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(2R)-2-(4-bromophenyl)-2-hydroxyacetamide
?
-
Substrates: 22% of the activity with (R)-mandelate
Products: -
?
(2R)-2-furyl(hydroxy)acetic acid
?
-
Substrates: 24% of the activity with (R)-mandelate
Products: -
?
(2R)-2-hydroxy-2-phenylacetamide
?
-
Substrates: 15% of the activity with (R)-mandelate
Products: -
?
(2R)-2-hydroxy-3-(1-H-imidazol-1-yl)propanoic acid
?
-
Substrates: 5.4% of the activity with (R)-mandelate
Products: -
?
(2R)-2-hydroxypentanoic acid
?
-
Substrates: 1% of the activity with (R)-mandelate
Products: -
?
(2R)-2-naphthylglycolate
(2S)-2-naphthylglycolate
Substrates: a non-natural substrate
Products: -
?
(2R)-3-furyl(hydroxy)acetic acid
?
-
Substrates: 38% of the activity with (R)-mandelate
Products: -
?
(2R)-cyclohex-1-en-1-yl(hydroxy)acetic acid
?
-
Substrates: 50% of the activity with (R)-mandelate
Products: -
?
(2R)-hydroxy(2-naphthyl)acetic acid
?
-
Substrates: 26% of the activity with (R)-mandelate
Products: -
?
(2S)-hydroxy(2-thienyl)acetic acid
?
-
Substrates: 59% of the activity with (R)-mandelate
Products: -
?
(R)-(E)-2-hydroxy-3-pentenoic acid
?
-
Substrates: 36% of the activity with (R)-mandelate
Products: -
?
(R)-(E)-2-hydroxy-4-phenyl-3-butenoic acid
?
-
Substrates: 53% of the activity with (R)-mandelate
Products: -
?
(R)-2-chloromandelate
(S)-2-chloromandelate
(R)-2-naphthylglycolate
(S)-2-naphthylglycolate
(R)-2-naphtylglycolate
(S)-2-naphthylglycolate
Substrates: -
Products: -
r
(R)-3-chloromandelate
(S)-3-chloromandelate
Substrates: a non-natural substrate
Products: -
?
(R)-lactate
(S)-lactate
Substrates: -
Products: -
?
(R)-mandelamide
(S)-mandelamide
Substrates: a non-natural substrate
Products: -
?
(R)-mandelate
(S)-mandelate
(R)-trifluorolactate
trifluorolactate
Substrates: racemization
Products: -
?
(S)-2-chloromandelate
(R)-2-chloromandelate
(S)-2-hydroxy-3-butenoic acid
(R)-2-hydroxy-3-butenoic acid
(S)-2-naphthylglycolate
(R)-2-naphthylglycolate
(S)-atrolactate
(R)-atrolactate
Substrates: -
Products: -
r
(S)-lactate
(R)-lactate
Substrates: -
Products: -
?
(S)-mandelate
(R)-mandelate
(S)-mandelic acid amide
(R)-mandelic acid amide
-
Substrates: activity is enhanced by an electron-withdrawing substituent in the phenyl moiety
Products: -
?
(S)-trifluorolactate
(R)-trifluorolactate
(S)-vinylglycolate
(R)-vinylglycolate
Substrates: two-step quite symmetric process through a dianionic enolic intermediate that is formed after the abstraction of the alpha-protein of vinylglycolate by a basic enzymatic residue and is then reprotonated by another residue
Products: -
?
2-hydroxybut-3-enoic acid
?
-
Substrates: 35% of the activity with (R)-mandelate
Products: -
?
4-bromo-(R)-mandelate
4-bromo-(S)-mandelate
-
Substrates: 376% of the activity with (R)-mandelate
Products: -
r
4-bromo-D-mandelate
4-bromo-L-mandelate
4-chloro-(R)-mandelate
4-chloro-(S)-mandelate
-
Substrates: 326% of the activity with (R)-mandelate
Products: -
r
4-chloro-D-mandelate
4-chloro-L-mandelate
4-fluoro-(R)-mandelate
4-fluoro-(S)-mandelate
-
Substrates: 96% of the activity with (R)-mandelate
Products: -
r
4-hydroxy-(R)-mandelate
4-hydroxy-(S)-mandelate
-
Substrates: 45% of the activity with (R)-mandelate
Products: -
r
4-hydroxy-D-mandelate
4-hydroxy-L-mandelate
4-methoxy-(R)-mandelate
4-methoxy-(S)-mandelate
-
Substrates: 17% of the activity with (R)-mandelate
Products: -
r
4-methoxy-D-mandelate
4-methoxy-L-mandelate
-
Substrates: -
Products: -
?
5-chloro-(R)-mandelate
5-chloro-(S)-mandelate
-
Substrates: 61% of the activity with (R)-mandelate
Products: -
r
p-(bromomethyl)mandelate
p-(methyl)benzoylformate + Br-
p-hydroxy-D-mandelate
p-hydroxy-L-mandelate
-
Substrates: -
Products: -
?
S-mandelate
R-mandelate
-
Substrates: -
Products: -
?
additional information
?
-
(R)-2-chloromandelate
(S)-2-chloromandelate
Substrates: -
Products: -
r
(R)-2-chloromandelate
(S)-2-chloromandelate
Substrates: -
Products: -
r
(R)-2-naphthylglycolate
(S)-2-naphthylglycolate
Substrates: -
Products: -
?
(R)-2-naphthylglycolate
(S)-2-naphthylglycolate
Substrates: -
Products: -
r
(R)-2-naphthylglycolate
(S)-2-naphthylglycolate
-
Substrates: -
Products: -
r
(R)-mandelate
(S)-mandelate
-
Substrates: -
Products: -
?
(R)-mandelate
(S)-mandelate
-
Substrates: -
Products: -
r
(R)-mandelate
(S)-mandelate
Substrates: -
Products: -
?
(R)-mandelate
(S)-mandelate
-
Substrates: -
Products: -
?
(R)-mandelate
(S)-mandelate
Substrates: -
Products: -
r
(R)-mandelate
(S)-mandelate
Substrates: wild-type enzyme shows slightly higher affinity for (S)-mandelate than for (R)-mandelate, but catalyzes the turnover of (R)-mandelate slightly more rapidly
Products: -
r
(S)-2-chloromandelate
(R)-2-chloromandelate
Substrates: binding structure
Products: -
r
(S)-2-chloromandelate
(R)-2-chloromandelate
Substrates: binding structure
Products: -
r
(S)-2-hydroxy-3-butenoic acid
(R)-2-hydroxy-3-butenoic acid
-
Substrates: -
Products: -
?
(S)-2-hydroxy-3-butenoic acid
(R)-2-hydroxy-3-butenoic acid
-
Substrates: maximal racemization rate is 35% relative to mandelate
Products: -
?
(S)-2-naphthylglycolate
(R)-2-naphthylglycolate
Substrates: -
Products: -
r
(S)-2-naphthylglycolate
(R)-2-naphthylglycolate
Substrates: racemisation
Products: -
r
(S)-mandelate
(R)-mandelate
-
Substrates: -
Products: -
?
(S)-mandelate
(R)-mandelate
Substrates: -
Products: -
?
(S)-mandelate
(R)-mandelate
-
Substrates: -
Products: -
?
(S)-mandelate
(R)-mandelate
Substrates: -
Products: -
?
(S)-mandelate
(R)-mandelate
-
Substrates: -
Products: -
?
(S)-mandelate
(R)-mandelate
Substrates: -
Products: -
?
(S)-mandelate
(R)-mandelate
Substrates: -
Products: -
r
(S)-mandelate
(R)-mandelate
Substrates: mechanism
Products: -
?
(S)-mandelate
(R)-mandelate
Substrates: catalyzes the Mg2+-dependent 1,1-proton transfer that interconverts the enantiomers, catalysis is done via a two-base mechanism
Products: -
r
(S)-trifluorolactate
(R)-trifluorolactate
Substrates: -
Products: -
?
(S)-trifluorolactate
(R)-trifluorolactate
Substrates: racemization
Products: -
?
4-bromo-D-mandelate
4-bromo-L-mandelate
-
Substrates: -
Products: -
?
4-bromo-D-mandelate
4-bromo-L-mandelate
-
Substrates: -
Products: -
?
4-chloro-D-mandelate
4-chloro-L-mandelate
-
Substrates: -
Products: -
?
4-chloro-D-mandelate
4-chloro-L-mandelate
-
Substrates: -
Products: -
?
4-hydroxy-D-mandelate
4-hydroxy-L-mandelate
-
Substrates: -
Products: -
?
4-hydroxy-D-mandelate
4-hydroxy-L-mandelate
-
Substrates: -
Products: -
?
D-mandelate
L-mandelate
-
3649, 4814, 285167, 285168, 285169, 285170, 285171, 285172, 285173, 285174, 285175, 285176, 285177, 285179, 285180, 285181, 285182, 285184, 285186, 285187, 285188, 285189, 285190, 285191, 285192, 285193, 285194 Substrates: -
Products: -
?
D-mandelate
L-mandelate
-
Substrates: -
Products: -
r
D-mandelate
L-mandelate
Substrates: -
Products: -
?
D-mandelate
L-mandelate
-
Substrates: inducible enzyme
Products: -
?
D-mandelate
L-mandelate
-
Substrates: strictly inducible enzyme. Inducers: D-mandelate, L-mandelate, benzoylformate
Products: -
?
D-mandelate
L-mandelate
-
Substrates: first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid
Products: -
?
D-mandelate
L-mandelate
-
Substrates: first enzyme of pathway of oxidation of D,L-mandelate that permits certain strains of Pseudomonas putida to use mandelate as a sole source of carbon and energy
Products: -
?
D-mandelate
L-mandelate
-
Substrates: -
Products: -
?
D-mandelate
L-mandelate
-
Substrates: inducible enzyme
Products: -
?
D-mandelate
L-mandelate
-
Substrates: -
Products: -
?
p-(bromomethyl)mandelate
p-(methyl)benzoylformate + Br-
-
Substrates: -
Products: -
?
p-(bromomethyl)mandelate
p-(methyl)benzoylformate + Br-
-
Substrates: -
Products: i.e. alpha-carboxy-alpha-hydroxy-p-xylylene
?
additional information
?
-
-
Substrates: not racemized: 4-hydroxy-3-methoxymandelate, 3,4-dihydroxymandelate
Products: -
?
additional information
?
-
-
Substrates: efficient racemization of 2-hydroxy-2-heteroaryl-acetic acid derivatives. Steric limitations for aryl-substituted mandelate derivatives are elucidated to be particularly striking for o-substituents, whereas m- and p-analogues are freely accepted as well as heteroaryl and naphthyl analogs. The electronic character of substituents is found to play an important role: whereas electron-withdrawing substituents dramatically enhance the racemization rates, electron-donating analogs cause a depletion
Products: -
?
additional information
?
-
-
Substrates: no activity with phenyl glycine and mandelic acid hydrazide
Products: -
?
additional information
?
-
Substrates: mandelate racemase catalyzes the Mg2+-dependent 1,1-proton transfer that interconverts the enantiomers of mandelate
Products: -
?
additional information
?
-
-
Substrates: mandelate racemase catalyzes the Mg2+-dependent 1,1-proton transfer that interconverts the enantiomers of mandelate
Products: -
?
additional information
?
-
Substrates: substrate recognition and binding method, overview. Mandelate racemase from Pseudomonas putida catalyzes the interconversion of the enantiomers of mandelic acid and a variety of aryl- and heteroaryl-substituted mandelate derivatives. beta,gamma-Unsaturation is not an absolute requirement for catalysis and that mandelate racemase can bind and catalyze the racemization of (S)- and (R)-trifluorolactate. The enzyme catalyzes hydrogen-deuterium exchange at the alpha-postion of trifluorolactate
Products: -
?
additional information
?
-
-
Substrates: substrate recognition and binding method, overview. Mandelate racemase from Pseudomonas putida catalyzes the interconversion of the enantiomers of mandelic acid and a variety of aryl- and heteroaryl-substituted mandelate derivatives. beta,gamma-Unsaturation is not an absolute requirement for catalysis and that mandelate racemase can bind and catalyze the racemization of (S)- and (R)-trifluorolactate. The enzyme catalyzes hydrogen-deuterium exchange at the alpha-postion of trifluorolactate
Products: -
?
additional information
?
-
Substrates: enzyme activity detection in the high-throughput screening method of enzymes involving the racemization of (S)-2-chloromandelate, method evaluation, overview
Products: -
?
additional information
?
-
Substrates: enzyme activity detection in the high-throughput screening method of enzymes involving the racemization of (S)-2-chloromandelate, method evaluation, overview
Products: -
?
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1.2 - 4.2
(2R)-2-naphthylglycolate
9.94 - 15.97
(R)-2-chloromandelate
3.5
(R)-2-hydroxy-3-butenoic acid
-
-
0.35 - 4.4
(R)-2-naphthylglycolate
1.1 - 4.4
(R)-2-naphtylglycolate
-
1.27 - 3.92
(R)-3-chloromandelate
1.13 - 1.24
(R)-mandelamide
1.2
(R)-trifluorolactate
pH 7.5, 25°C, recombinant wild-type enzyme
10.62 - 19.91
(S)-2-chloromandelate
0.41 - 2.9
(S)-2-naphthylglycolate
1.74
(S)-trifluorolactate
pH 7.5, 25°C, recombinant wild-type enzyme
0.256
4-Bromo-D-mandelate
-
-
0.29
4-Hydroxy-D-mandelate
-
-
0.33
4-Methoxy-D-mandelate
-
-
additional information
additional information
-
1.2
(2R)-2-naphthylglycolate
pH 7.5, 25°C, wild-type enzyme
1.6
(2R)-2-naphthylglycolate
pH 7.5, 25°C, mutant V29L
3.5
(2R)-2-naphthylglycolate
pH 7.5, 25°C, wild-type enzyme, in presence of 20 mM MgCl2
4.2
(2R)-2-naphthylglycolate
pH 7.5, 25°C, mutant V22I
9.94
(R)-2-chloromandelate
mutant V29I/Y45F, pH 7.5, 25°C
11.66
(R)-2-chloromandelate
mutant Y45F, pH 7.5, 25°C
11.99
(R)-2-chloromandelate
mutant V29I, pH 7.5, 25°C
14.52
(R)-2-chloromandelate
mutant V22I/V29I/Y54F, pH 7.5, 25°C
14.82
(R)-2-chloromandelate
wild-type enzyme, pH 7.5, 25°C
15.1
(R)-2-chloromandelate
mutant V22I/V29I, pH 7.5, 25°C
15.51
(R)-2-chloromandelate
mutant V22I, pH 7.5, 25°C
15.97
(R)-2-chloromandelate
mutant V22I/Y45F, pH 7.5, 25°C
0.35
(R)-2-naphthylglycolate
mutant enzyme F52W/Y54W
0.46
(R)-2-naphthylglycolate
wild-type enzyme
0.46
(R)-2-naphthylglycolate
25°C, pH 7.5
1.1
(R)-2-naphthylglycolate
mutant V29F, pH 7.5, 25°C
1.2
(R)-2-naphthylglycolate
wild-type, pH 7.5, 25°C
1.3
(R)-2-naphthylglycolate
mutant V26L, pH 7.5, 25°C
1.6
(R)-2-naphthylglycolate
mutant V29L, pH 7.5, 25°C
1.7
(R)-2-naphthylglycolate
mutant V26F, pH 7.5, 25°C
1.8
(R)-2-naphthylglycolate
mutant V29A, pH 7.5, 25°C
1.9
(R)-2-naphthylglycolate
mutant A25V, pH 7.5, 25°C
1.9
(R)-2-naphthylglycolate
mutant V22A, pH 7.5, 25°C
2.1
(R)-2-naphthylglycolate
mutant V26A, pH 7.5, 25°C
2.2
(R)-2-naphthylglycolate
mutant V22F, pH 7.5, 25°C
3.2
(R)-2-naphthylglycolate
mutant T24S, pH 7.5, 25°C
3.5
(R)-2-naphthylglycolate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
3.7
(R)-2-naphthylglycolate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
4.2
(R)-2-naphthylglycolate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
4.4
(R)-2-naphthylglycolate
mutant V26A/V29L, pH 7.5, 25°C
1.1
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F
-
1.2
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, wild-type
-
1.3
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26L
-
1.6
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29L
-
1.7
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26F
-
1.8
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A
-
1.9
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V
-
1.9
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22A
-
2.1
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A
-
2.2
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22F
-
3.2
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant T24S
-
3.5
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 20 mM Mg2+, wild-type
-
3.7
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I/V29L
-
4.2
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I
-
4.4
(R)-2-naphtylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
-
1.27
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V29L
1.6 - 2
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54L
1.7 - 2
(R)-3-chloromandelate
pH 7.5, 25°C, mutant L319F
1.87
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26L
1.89
(R)-3-chloromandelate
pH 7.5, 25°C, wild-type enzyme
1.9
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26S
1.95
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54F
1.99
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I/Y54I
2.12
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V22I
2.17
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54V
2.22
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54A
2.4
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V22L
2.46
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I
3.02
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54I
3.92
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I/Y54V
1.13
(R)-mandelamide
pH 7.5, 25°C, wild-type enzyme
1.24
(R)-mandelamide
pH 7.5, 25°C, mutant V26L
0.29
(R)-mandelate
mutant enzyme F52W/Y64W
0.34
(R)-mandelate
-
wild type
0.4
(R)-mandelate
-
wild type enzyme
0.44
(R)-mandelate
-
pH 7.5
0.7
(R)-mandelate
wild-type enzyme
0.81
(R)-mandelate
-
25°C, pH 7.5, wild-type enzyme
0.9
(R)-mandelate
mutant V29F, pH 7.5, 25°C
0.9
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F
0.91
(R)-mandelate
mutant V26A, pH 7.5, 25°C
0.91
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A
0.95
(R)-mandelate
-
pH 6.3
1.1
(R)-mandelate
mutant enzyme Y54W
1.1
(R)-mandelate
mutant A25V, pH 7.5, 25°C
1.1
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V
1.2
(R)-mandelate
pH 7.5, 25°C, recombinant wild-type enzyme
1.2
(R)-mandelate
-
pH 7.5, 25°C, recombinant wild-type enzyme
1.2
(R)-mandelate
wild-type, pH 7.5, 25°C
1.2
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, wild-type
1.4
(R)-mandelate
mutant V26A/V29L, pH 7.5, 25°C
1.4
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
1.47
(R)-mandelate
pH 7.5 at 25°C, 20 mM Mg2+, wild-type
1.47
(R)-mandelate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
1.5
(R)-mandelate
D270N mutant
1.7
(R)-mandelate
mutant V26L, pH 7.5, 25°C
1.7
(R)-mandelate
mutant V29L, pH 7.5, 25°C
1.7
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26L
1.7
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29L
1.8
(R)-mandelate
mutant V26F, pH 7.5, 25°C
1.8
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26F
2.02
(R)-mandelate
-
pH 8.7
2.4
(R)-mandelate
-
E317Q mutant
2.5
(R)-mandelate
mutant enzyme F52W
2.8
(R)-mandelate
mutant T24S, pH 7.5, 25°C
2.8
(R)-mandelate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
2.8
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant T24S
2.8
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I/V29L
2.9
(R)-mandelate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
2.9
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I
4.4
(R)-mandelate
mutant V22A, pH 7.5, 25°C
4.4
(R)-mandelate
mutant V22F, pH 7.5, 25°C
4.4
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22A
4.4
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22F
5
(R)-mandelate
mutant V29A, pH 7.5, 25°C
5
(R)-mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A
5.4
(R)-mandelate
-
25°C, pH 7.5, mutant enzyme N197A
10.62
(S)-2-chloromandelate
mutant V29I/Y45F, pH 7.5, 25°C
10.9
(S)-2-chloromandelate
mutant Y45F, pH 7.5, 25°C
13.74
(S)-2-chloromandelate
mutant V22I/V29I, pH 7.5, 25°C
14.19
(S)-2-chloromandelate
mutant V22I/Y45F, pH 7.5, 25°C
14.35
(S)-2-chloromandelate
mutant V29I, pH 7.5, 25°C
17.74
(S)-2-chloromandelate
wild-type enzyme, pH 7.5, 25°C
17.94
(S)-2-chloromandelate
mutant V22I/V29I/Y54F, pH 7.5, 25°C
19.91
(S)-2-chloromandelate
mutant V22I, pH 7.5, 25°C
0.41
(S)-2-naphthylglycolate
wild-type enzyme
0.41
(S)-2-naphthylglycolate
25°C, pH 7.5
0.55
(S)-2-naphthylglycolate
mutant V29F, pH 7.5, 25°C
0.55
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F
0.62
(S)-2-naphthylglycolate
mutant V22F, pH 7.5, 25°C
0.62
(S)-2-naphthylglycolate
mutant V26L, pH 7.5, 25°C
0.62
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22F
0.62
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26L
0.74
(S)-2-naphthylglycolate
mutant V26A, pH 7.5, 25°C
0.74
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A
0.8
(S)-2-naphthylglycolate
mutant V29L, pH 7.5, 25°C
0.8
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29L
0.93
(S)-2-naphthylglycolate
mutant V29A, pH 7.5, 25°C
0.93
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A
1
(S)-2-naphthylglycolate
wild-type, pH 7.5, 25°C
1
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, wild-type
1.1
(S)-2-naphthylglycolate
mutant V26F, pH 7.5, 25°C
1.1
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26F
1.4
(S)-2-naphthylglycolate
mutant T24S, pH 7.5, 25°C
1.4
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant T24S
1.5
(S)-2-naphthylglycolate
mutant enzyme F52W/Y54W
1.55
(S)-2-naphthylglycolate
mutant V22A, pH 7.5, 25°C
1.55
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22A
1.6
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 20 mM Mg2+, wild-type
1.6
(S)-2-naphthylglycolate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
1.67
(S)-2-naphthylglycolate
mutant A25V, pH 7.5, 25°C
1.67
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V
1.7
(S)-2-naphthylglycolate
mutant V26A/V29L, pH 7.5, 25°C
1.7
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
2.4
(S)-2-naphthylglycolate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
2.4
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
2.9
(S)-2-naphthylglycolate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
2.9
(S)-2-naphthylglycolate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I
0.3
(S)-Mandelate
recombinant mandelate racemase, putative misfolded form with N-terminal hexahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
0.35
(S)-Mandelate
-
wild type
0.54
(S)-Mandelate
wild-type enzyme
0.59
(S)-Mandelate
-
mutant K166R
0.6
(S)-Mandelate
mutant V29L, pH 7.5, 25°C
0.6
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29L
0.6
(S)-Mandelate
recombinant mrIII fusion protein bearing an N-terminal StrepII-tag and a C-terminal decahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
0.62
(S)-Mandelate
-
25°C, pH 7.5, wild-type enzyme
0.8
(S)-Mandelate
recombinant mandelate racemase represents correctly folded enzyme with N-terminal hexahistidine tag, in Na-HEPES buffer (0.1 M, pH 7.5),3.3 mM MgCl2
0.97
(S)-Mandelate
wild-type, pH 7.5, 25°C
0.97
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, wild-type
1
(S)-Mandelate
pH 7.5, 25°C, recombinant wild-type enzyme
1
(S)-Mandelate
-
pH 7.5, 25°C, recombinant wild-type enzyme
1.07
(S)-Mandelate
pH 7.5 at 25°C, 20 mM Mg2+, wild-type
1.07
(S)-Mandelate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
1.1
(S)-Mandelate
mutant V26A/V29L, pH 7.5, 25°C
1.1
(S)-Mandelate
mutant V26F, pH 7.5, 25°C
1.1
(S)-Mandelate
mutant V26L, pH 7.5, 25°C
1.1
(S)-Mandelate
mutant V29F, pH 7.5, 25°C
1.1
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
1.1
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26F
1.1
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26L
1.1
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F
1.1
(S)-Mandelate
recombinant mandelate racemase, replacement of the N-terminal hexahistidine tag by a StrepII-tag appears to ameliorate the folding problem yielding a single enzyme species, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
1.4
(S)-Mandelate
-
mutant K166R
1.4
(S)-Mandelate
-
25°C, pH 7.5, mutant enzyme N197A
1.5
(S)-Mandelate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
1.5
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
1.7
(S)-Mandelate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
1.7
(S)-Mandelate
mutant V26A, pH 7.5, 25°C
1.7
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I
1.7
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A
1.8
(S)-Mandelate
mutant A25V, pH 7.5, 25°C
1.8
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V
2.1
(S)-Mandelate
D270N mutant
2.9
(S)-Mandelate
mutant enzyme Y54W
3
(S)-Mandelate
mutant T24S, pH 7.5, 25°C
3
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant T24S
3.3
(S)-Mandelate
mutant enzyme F52W
3.4
(S)-Mandelate
mutant V22A, pH 7.5, 25°C
3.4
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22A
3.8
(S)-Mandelate
mutant enzyme F52W/Y64W
3.9
(S)-Mandelate
mutant V29A, pH 7.5, 25°C
3.9
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A
6.1
(S)-Mandelate
mutant V22F, pH 7.5, 25°C
6.1
(S)-Mandelate
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22F
0.1
D(-)-mandelate
-
in presence of 1 mM Mg2+
0.1
D(-)-mandelate
-
4-chloro-D-mandelate
0.093
D-mandelate
-
-
0.25
D-mandelate
-
L-mandelate
0.04
Mg2+
pH 7.5, mutant V22A, addition of either 10 mM (R)- or (S)-mandelate
0.04
Mg2+
pH 7.5, mutant V22F, addition of either 10 mM (R)- or (S)-mandelate
0.05
Mg2+
pH 7.5, mutant V26F, addition of either 10 mM (R)- or (S)-mandelate
0.08
Mg2+
pH 7.5, mutant V29A, addition of either 10 mM (R)- or (S)-mandelate
0.12
Mg2+
pH 7.5, mutant V26L, addition of either 10 mM (R)- or (S)-mandelate
0.15
Mg2+
pH 7.5, mutant V26A, addition of either 10 mM (R)- or (S)-mandelate
0.22
Mg2+
pH 7.5, mutant V29F, addition of either 10 mM (R)- or (S)-mandelate
0.29
Mg2+
pH 7.5, mutant T24S, addition of either 10 mM (R)- or (S)-mandelate
0.34
Mg2+
pH 7.5, wild-type, addition of either 10 mM (R)- or (S)-mandelate
0.47
Mg2+
pH 7.5, mutant V29L, addition of either 10 mM (R)- or (S)-mandelate
0.51
Mg2+
pH 7.5, mutant V26A/V29L, addition of either 10 mM (R)- or (S)-mandelate
0.64
Mg2+
pH 7.5, mutant A25V, addition of either 10 mM (R)- or (S)-mandelate
3.8
Mg2+
pH 7.5, mutant V22I, addition of either 10 mM (R)- or (S)-mandelate
4.2
Mg2+
pH 7.5, mutant V22I/V29L, addition of either 10 mM (R)- or (S)-mandelate
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
46 - 147
(2R)-2-naphthylglycolate
0.9 - 2.6
(R)-2-chloromandelate
240
(R)-2-hydroxy-3-butenoic acid
-
-
5.4 - 147
(R)-2-naphthylglycolate
5.4 - 147
(R)-2-naphtylglycolate
-
388 - 2020
(R)-3-chloromandelate
11.03 - 21.17
(R)-mandelamide
0.018 - 1150
(R)-mandelate
2
(R)-trifluorolactate
pH 7.5, 25°C, recombinant wild-type enzyme
0.99 - 3.49
(S)-2-chloromandelate
250
(S)-2-Hydroxy-3-butenoic acid
-
-
2.95 - 101
(S)-2-naphthylglycolate
0.012 - 1124
(S)-Mandelate
2.5
(S)-trifluorolactate
pH 7.5, 25°C, recombinant wild-type enzyme
additional information
additional information
-
46
(2R)-2-naphthylglycolate
pH 7.5, 25°C, wild-type enzyme
70
(2R)-2-naphthylglycolate
pH 7.5, 25°C, wild-type enzyme, in presence of 20 mM MgCl2
137
(2R)-2-naphthylglycolate
pH 7.5, 25°C, mutant V29L
147
(2R)-2-naphthylglycolate
pH 7.5, 25°C, mutant V22I
0.9
(R)-2-chloromandelate
wild-type enzyme, pH 7.5, 25°C
1.23
(R)-2-chloromandelate
mutant Y45F, pH 7.5, 25°C
1.45
(R)-2-chloromandelate
mutant V29I, pH 7.5, 25°C
1.73
(R)-2-chloromandelate
mutant V29I/Y45F, pH 7.5, 25°C
1.82
(R)-2-chloromandelate
mutant V22I, pH 7.5, 25°C
2.4
(R)-2-chloromandelate
mutant V22I/Y45F, pH 7.5, 25°C
2.57
(R)-2-chloromandelate
mutant V22I/V29I/Y54F, pH 7.5, 25°C
2.6
(R)-2-chloromandelate
mutant V22I/V29I, pH 7.5, 25°C
5.4
(R)-2-naphthylglycolate
mutant A25V, pH 7.5, 25°C
7.3
(R)-2-naphthylglycolate
mutant V26F, pH 7.5, 25°C
10.4
(R)-2-naphthylglycolate
mutant V22F, pH 7.5, 25°C
10.5
(R)-2-naphthylglycolate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
14
(R)-2-naphthylglycolate
mutant V26L, pH 7.5, 25°C
14.1
(R)-2-naphthylglycolate
mutant V29F, pH 7.5, 25°C
15.6
(R)-2-naphthylglycolate
mutant V22A, pH 7.5, 25°C
18.3
(R)-2-naphthylglycolate
mutant T24S, pH 7.5, 25°C
23
(R)-2-naphthylglycolate
mutant V26A/V29L, pH 7.5, 25°C
30
(R)-2-naphthylglycolate
mutant V26A, pH 7.5, 25°C
33
(R)-2-naphthylglycolate
25°C, pH 7.5
46
(R)-2-naphthylglycolate
wild-type, pH 7.5, 25°C
53
(R)-2-naphthylglycolate
mutant V29A, pH 7.5, 25°C
70
(R)-2-naphthylglycolate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
137
(R)-2-naphthylglycolate
mutant V29L, pH 7.5, 25°C
147
(R)-2-naphthylglycolate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
5.4
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant A25V
-
7.3
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26F
-
10.4
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V22F
-
10.5
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V22I/V29L
-
14
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26L
-
14.1
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V29F
-
15.6
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V22A
-
18.3
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant T24S
-
23
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
-
30
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26A
-
46
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, wild-type
-
53
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V29A
-
70
(R)-2-naphtylglycolate
pH 7.5, 20 mM Mg2+, wild-type
-
137
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V29L
-
147
(R)-2-naphtylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V22I
-
388
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V29L
469
(R)-3-chloromandelate
pH 7.5, 25°C, wild-type enzyme
507
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54F
510
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I/Y54V
559
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26S
565
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54L
637
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V22I
913
(R)-3-chloromandelate
pH 7.5, 25°C, mutant L319F
953
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54A
1030
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I/Y54I
1160
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54V
1220
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V22L
1520
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54I
1710
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26L
2020
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I
11.03
(R)-mandelamide
pH 7.5, 25°C, wild-type enzyme
21.17
(R)-mandelamide
pH 7.5, 25°C, mutant V26L
0.018
(R)-mandelate
D270N mutant
0.11
(R)-mandelate
-
mutant E317Q
0.21
(R)-mandelate
mutant K166R
1
(R)-mandelate
mutant enzyme F52W/Y64W
3 - 6
(R)-mandelate
mutant V26L, pH 7.5, 25°C
3 - 6
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26L
10
(R)-mandelate
mutant enzyme Y54W
13
(R)-mandelate
mutant A25V, pH 7.5, 25°C
13
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant A25V
16.9
(R)-mandelate
-
25°C, pH 7.5, mutant enzyme N197A
33
(R)-mandelate
mutant V26F, pH 7.5, 25°C
33
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26F
53
(R)-mandelate
mutant V29F, pH 7.5, 25°C
53
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V29F
82
(R)-mandelate
mutant V22A, pH 7.5, 25°C
82
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V22A
98
(R)-mandelate
mutant V22F, pH 7.5, 25°C
98
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V22F
102
(R)-mandelate
mutant T24S, pH 7.5, 25°C
102
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant T24S
106
(R)-mandelate
mutant V26A/V29L, pH 7.5, 25°C
106
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
159
(R)-mandelate
mutant enzyme F52W
240
(R)-mandelate
mutant V29A, pH 7.5, 25°C
240
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V29A
300
(R)-mandelate
mutant V29L, pH 7.5, 25°C
300
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V29L
304
(R)-mandelate
mutant V26A, pH 7.5, 25°C
304
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26A
480
(R)-mandelate
-
wild type enzyme
500
(R)-mandelate
-
wild type enzyme
514
(R)-mandelate
-
25°C, pH 7.5, wild-type enzyme
526
(R)-mandelate
wild-type enzyme
552
(R)-mandelate
wild-type, pH 7.5, 25°C
552
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, wild-type
620
(R)-mandelate
pH 7.5, 20 mM Mg2+, wild-type
620
(R)-mandelate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
792
(R)-mandelate
pH 7.5, 25°C, recombinant wild-type enzyme
1010
(R)-mandelate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
1010
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V22I/V29L
1150
(R)-mandelate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
1150
(R)-mandelate
pH 7.5, 3.3 mM Mg2+, mutant V22I
0.99
(S)-2-chloromandelate
wild-type enzyme, pH 7.5, 25°C
1.33
(S)-2-chloromandelate
mutant Y45F, pH 7.5, 25°C
1.83
(S)-2-chloromandelate
mutant V29I, pH 7.5, 25°C
1.96
(S)-2-chloromandelate
mutant V29I/Y45F, pH 7.5, 25°C
2.35
(S)-2-chloromandelate
mutant V22I/V29I, pH 7.5, 25°C
2.47
(S)-2-chloromandelate
mutant V22I, pH 7.5, 25°C
2.51
(S)-2-chloromandelate
mutant V22I/Y45F, pH 7.5, 25°C
3.49
(S)-2-chloromandelate
mutant V22I/V29I/Y54F, pH 7.5, 25°C
2.95
(S)-2-naphthylglycolate
mutant V22F, pH 7.5, 25°C
2.95
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V22F
5.4
(S)-2-naphthylglycolate
mutant V26F, pH 7.5, 25°C
5.4
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26F
5.8
(S)-2-naphthylglycolate
mutant A25V, pH 7.5, 25°C
5.8
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant A25V
7.1
(S)-2-naphthylglycolate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
7.1
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
8.2
(S)-2-naphthylglycolate
mutant V26L, pH 7.5, 25°C
8.2
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26L
8.9
(S)-2-naphthylglycolate
mutant T24S, pH 7.5, 25°C
8.9
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant T24S
9.7
(S)-2-naphthylglycolate
mutant V29F, pH 7.5, 25°C
9.7
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V29F
9.8
(S)-2-naphthylglycolate
mutant V26A/V29L, pH 7.5, 25°C
9.8
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
11.1
(S)-2-naphthylglycolate
mutant V22A, pH 7.5, 25°C
11.1
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V22A
14
(S)-2-naphthylglycolate
mutant V26A, pH 7.5, 25°C
14
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V26A
25
(S)-2-naphthylglycolate
25°C, pH 7.5
30
(S)-2-naphthylglycolate
mutant V29A, pH 7.5, 25°C
30
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V29A
32
(S)-2-naphthylglycolate
wild-type, pH 7.5, 25°C
32
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, wild-type
38.4
(S)-2-naphthylglycolate
pH 7.5, 20 mM Mg2+, wild-type
38.4
(S)-2-naphthylglycolate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
65
(S)-2-naphthylglycolate
mutant V29L, pH 7.5, 25°C
65
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V29L
101
(S)-2-naphthylglycolate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
101
(S)-2-naphthylglycolate
pH 7.5, 3.3 mM Mg2+, mutant V22I
0.012
(S)-Mandelate
-
mutant E317Q
0.037
(S)-Mandelate
D270N mutant
0.46
(S)-Mandelate
-
mutant K166R
2 - 8
(S)-Mandelate
mutant enzyme Y54W
2.5
(S)-Mandelate
-
25°C, pH 7.5, mutant enzyme N197A
12
(S)-Mandelate
mutant enzyme F52W/Y64W
22
(S)-Mandelate
mutant A25V, pH 7.5, 25°C
22
(S)-Mandelate
mutant V26F, pH 7.5, 25°C
22
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant A25V
22
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26F
23
(S)-Mandelate
mutant V26L, pH 7.5, 25°C
23
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26L
53
(S)-Mandelate
mutant V29F, pH 7.5, 25°C
53
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V29F
77
(S)-Mandelate
mutant V22A, pH 7.5, 25°C
77
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+ mutant V22A
89
(S)-Mandelate
mutant V26A/V29L, pH 7.5, 25°C
89
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
98
(S)-Mandelate
mutant V22F, pH 7.5, 25°C
98
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V22F
120
(S)-Mandelate
mutant T24S, pH 7.5, 25°C
120
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant T24S
176
(S)-Mandelate
mutant V29A, pH 7.5, 25°C
176
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V29A
180
(S)-Mandelate
mutant V29L, pH 7.5, 25°C
180
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V29L
190
(S)-Mandelate
recombinant mandelate racemase, putative misfolded form with N-terminal hexahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
248
(S)-Mandelate
mutant enzyme F52W
350
(S)-Mandelate
-
wild type enzyme
440
(S)-Mandelate
-
wild type enzyme
447
(S)-Mandelate
-
25°C, pH 7.5, wild-type enzyme
467
(S)-Mandelate
wild-type enzyme
470
(S)-Mandelate
wild-type, pH 7.5, 25°C
470
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, wild-type
472
(S)-Mandelate
recombinant mandelate racemase fusion protein bearing an N-terminal StrepII-tag and a C-terminal decahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
492
(S)-Mandelate
pH 7.5, 20 mM Mg2+, wild-type
492
(S)-Mandelate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
550
(S)-Mandelate
mutant V26A, pH 7.5, 25°C
550
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26A
637
(S)-Mandelate
pH 7.5, 25°C, recombinant wild-type enzyme
710
(S)-Mandelate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
710
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
740
(S)-Mandelate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
740
(S)-Mandelate
pH 7.5, 3.3 mM Mg2+, mutant V22I
940
(S)-Mandelate
recombinant mandelate racemase represents correctly folded enzyme, with N-terminal hexahistidine tag, in Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
1124
(S)-Mandelate
recombinant enzyme replacement of the N-terminal hexahistidine tag by a StrepII-tag appears to ameliorate the folding problem yielding a single enzyme species, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
additional information
additional information
-
dependence of turnover number on pH
-
additional information
additional information
dependence of turnover number on pH
-
additional information
additional information
-
dependence of turnover number on pH
-
additional information
additional information
-
the turnover number of the mutant enzyme is unaffected by varying solvent viscosity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
20.1 - 85
(2R)-2-naphthylglycolate
0.061 - 0.177
(R)-2-chloromandelate
249 - 1300
(R)-3-chloromandelate
9.79 - 17.1
(R)-mandelamide
650
(R)-mandelate
pH 7.5, 25°C, recombinant wild-type enzyme
1.6
(R)-trifluorolactate
pH 7.5, 25°C, recombinant wild-type enzyme
0.056 - 0.195
(S)-2-chloromandelate
1.4
(S)-trifluorolactate
pH 7.5, 25°C, recombinant wild-type enzyme
20.1
(2R)-2-naphthylglycolate
pH 7.5, 25°C, wild-type enzyme, in presence of 20 mM MgCl2
34
(2R)-2-naphthylglycolate
pH 7.5, 25°C, mutant V22I
38
(2R)-2-naphthylglycolate
pH 7.5, 25°C, wild-type enzyme
85
(2R)-2-naphthylglycolate
pH 7.5, 25°C, mutant V29L
0.061
(R)-2-chloromandelate
wild-type enzyme, pH 7.5, 25°C
0.106
(R)-2-chloromandelate
mutant Y45F, pH 7.5, 25°C
0.118
(R)-2-chloromandelate
mutant V22I, pH 7.5, 25°C
0.121
(R)-2-chloromandelate
mutant V29I, pH 7.5, 25°C
0.15
(R)-2-chloromandelate
mutant V22I/Y45F, pH 7.5, 25°C
0.172
(R)-2-chloromandelate
mutant V22I/V29I, pH 7.5, 25°C
0.174
(R)-2-chloromandelate
mutant V29I/Y45F, pH 7.5, 25°C
0.177
(R)-2-chloromandelate
mutant V22I/V29I/Y54F, pH 7.5, 25°C
249
(R)-3-chloromandelate
pH 7.5, 25°C, wild-type enzyme
259
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54F
294
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26S
300
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V22I
305
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V29L
349
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54L
429
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54A
502
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54I
509
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V22L
515
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I/Y54I
531
(R)-3-chloromandelate
pH 7.5, 25°C, mutant L319F
533
(R)-3-chloromandelate
pH 7.5, 25°C, mutant Y54V
821
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I
916
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26L
1300
(R)-3-chloromandelate
pH 7.5, 25°C, mutant V26I/Y54V
9.79
(R)-mandelamide
pH 7.5, 25°C, wild-type enzyme
17.1
(R)-mandelamide
pH 7.5, 25°C, mutant V26L
0.056
(S)-2-chloromandelate
wild-type enzyme, pH 7.5, 25°C
0.122
(S)-2-chloromandelate
mutant Y45F, pH 7.5, 25°C
0.124
(S)-2-chloromandelate
mutant V22I, pH 7.5, 25°C
0.128
(S)-2-chloromandelate
mutant V29I, pH 7.5, 25°C
0.159
(S)-2-chloromandelate
mutant V22I/V29I, pH 7.5, 25°C
0.177
(S)-2-chloromandelate
mutant V22I/Y45F, pH 7.5, 25°C
0.185
(S)-2-chloromandelate
mutant V29I/Y45F, pH 7.5, 25°C
0.195
(S)-2-chloromandelate
mutant V22I/V29I/Y54F, pH 7.5, 25°C
620
(S)-Mandelate
pH 7.5, 25°C, recombinant wild-type enzyme
1100
(S)-Mandelate
recombinant mandelate racemase, replacement of the N-terminal hexahistidine tag by a StrepII-tag appears to ameliorate the folding problem yielding a single enzyme species, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
1200
(S)-Mandelate
recombinant mandelate racemase, represents correctly folded enzyme with N-terminal hexahistidine tag, in Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
7300
(S)-Mandelate
recombinant mandelate racemase, putative misfolded form with N-terminal hexahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
8000
(S)-Mandelate
recombinant mandelate racemase, fusion protein bearing an N-terminal StrepII-tag and a C-terminal decahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
17.3 - 98
(R)-2-hydroxybutyrate
0.16 - 33
(R)-2-naphthylglycolate
0.95 - 3.3
(R)-atrolactate
32
(R)-lactate
pH 7.5, 25°C, recombinant wild-type enzyme
40.2
(R,S)-1-hydroxyethylphosphonate
pH 7.5, 25°C, recombinant wild-type enzyme
1.9
(R,S)-1-naphthylglycolate
25°C, pH 7.5
0.67
(R,S)-2,2,2-trifluoro-1-hydroxyethylphosphonate
pH 7.5, 25°C, recombinant wild-type enzyme
0.52
(R,S)-2-naphthylglycolate
25°C, pH 7.5
0.0047 - 0.238
(R,S)-alpha-hydroxybenzylphosphonate
5.1
(R,S)-methyl-alpha-hydroxybenzylphosphonate
-
-
11.4 - 71
(S)-2-hydroxybutyrate
0.48 - 5
(S)-2-naphthylglycolate
0.5
(S)-cyclohexylphenylglycolate
wild-type enzyme
26.1
(S)-lactate
pH 7.5, 25°C, recombinant wild-type enzyme
0.00591 - 1.41
1,1-diphenyl-1-hydroxymethylphosphonate
0.023 - 0.19
2-naphthohydroxamate
0.023 - 0.19
2-naphtholhydroxamate
0.027
3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl)-propanoate
pH 7.5, 25°C, recombinant wild-type enzyme
1.3
3-Fluoropyruvate
pH and temperature not specified in the publication
5.5
alpha-hydroxyisobutyrate
pH 7.5, 25°C, recombinant wild-type enzyme
0.0117 - 0.216
benzohydroxamate
0.0093
benzohydroxamic acid
-
-
0.3
benzoylphosphonate
-
-
3.5
benzylphosphonate
-
-
4.5
diphenylacetate
wild-type enzyme
1.8
mesoxalate
pH and temperature not specified in the publication
0.00279
N-hydroxyformanilide
-
-
1.8
Tartronate
pH 7.5, 25°C, recombinant wild-type enzyme
17.3
(R)-2-hydroxybutyrate
wild-type enzyme
98
(R)-2-hydroxybutyrate
mutant enzyme F52W/Y54W
0.16
(R)-2-naphthylglycolate
mutant enzyme F52W/Y54W
33
(R)-2-naphthylglycolate
wild-type enzyme
0.95
(R)-atrolactate
-
wild-type enzyme
0.95
(R)-atrolactate
-
25°C, pH 7.5, wild-type enzyme
3.3
(R)-atrolactate
-
mutant N197A
3.3
(R)-atrolactate
-
25°C, pH 7.5, mutant enzyme N197A
0.0047
(R,S)-alpha-hydroxybenzylphosphonate
-
-
0.0047
(R,S)-alpha-hydroxybenzylphosphonate
-
25°C, pH 7.5, wild-type enzyme
0.0047
(R,S)-alpha-hydroxybenzylphosphonate
pH 7.5, 25°C, recombinant wild-type enzyme
0.0087
(R,S)-alpha-hydroxybenzylphosphonate
-
-
0.238
(R,S)-alpha-hydroxybenzylphosphonate
-
25°C, pH 7.5, mutant enzyme N197A
11.4
(S)-2-hydroxybutyrate
wild-type enzyme
71
(S)-2-hydroxybutyrate
mutant enzyme F52W/Y54W
0.48
(S)-2-naphthylglycolate
mutant enzyme F52W/Y54W
2 - 5
(S)-2-naphthylglycolate
wild-type enzyme
0.00591
1,1-diphenyl-1-hydroxymethylphosphonate
-
pH 6.3
0.00693
1,1-diphenyl-1-hydroxymethylphosphonate
-
pH 8.7
1.41
1,1-diphenyl-1-hydroxymethylphosphonate
-
pH 7.5
0.023
2-naphthohydroxamate
wild-type, 20 mM Mg2+, pH 7.5
0.027
2-naphthohydroxamate
wild-type, 3.3 mM Mg2+, pH 7.5
0.035
2-naphthohydroxamate
mutant V29L, 3.3 mM Mg2+, pH 7.5
0.057
2-naphthohydroxamate
25°C, pH 7.5
0.112
2-naphthohydroxamate
mutant V29I/V29I, 20 mM Mg2+, pH 7.5
0.19
2-naphthohydroxamate
mutant V22I, 3.3 mM Mg2+, pH 7.5
0.023
2-naphtholhydroxamate
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
0.027
2-naphtholhydroxamate
wild-type, pH 7.5, 25°C
0.035
2-naphtholhydroxamate
mutant V29L, pH 7.5, 25°C
0.112
2-naphtholhydroxamate
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
0.19
2-naphtholhydroxamate
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
0.67
benzilate
wild-type enzyme
0.67
benzilate
pH 7.5, 25°C, recombinant wild-type enzyme
45
benzilate
mutant enzyme F52W/Y54W
0.0117
benzohydroxamate
-
25°C, pH 7.5, wild-type enzyme
0.216
benzohydroxamate
-
25°C, pH 7.5, mutant enzyme N197A
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C92S/C264S/K166C
site-directed mutagenesis
D270N
structure of D270N with (S)-atrolactate bound in the active site reveals no geometric alterations when compared to the structure of the wild type enzyme complexed with (S)-atrolactate, with the exception that the side chain of His297 is tilted and displaced about 0.5A away from Asn270 and towards the (S)-atrolactate. The turnover number for both (R)-mandelate and (S)-mandelate are reduced 10000fold
E317Q
-
E317Q with 3400fold reduced turnover number for (R)-mandelate and 29000fold reduced turnover number for (S)-mandelate. E317Q mutant enzyme does not catalyze detectable elimination of Br- from either enantiomer of p-(bromomethyl)mandelate. E317Q mutant enzyme is irreversibly inactivated by racemic alpha-phenylglycidate at a rate comparable to that measured for wild type enzyme
F52W
compared to wild-type enzyme the catalytic preference of the mutant enzyme is reversed and catalytic efficiency is reduced. Mutant enzyme exhibits higher affinity for (R)-mandelate than for (S)-mandelate, and a higher turnover number with (S)-mandelate as the substrate, relative to that with (R)-mandelate
F52W/Y54W
compared to wild-type enzyme the catalytic preference of the mutant enzyme is reversed and catalytic efficiency is reduced. Mutant enzyme exhibits higher affinity for (R)-mandelate than for (S)-mandelate, and a higher turnover number with (S)-mandelate as the substrate, relative to that with (R)-mandelate
K166C
site-directed mutagenesis, analysis of ligand binding, kinetics
K166E
-
K166R retains low level of racemase activity. K166R mutant catalyzes the elimination of Br- from only the (R)-enantiomer of (R,S)-p-(bromomethyl)mandelate
K166M
site-directed mutagenesis, analysis of ligand binding, kinetics
K166M/H297N
site-directed mutagenesis, analysis of ligand binding, kinetics
S139A
site-directed mutagenesis, the mutation leads to a significant reduction of catalytic efficiency by about 45fold and 60fold in R to S and S to R directions
V22I/V29I
site-directed mutagenesis, kinetic analysis
V22I/V29I/Y54F
site-directed mutagenesis, the mutant shows 3.5fold greater relative activity as compared to the wild-type enzyme. The enhanced catalytic efficiency mainly arises from the elevated kcat, kinetic analysis
V22I/Y54F
site-directed mutagenesis, kinetic analysis
V26I
site-directed mutagenesis, the mutant shows 2fold higher catalytic efficiency towards R-mandelamide than the wild-type enzyme
V26I/Y54V
site-directed mutagenesis, the mutant shows 5.2fold higher catalytic efficiency towards (3R)-3-chloromandelic acid than the wild-type enzyme
V29I
site-directed mutagenesis, kinetic analysis
V29I/Y54F
site-directed mutagenesis, kinetic analysis
Y54L
site-directed mutagenesis
Y54Q
compared to wild-type enzyme the catalytic preference of the mutant enzyme is reversed and catalytic efficiency is reduced. Mutant enzyme exhibits higher affinity for (R)-mandelate than for (S)-mandelate, and a higher turnover number with (S)-mandelate as the substrate, relative to that with (R)-mandelate
V22I
-
site-directed mutagenesis, kinetic analysis
-
V22I/V29I/Y54F
-
site-directed mutagenesis, the mutant shows 3.5fold greater relative activity as compared to the wild-type enzyme. The enhanced catalytic efficiency mainly arises from the elevated kcat, kinetic analysis
-
V29I
-
site-directed mutagenesis, kinetic analysis
-
Y54F
-
site-directed mutagenesis, kinetic analysis
-
A25V
site-directed mutagenesis
A25V
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
A25V
variation of the hydrophobic loop, decrease in catalytic efficiency
H297N
-
H297N has no detectable mandelate racemase activity. However, H297N catalyzes the stereospecific elimination of Br- from racemic p-(bromomethyl)mandelate to give p-(methyl)benzoylformate in 45% yield at a rate equal to that measured for wild type enzyme
H297N
-
H297N, which is inactive as a racemase catalyzes the stereospecific exchange of the alpha-proton of S- but not R-mandelate with solvent D2O at a rate that is 30% of that of the wild type enzyme
H297N
site-directed mutagenesis, analysis of ligand binding, kinetics
N197A
-
Kcat for (R)-mandelate reduced 30fold, Kcat for (S)-mandelate reduced 179fold relative to wild-type
N197A
-
slight activating effect of sucrose on mutant enzyme efficiency. In presewnce of polymeric viscosogens poly(ethylene glycol) and Ficoll, no effect on turnover number or the ratio of turnover number and Km-value for the wild-type enzyme is observed
N197A
-
turnover number is reduced 30fold for (R)-mandelate and 179fold for (S)-mandelate relative to wild-type enzyme. The ratio of turnover number to Km-value is reduced 208fold for (R)-mandelate and 556fold for (S)-mandelate, 3.5fold reduction in affinity for the substrate analogue (R)-atrolactate, but 51fold and 18fold reduction in affinity for alpha-hydroxybenzylphosphonate and benzohydroxamate, respectively
T24S
site-directed mutagenesis
T24S
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
T24S
variation of the hydrophobic loop, decrease in catalytic efficiency
V22A
site-directed mutagenesis
V22A
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V22A
variation of the hydrophobic loop, decrease in catalytic efficiency
V22F
site-directed mutagenesis
V22F
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V22F
variation of the hydrophobic loop, decrease in catalytic efficiency
V22I
site-directed mutagenesis
V22I
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V22I
variation of the hydrophobic loop. For mandelate, catalytic efficiency similar to wild-type. For substrate 2-naphthylglycolate, increase in catalytic efficiency
V22I
site-directed mutagenesis, kinetic analysis
V22I/V29L
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V22I/V29L
variation of the hydrophobic loop, catalytic efficiency similar to wild-type
V26A
site-directed mutagenesis
V26A
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V26A
variation of the hydrophobic loop, catalytic efficiency similar to wild-type
V26A/V29L
site-directed mutagenesis
V26A/V29L
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V26A/V29L
variation of the hydrophobic loop, decrease in catalytic efficiency
V26F
site-directed mutagenesis
V26F
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V26F
variation of the hydrophobic loop, decrease in catalytic efficiency
V26L
site-directed mutagenesis
V26L
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V26L
variation of the hydrophobic loop, decrease in catalytic efficiency
V29A
site-directed mutagenesis
V29A
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V29A
variation of the hydrophobic loop, decrease in catalytic efficiency
V29F
site-directed mutagenesis
V29F
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V29F
variation of the hydrophobic loop, decrease in catalytic efficiency
V29L
site-directed mutagenesis
V29L
Catalytic efficiencies (kcat/Km) for all mutants are reduced between 6- and 40fold with the exception of V22I, V26A, V29L, and V22I/V29L which have near wildtype efficiencies with mandelate
V29L
variation of the hydrophobic loop. For mandelate, catalytic efficiency similar to wild-type. For substrate 2-naphthylglycolate, increase in catalytic efficiency
V29L
site-directed mutagenesis, the mutant shows 2fold higher catalytic efficiency towards R-2-naphthylglycolate than the wild-type enzyme
Y54F
site-directed mutagenesis
Y54F
site-directed mutagenesis, kinetic analysis
additional information
mandelate racemase and mandelate dehydrogenase are coexpressed in Escherichia coli for the synthesis of benzoylformate by converting racemic mandelate
additional information
-
mandelate racemase and mandelate dehydrogenase are coexpressed in Escherichia coli for the synthesis of benzoylformate by converting racemic mandelate
additional information
-
mandelate racemase and mandelate dehydrogenase are coexpressed in Escherichia coli for the synthesis of benzoylformate by converting racemic mandelate
-
additional information
development and evaluation of a virtual mutant screening method for non-natural substrates based on the binding energy in the transition state, the method is beneficial in enzyme rational redesign and helps to better understand the catalytic properties of the enzyme, and it is effective in predicting the trend of mutational effects on catalysis, molecular dynamic simulation, overview
additional information
Comparison of the binding affinities of the mutant variants with the intermediate/transition state analogues benzohydroxamate and cyclohexanecarbohydroxamate reveals that cationPi/N-Pi interactions between His297 and the hydroxamate/hydroximate moiety and the phenyl ring of benzohydroxamate contribute approximately 0.26 and 0.91 kcal/mol to binding, respectively, while interactions with Lys166 contribute approximately 1.74 and 1.74 kcal/mol, respectively. Lys166 contributes over 2.93 kcal/mol to the binding of (R)-atrolactate, and His297 contributes 2.46 kcal/mol to the binding of (S)-atrolactate
additional information
directed evolution of mandelate racemase by a high-throughput screening method, overview
additional information
evaluation of design of mandelate racemase with higher stability, usage of structural enzyme analysis for reengineering of mandelate racemase for enhanced thermal stability
additional information
-
directed evolution of mandelate racemase by a high-throughput screening method, overview
-
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1990
Pseudomonas putida
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1990
Pseudomonas putida
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1988
Pseudomonas putida
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1988
Pseudomonas putida
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Symmetry and asymmetry in mandelate racemase catalysis
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Pseudomonas putida
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Mandelate racemase
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Pseudomonas putida
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1974
Pseudomonas putida
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1970
Pseudomonas putida
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1970
Pseudomonas putida, Pseudomonas putida A.3.12
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Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant
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35
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1996
Pseudomonas putida (P11444), Pseudomonas putida
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1977
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Selection and characterization of a mutant of the cloned gene for mandelate racemase that confers resistance to an affinity label by greatly enhanced production of enzyme
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28
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1989
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Restructuring catalysis in the mandelate pathway
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57
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1990
Pseudomonas putida
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Biochemistry
30
9274-9281
1991
Pseudomonas putida
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30
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1991
Pseudomonas putida
brenda
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Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism
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30
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1991
Pseudomonas putida
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Mandelate racemase and class-related enzymes
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2
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1992
Pseudomonas putida
-
brenda
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33
635-643
1994
Pseudomonas putida
brenda
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Racemization of vinylglycolate catalyzed by mandelate racemase
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60
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1995
Pseudomonas putida
-
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Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant
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34
2788-2797
1995
Pseudomonas putida
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Large-scale production of mandelate racemase by Pseudomonas putida ATCC 12633: optimization of enzyme induction and development of a stable crude enzyme preparation
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56
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1997
Pseudomonas putida
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Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317
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34
2777-2787
1995
Pseudomonas putida
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ST.Maurice, M.; Bearne, S.L.
Reaction intermediate analogues for mandelate racemase: interaction between Asn 197 and the alpha-hydroxyl of the substrate promotes catalysis
Biochemistry
39
13324-13335
2000
Pseudomonas putida
brenda
St Maurice, M.; Bearne, S.L.
Kinetics and thermodynamics of mandelate racemase catalysis
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41
4048-4058
2002
Pseudomonas putida
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St Maurice, M.; Bearne, S.L.
Hydrophobic nature of the active site of mandelate racemase
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43
2524-2532
2004
Pseudomonas putida (P11444), Pseudomonas putida
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Stabilization and activity-enhancement of mandelate racemase from Pseudomonas putida ATCC 12336 by immobilization
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22
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2000
Pseudomonas putida, Pseudomonas putida ATCC 12336
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brenda
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A QM/MM study of the racemization of vinylglycolate catalyzed by mandelate racemase enzyme
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123
709-721
2001
Pseudomonas putida (P11444)
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Substrate spectrum of mandelate racemase. Part 1: Variation of the a-hydroxy acid moiety
J. Mol. Catal. B
15
207-211
2001
Pseudomonas putida
-
brenda
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Substrate spectrum of mandelate racemase. Part 2. (Hetero)-aryl-substituted mandelate derivatives and modulation of activity
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15
213-222
2001
Pseudomonas putida
-
brenda
Bauer, C.; Boy, M.; Faber, K.; Felfer, U.; Voss, H.
Activation of mandelate racemase via immobilization in lyotropic liquid crystals for biocatalysis in organic solvents: application and modeling
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16
91-100
2001
Pseudomonas putida
-
brenda
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347
951-961
2005
Pseudomonas putida
-
brenda
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Perturbing the hydrophobic pocket of mandelate racemase to probe phenyl motion during catalysis
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44
9013-9021
2005
Pseudomonas putida (P11444), Pseudomonas putida
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Inhibition of mandelate racemase by the substrate-intermediate-product analogue 1,1-diphenyl-1-hydroxymethylphosphonate
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15
4342-4344
2005
Pseudomonas putida
brenda
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Electrochemical quartz crystal nanobalance (EQCN) studies of the adsorption behaviour of an enzyme, mandelate racemase, and its substrate, mandelic acid, on Pt
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50
1289-1297
2005
Pseudomonas putida
-
brenda
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Reaction mechanism of the mandelate anion racemization catalyzed by mandelate racemase enzyme: A QM/MM Molecular Dynamics Free Energy Study
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109
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2005
Pseudomonas putida (P11444)
brenda