrates: -
Products: -
?
additional information
?
-
Substrates: (S)-mandelamide, (S)-1-phenyl-2-propen-1-ol, (S)-1-phenyl-1,2-ethanediol, (S)-1-phenyl-2-propyn-1-ol, (R,S)-pantoyllactone, and (S)-1-phenyl-2,2,2-trifluoroethanol are no substrates
Products: -
?
additional information
?
-
-
Substrates: (S)-mandelamide, (S)-1-phenyl-2-propen-1-ol, (S)-1-phenyl-1,2-ethanediol, (S)-1-phenyl-2-propyn-1-ol, (R,S)-pantoyllactone, and (S)-1-phenyl-2,2,2-trifluoroethanol are no substrates
Products: -
?
additional information
?
-
-
Substrates: enzyme-catalyzed reaction proceeds via the same transition state for each substrate and indicates that this transition state is relatively non-polar but has an electron-rich centre at the alpha-carbon position
Products: -
?
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22
(R,S)-2-hydroxy-3-butynoic acid
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
32
(R,S)-2-hydroxybutyrate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
4.9
(R,S)-2-hydroxyhexanoate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
4.3
(R,S)-2-hydroxyisocaproate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
9.5
(R,S)-2-hydroxyisovalerate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
0.75
(R,S)-2-hydroxyoctanoate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
15.3
(R,S)-2-hydroxyvalerate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
0.9
(R,S)-3-indolelactate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
0.4
(R,S)-indoleglycolate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
0.33
(R,S)-mandelate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
0.074 - 4.3
(S)-3-phenyllactate
0.78 - 2.6
(S)-phenyllactate
10.3
2-Hydroxy-3-butenoate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
4.3 - 22
2-Hydroxy-3-butynoate
4.4 - 32
2-Hydroxybutyrate
0.89 - 4.9
2-hydroxyhexanoate
0.49 - 4.3
2-hydroxyisocaproate
2.6
2-Hydroxyisovalerate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.14 - 0.8
2-Hydroxyoctanoate
3.2 - 15.3
2-hydroxyvalerate
0.08
3-hydroxy-D,L-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.13 - 0.9
3-indolelactate
0.12
3-methoxy-D,L-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.26
4-bromo-D,L-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.15 - 0.38
4-chloro-D,L-mandelate
0.27 - 0.43
4-chloromandelate
0.16
4-fluoro-D,L-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.12
4-methoxy-D,L-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.17
4-methyl-D,L-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.35
D,L-Mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
2
DL-3-phenyllactate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C
0.47 - 0.78
DL-[2-1H]-mandelate
0.53 - 1.33
DL-[2-2H]-mandelate
2.7 - 3.7
ethyl-(S)-mandelate
3.87
ferricyanide
-
at pH 6.5 and 30°C
0.24 - 0.63
indoleglycolate
0.24
L-Mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
7.4 - 11.3
methyl-(S)-mandelate
0.074
(S)-3-phenyllactate
-
pH 7.5, 20°C, mutant enzyme R277G
4.3
(S)-3-phenyllactate
-
pH 7.5, 20°C, wild-type enzyme
0.04
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme, G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH
0.085
(S)-Mandelate
-
pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.09
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.11
(S)-Mandelate
-
pH 7.5, 4°C
0.12
(S)-Mandelate
-
pH 7.5, 20°C
0.12
(S)-Mandelate
-
pH 7.5, 20°C, wild-type enzyme
0.12
(S)-Mandelate
wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5
0.13
(S)-Mandelate
-
pH 7.5, 20°C, wild-type enzyme
0.15
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme G81A
0.158
(S)-Mandelate
-
pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus
0.17
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme G81V
0.18
(S)-Mandelate
-
pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, wild-type enzyme
0.18
(S)-Mandelate
-
pH 7.5, 25°C, electron acceptor: 2,6-dichloroindophenol
0.206
(S)-Mandelate
-
pH 7.5, wild-type enzyme
0.225
(S)-Mandelate
-
pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted
0.229
(S)-Mandelate
-
pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach
0.27
(S)-Mandelate
-
pH 7.5, 25°C, electron acceptor: ferricyanide
0.27
(S)-Mandelate
-
chitosan-immobilized enzyme, at pH 3.4 and 45°C
0.49
(S)-Mandelate
-
pH 7.5, 25°C, electron acceptor: cytochrome c
0.92
(S)-Mandelate
-
at pH 6.5 and 30°C
1.5
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165K
2
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme G81D
2.3
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme G81S
4.4
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165M
4.4
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277K
5.6
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277K
5.6
(S)-Mandelate
mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5
5.8
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165G
12
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165E
13
(S)-Mandelate
-
mutant enzyme H274G, in presence of 20 mM imidazole
15.2
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165K/R277K
17
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277G
17
(S)-Mandelate
mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5
19.2
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277H
31.4
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165G/R277K
47
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277G
73
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277L
0.78
(S)-phenyllactate
-
pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach
2.6
(S)-phenyllactate
-
pH 7.5, wild-type enzyme
4.3
2-Hydroxy-3-butynoate
-
pH 7.5, 20°C, mutant enzyme G81A
17.2
2-Hydroxy-3-butynoate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
22
2-Hydroxy-3-butynoate
-
pH 7.5, 20°C, wild-type enzyme
4.4
2-Hydroxybutyrate
-
pH 7.5, 20°C, mutant enzyme G81A
13.2
2-Hydroxybutyrate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
32
2-Hydroxybutyrate
-
pH 7.5, 20°C, wild-type enzyme
0.89
2-hydroxyhexanoate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
1.4
2-hydroxyhexanoate
-
pH 7.5, 20°C, mutant enzyme G81A
4.9
2-hydroxyhexanoate
-
pH 7.5, 20°C, wild-type enzyme
0.49
2-hydroxyisocaproate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
1.6
2-hydroxyisocaproate
-
pH 7.5, 20°C, mutant enzyme G81A
4.3
2-hydroxyisocaproate
-
pH 7.5, 20°C, wild-type enzyme
0.14
2-Hydroxyoctanoate
-
pH 7.5, 20°C, mutant enzyme G81A
0.14
2-Hydroxyoctanoate
mutant G81A
0.29
2-Hydroxyoctanoate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.29
2-Hydroxyoctanoate
chimera MDH-GOX2
0.57
2-Hydroxyoctanoate
mutant G81A of chimera MDH-GOX2
0.8
2-Hydroxyoctanoate
wild-type enzyme
0.8
2-Hydroxyoctanoate
-
pH 7.5, 20°C, wild-type enzyme
3.2
2-hydroxyvalerate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
6.4
2-hydroxyvalerate
-
pH 7.5, 20°C, mutant enzyme G81A
15.3
2-hydroxyvalerate
-
pH 7.5, 20°C, wild-type enzyme
0.13
3-indolelactate
mutant G81A of chimera MDH-GOX2
0.17
3-indolelactate
-
pH 7.5, 20°C, mutant enzyme G81A
0.17
3-indolelactate
mutant G81A
0.64
3-indolelactate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.64
3-indolelactate
chimera MDH-GOX2
0.9
3-indolelactate
wild-type enzyme
0.9
3-indolelactate
-
pH 7.5, 20°C, wild-type enzyme
0.37
3-Phenyllactate
-
pH 7.5, 20°C, mutant enzyme G81A
1.3
3-Phenyllactate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
2
3-Phenyllactate
-
pH 7.5, 20°C, wild-type enzyme
0.15
4-chloro-D,L-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.38
4-chloro-D,L-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.27
4-chloromandelate
-
pH 7.5, 20°C, wild-type enzyme
0.43
4-chloromandelate
-
pH 7.5, 20°C, mutant enzyme G81A
0.47
DL-[2-1H]-mandelate
-
pH 7.5, 25°C, cosubstrate ferricyanide, LMDH holoenzyme
0.74
DL-[2-1H]-mandelate
-
pH 7.5, 25°C, cosubstrate ferricyanide, L-MDH flavin domain
0.78
DL-[2-1H]-mandelate
-
pH 7.5, 25°C, cosubstrate cytochrome c, LMDH holoenzyme
0.53
DL-[2-2H]-mandelate
-
pH 7.5, 25°C, cosubstrate ferricyanide, LMDH holoenzyme
0.74
DL-[2-2H]-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.79
DL-[2-2H]-mandelate
-
pH 7.5, 25°C, cosubstrate ferricyanide, L-MDH flavin domain
1.33
DL-[2-2H]-mandelate
-
pH 7.5, 25°C, cosubstrate cytochrome, LMDH holoenzyme
2.7
ethyl-(S)-mandelate
mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5
2.9
ethyl-(S)-mandelate
wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5
3.7
ethyl-(S)-mandelate
mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5
0.24
indoleglycolate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.4
indoleglycolate
-
pH 7.5, 20°C, wild-type enzyme
0.63
indoleglycolate
-
pH 7.5, 20°C, mutant enzyme G81A
0.04
Mandelate
mutant G81A of chimera MDH-GOX2
0.09
Mandelate
chimera MDH-GOX2
0.14
Mandelate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.24
Mandelate
wild-type enzyme
0.24
Mandelate
-
pH 7.5, 20°C, mutant enzyme G81A
0.24
Mandelate
-
pH 7.5, 20°C, wild-type enzyme
0.24
Mandelate
mutant G81A
7.4
methyl-(S)-mandelate
mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5
10.3
methyl-(S)-mandelate
mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5
11.3
methyl-(S)-mandelate
wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5
0.04
O2
-
pH 7.5, 20°C, mutant enzyme G81V
0.22
O2
-
pH 7.5, 20°C, mutant enzyme G81D
0.49
O2
-
pH 7.5, 20°C, mutant enzyme, G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH
0.68
O2
-
pH 7.5, 20°C, mutant enzyme MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with 205 residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
1.1
O2
-
pH 7.5, 20°C, mutant enzyme G81A
1.4
O2
-
pH 7.5, 20°C, mutant enzyme G81S
3.2
O2
-
pH 7.5, 20°C, wild-type enzyme
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0.03
(R,S)-p-chloromandelate
-
mutant enzyme H274G, in presence of 20 mM imidazole
201 - 270
(S)-3-phenyllactate
0.5
2-Hydroxy-3-butenoate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
3.9 - 14.8
2-Hydroxy-3-butynoate
0.1 - 0.37
2-Hydroxybutyrate
0.19 - 0.48
2-hydroxyhexanoate
0.48 - 1.28
2-hydroxyisocaproate
0.03
2-Hydroxyisovalerate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.26 - 1
2-Hydroxyoctanoate
0.27 - 0.5
2-hydroxyvalerate
313
2-oxo-2-phenylacetate
-
-
108
3-hydroxy-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.27 - 3.9
3-indolelactate
68
3-methoxy-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.15 - 0.87
3-Phenyllactate
108
4-bromo-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
68 - 116
4-chloro-DL-mandelate
9.3 - 334
4-chloromandelate
98
4-fluoro-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
146
4-hydroxy-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
106
4-methoxy-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
80
4-methyl-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
225
cytochrome c
-
pH 7.5, 25°C
94
D,L-Mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanid
155 - 316
DL-[2-1H]-mandelate
88 - 99
DL-[2-2H]-mandelate
0.3 - 204
ethyl-(S)-mandelate
550
ferricyanide
-
pH 7.5, 25°C
1.2 - 122
indoleglycolate
114
L-Mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
2.3 - 151
methyl-(S)-mandelate
201
(S)-3-phenyllactate
-
pH 7.5, 20°C, mutant enzyme R277G
270
(S)-3-phenyllactate
-
pH 7.5, 20°C, wild-type enzyme
0.04
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165G/R277K
0.05
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme G81V
0.09
(S)-Mandelate
-
mutant enzyme H274G, in presence of 20 mM imidazole
0.11
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme G81D
0.23
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277G
0.23
(S)-Mandelate
mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5
0.27
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277L
0.64
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277G
1.1
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165K/R277K
1.52
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277H
1.6
(S)-Mandelate
-
pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach
2.3
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme, G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH
2.8
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme G81S
3 - 6
(S)-Mandelate
-
pH 7.5, 25°C, electron acceptor: 2,6-dichloroindophenol
4.4
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165E
9
(S)-Mandelate
-
pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted
13.2
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165G
18.4
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165M
19.2
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme G81A
24
(S)-Mandelate
-
pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus
49
(S)-Mandelate
-
pH 7.5, 25°C, electron acceptor: cytochrome c
66
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277K
66
(S)-Mandelate
mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5
73
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R277K
109
(S)-Mandelate
-
pH 7.5, 25°C, electron acceptor: ferricyanide
120
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme R165K
134
(S)-Mandelate
-
pH 7.5, 4°C
174
(S)-Mandelate
-
pH 7.5, wild-type enzyme
205
(S)-Mandelate
-
pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
205
(S)-Mandelate
-
pH 7.5, 20°C, mutant enzyme MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with 205 residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
270
(S)-Mandelate
-
pH 7.5, 20°C, wild-type enzyme
290
(S)-Mandelate
-
pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, wild-type enzyme
360
(S)-Mandelate
-
pH 7.5, 20°C
360
(S)-Mandelate
-
pH 7.5, 20°C, wild-type enzyme
360
(S)-Mandelate
wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5
3.9
2-Hydroxy-3-butynoate
-
pH 7.5, 20°C, wild-type enzyme
6.6
2-Hydroxy-3-butynoate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
14.8
2-Hydroxy-3-butynoate
-
pH 7.5, 20°C, mutant enzyme G81A
0.1
2-Hydroxybutyrate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.1
2-Hydroxybutyrate
-
pH 7.5, 20°C, wild-type enzyme
0.37
2-Hydroxybutyrate
-
pH 7.5, 20°C, mutant enzyme G81A
0.19
2-hydroxyhexanoate
-
pH 7.5, 20°C, mutant enzyme G81A
0.34
2-hydroxyhexanoate
-
pH 7.5, 20°C, wild-type enzyme
0.48
2-hydroxyhexanoate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.48
2-hydroxyisocaproate
-
pH 7.5, 20°C, mutant enzyme G81A
0.8
2-hydroxyisocaproate
-
pH 7.5, 20°C, wild-type enzyme
1.28
2-hydroxyisocaproate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.26
2-Hydroxyoctanoate
-
pH 7.5, 20°C, mutant enzyme G81A
0.3
2-Hydroxyoctanoate
mutant G81A
0.42
2-Hydroxyoctanoate
mutant G81A of chimera MDH-GOX2
0.5
2-Hydroxyoctanoate
wild-type enzyme
0.5
2-Hydroxyoctanoate
-
pH 7.5, 20°C, wild-type enzyme
0.96
2-Hydroxyoctanoate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
1
2-Hydroxyoctanoate
chimera MDH-GOX2
0.27
2-hydroxyvalerate
-
pH 7.5, 20°C, mutant enzyme G81A
0.36
2-hydroxyvalerate
-
pH 7.5, 20°C, wild-type enzyme
0.5
2-hydroxyvalerate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.27
3-indolelactate
-
pH 7.5, 20°C, mutant enzyme G81A
0.3
3-indolelactate
mutant G81A
1
3-indolelactate
wild-type enzyme
1
3-indolelactate
-
pH 7.5, 20°C, wild-type enzyme
1.4
3-indolelactate
mutant G81A of chimera MDH-GOX2
3.13
3-indolelactate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
3.85
3-indolelactate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
3.9
3-indolelactate
chimera MDH-GOX2
0.15
3-Phenyllactate
-
pH 7.5, 20°C, mutant enzyme G81A
0.52
3-Phenyllactate
-
pH 7.5, 20°C, wild-type enzyme
0.87
3-Phenyllactate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
68
4-chloro-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
116
4-chloro-DL-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
9.3
4-chloromandelate
-
pH 7.5, 20°C, mutant enzyme G81A
334
4-chloromandelate
-
pH 7.5, 20°C, wild-type enzyme
155
DL-[2-1H]-mandelate
-
pH 7.5, 25°C, cosubstrate cytochrome c, LMDH holoenzyme
300
DL-[2-1H]-mandelate
-
pH 7.5, 25°C, cosubstrate ferricyanide, LMDH holoenzyme
316
DL-[2-1H]-mandelate
-
pH 7.5, 25°C, cosubstrate ferricyanide, L-MDH flavin domain
88
DL-[2-2H]-mandelate
-
pH 7.5, 25°C, cosubstrate ferricyanide, LMDH holoenzyme
92
DL-[2-2H]-mandelate
-
pH 7.5, 25°C, cosubstrate cytochrome, LMDH holoenzyme
93
DL-[2-2H]-mandelate
-
pH 7.5, 25°C, cosubstrate: ferricyanide
99
DL-[2-2H]-mandelate
-
pH 7.5, 25°C, cosubstrate ferricyanide, L-MDH flavin domain
0.3
ethyl-(S)-mandelate
mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5
2.6
ethyl-(S)-mandelate
mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5
204
ethyl-(S)-mandelate
wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5
1.2
indoleglycolate
-
pH 7.5, 20°C, mutant enzyme G81A
38.5
indoleglycolate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
122
indoleglycolate
-
pH 7.5, 20°C, wild-type enzyme
2.3
Mandelate
mutant G81A of chimera MDH-GOX2
15.2
Mandelate
-
pH 7.5, 20°C, mutant enzyme G81A
15.2
Mandelate
mutant G81A
195
Mandelate
-
pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
205
Mandelate
chimera MDH-GOX2
350
Mandelate
wild-type enzyme
350
Mandelate
-
pH 7.5, 20°C, wild-type enzyme
2.3
methyl-(S)-mandelate
mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5
2.5
methyl-(S)-mandelate
mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5
151
methyl-(S)-mandelate
wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5
0.03
O2
-
pH 7.5, 20°C, mutant enzyme MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with 205 residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.05
O2
-
pH 7.5, 20°C, mutant enzyme G81D
0.07
O2
-
pH 7.5, 20°C, mutant enzyme G81V
0.22
O2
-
pH 7.5, 20°C, mutant enzyme, G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH
0.61
O2
-
pH 7.5, 20°C, mutant enzyme G81S
1.2
O2
-
pH 7.5, 20°C, wild-type enzyme
3.4
O2
-
pH 7.5, 20°C, mutant enzyme G81A
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G81D
-
extreme low activity, reduction in activity is due to the decrease in electrophilicity of the FMN
G81S
-
the rate of the first half-reaction is slower than the wild-type rate. The rate of the first half-reaction is slower than the wild-type rate. Affinity for O2 increases 10-15fold
G81V
-
extreme low activity, reduction in activity is due to the decrease in electrophilicity of the FMN
H274A
-
inactive mutant, activity can partially be restored by the addition of exogenous imidazole
H274G
-
inactive mutant, activity can be restored by the addition of exogenous imidazole
R165E
-
mutant is less stable than wild-type enzyme, mutant enzyme is only partially reduced by (S)-mandelate. 81.8fold decrease in kcat for (S)-mandelate, 199fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165G
-
mutant is less stable than wild-type enzyme, mutant enzyme is only partially reduced by (S)-mandelate. 27.3fold decrease in kcat for (S)-mandelate, 48.3fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165G/R277G
-
no activity. Double mutant is less stable than single Arg165 mutant in term of long-term storage
R165G/R277K
-
double mutant is less stable than single Arg165 mutant in term of long-term storage. 9000fold decrease in kcat for (S)-mandelate, 261.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165K
-
mutant is less stable than wild-type enzyme, mutant enzyme is fully reduced on addition of (S)-mandelate. 3fold decrease in kcat for (S)-mandelate, 12.5fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165K/R277G
-
no activity. Double mutant is less stable than single Arg165 mutant in term of long-term storage
R165K/R277K
-
double mutant is less stable than single Arg165 mutant in term of long-term storage. 327fold decrease in kcat for (S)-mandelate, 126.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R165M
-
mutant is less stable than wild-type enzyme, mutant enzyme is fully reduced on addition of (S)-mandelate. 19.6fold decrease in kcat for (S)-mandelate, 36.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R277H
-
kcat for (S)-mandelate is 1000fold lower than wild-type value, KM-value for (S)-mandelate is 608fold higher than wild-type value
R277L
-
kcat for (S)-mandelate is 421fold lower fold than wild-type value, KM-value for (S)-mandelate is 392fold higher than wild-type value
G81A
-
higher specificity for small substrates, compared to that of wild-type enzyme, the affinity for (S)-mandelate is relatively unchanged. The rate of the first half-reaction is slower than the wild-type rate. 2fold increase in oxidative half-reaction. Affinity for oxygen increases 10-15fold
G81A
mutation in the catalytically similar chimera MDH-GOX2 (mandelate dehydrogenase/glycolate oxidase), mutant has lower reactivity with substrate
G81A
wild type, mutant has lower reactivity with substrate
R277G
-
1565fold decrease in kcat for (S)-mandelate, 141fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R277G
-
kcat for (S)-mandelate is 178fold lower than wild-type value, KM-value for (S)-mandelate is 160fold higher than wild-type value, KM-value for {(S)-3-phenyllactate is 1.6fold lower than wild-type value
R277G
reduced activity compared to the wild type enzyme, the mutation at Arg277 has no influence on the binding affinity of ester substrates
R277K
-
5.5 fold decrease in kcat for (S)-mandelate, 46.7fold increase in KM-value for (S)-mandelate compared to wild-type enzyme
R277K
-
kcat for (S)-mandelate is 3.7fold lower than wild-type value, KM-value for (S)-mandelate is 36.7fold higher than wild-type value
R277K
reduced activity compared to the wild type enzyme, the mutation at Arg277 has no influence on the binding affinity of ester substrates
additional information
-
chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach is soluble and retains partial catalytic activity (about 1%) using (S)-mandelate as substrate. The activities of the soluble mutant enzymes (S)-mandelate dehydrogenase with residues 2-4 deleted and (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus are nearly the same when (S)-phenyllactate is used as substrate
additional information
-
MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach. G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH
additional information
-
MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach. This mutant is very similar to the wild-type membrane-bound enzyme in its spectroscopic properties, substrate specificity, catalytic activity, kinetic mechanism, and lack of reactivity toeards oxygen. It should prove to be a highly useful model for structural studies of MDH
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Smekal, O.; Yasin, M.; Fewson, C.A.; Reid, G.A.; Chapman, S.K.
L-mandelate dehydrogenase from Rhodotorula graminis: comparisons with the L-lactate dehydrogenase (flavocytochrome b2) from Saccharomyces cerevisiae
Biochem. J.
290
103-107
1993
Rhodotorula graminis
brenda
Smekal, O.; Reid, G.A.; Chapman, S.K.
Substrate analogues as probes of the catalytic mechanism of L-mandelate dehydrogenase from Rhodotorula graminis
Biochem. J.
297
647-652
1994
Rhodotorula graminis
brenda
Illias, R.M.; Sinclair, R.; Robertson, D.; Neu, A.; Chapman, S.K.; Reid, G.A.
L-Mandelate dehydrogenase from Rhodotorula graminis: cloning, sequencing and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain
Biochem. J.
333
107-115
1998
Rhodotorula graminis
brenda
Mitra, B.; Gerlt, J.A.; Babbitt, P.C.; Koo, C.W.; Kenyon, G.L.; Joseph, D.; Petsko, G.A.
A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida
Biochemistry
32
12959-12967
1993
Pseudomonas putida
brenda
Xu, Y.; Mitra, B.
A highly active, soluble mutant of the membrane-associated (S)-mandelate dehydrogenase from Pseudomonas putida
Biochemistry
38
12367-12376
1999
Pseudomonas putida
brenda
Lehoux, I.E.; Mitra, B.
(S)-Mandelate dehydrogenase from Pseudomonas putida: mutations of the catalytic base histidine-274 and chemical rescue of activity
Biochemistry
38
9948-9955
1999
Pseudomonas putida
brenda
Lehoux, I.E.; Mitra, B.
Role of arginine 277 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate binding and transition state stabilization
Biochemistry
39
10055-10065
2000
Pseudomonas putida
brenda
Sukumar, N.; Xu, Y.; Gatti, D.L.; Mitra, B.; Mathews, F.S.
Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase
Biochemistry
40
9870-9878
2001
Pseudomonas putida (P20932), Pseudomonas putida
brenda
Xu, Y.; Dewanti, A.R.; Mitra, B.
Arginine 165/arginine 277 pair in (S)-mandelate dehydrogenase from Pseudomonas putida: role in catalysis and substrate binding
Biochemistry
41
12313-12319
2002
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Pseudomonas putida
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Pseudomonas putida
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1999
Pseudomonas putida (P20932), Pseudomonas putida
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Dewanti, A.R.; Xu, Y.; Mitra, B.
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Biochemistry
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Pseudomonas putida (P20932), Pseudomonas putida
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Pseudomonas putida (P20932), Pseudomonas putida
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Pseudomonas putida, Pseudomonas putida DSM 291
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Escherichia coli
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Pseudomonas putida (P20932), Pseudomonas putida
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