Ligand (R)-mandelate

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Basic Ligand Information

Molecular Structure
Picture of (R)-mandelate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C8H8O3
(R)-mandelate
IWYDHOAUDWTVEP-SSDOTTSWSA-N
Synonyms:
(-)-(R)-mandelic acid, (2R)-hydroxy(phenyl)acetic acid, (2R)-hydroxy(phenyl)ethanoate, (2R)-hydroxy(phenyl)ethanoic acid, (R)-(+)-mandelate, (R)-(-)-mandelic acid, (R)-(-)mandelate, (R)-(-)mandelic acid, (R)-2-hydroxy-2-phenylacetic acid, (R)-alpha-hydroxyphenylacetic acid, (R)-mandelic acid, D(-)-mandelate, D-mandelate, R-mandelate

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
(R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+
-
show the reaction diagram
(R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+
-
show the reaction diagram
D-mandelate = L-mandelate

In Vivo Product in Enzyme-catalyzed Reactions (3 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
(R)-mandelamide + H2O = (R)-mandelate + NH3
-
-
show the reaction diagram
mandelonitrile + 2 H2O = (R)-mandelic acid + NH3
-
-
show the reaction diagram
(S)-mandelate = (R)-mandelate

Substrate in Enzyme-catalyzed Reactions (8 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
(R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+
-
show the reaction diagram
7-aminocephalosporanic acid + (R)-mandelic acid = 7-[(1-hydroxy-1-phenyl)-acetamido]-3-acetoxymethyl-D3-cephem-4-carboxylic acid
-

Product in Enzyme-catalyzed Reactions (25 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
(R)-1-phenyl-1,2-ethanediol + O2 = (2R)-hydroxy(phenyl)ethanoic acid + H2O2
-
-
show the reaction diagram
methyl (R)-mandelate + H2O = (R)-mandelic acid + methanol
-
-
show the reaction diagram
cefamandole + H2O = (6R,7R)-7-amino-3-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (2R)-hydroxy(phenyl)acetic acid
-

Inhibitor in Enzyme-catalyzed Reactions (9 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
a substrate-analogue inhibitor, the carboxylate of the inhibitor is in an apparent hydrogen bond with Ser26, whereas one of the histidine residues, His70, is positioned to act as a proton donor in the formation of the first tetrahedral intermediate, mandelyl-ThDP
competitive
substrate analogue inhibitor

3D Structure of Enzyme-Ligand-Complex (PDB) (4 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (45 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
pH 8.5, 30°C
0.9
-
pH 7.5, 3.3 mM Mg2+, mutant V26L
3
6
pH 7.5, 20 mM Mg2+, wild-type
620
-
pH 7.5, 25°C, recombinant wild-type enzyme
792
-
pH 7.5, 3.3 mM Mg2+, mutant A25V
13
-
pH 7.5, 3.3 mM Mg2+, mutant T24S
102
-
pH 7.5, 3.3 mM Mg2+, mutant V22A
82
-
pH 7.5, 3.3 mM Mg2+, mutant V22F
98
-
pH 7.5, 3.3 mM Mg2+, mutant V22I
1150
-
pH 7.5, 3.3 mM Mg2+, mutant V22I/V29L
1010
-
pH 7.5, 3.3 mM Mg2+, mutant V26A
304
-
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
106
-
pH 7.5, 3.3 mM Mg2+, mutant V26F
33
-
mutant V29L, pH 7.5, 25°C
300
-
pH 7.5, 3.3 mM Mg2+, mutant V29A
240
-
pH 7.5, 3.3 mM Mg2+, mutant V29F
53
-
pH 7.5, 3.3 mM Mg2+, mutant V29L
300
-
pH 7.5, 3.3 mM Mg2+, wild-type
552
-
wild type enzyme
wild-type enzyme
526
-
wild-type, pH 7.5, 25°C
552
-
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
620
-
mutant T24S, pH 7.5, 25°C
102
-
-
1070
-
25°C, pH 7.5, mutant enzyme N197A
16.9
-
25°C, pH 7.5, wild-type enzyme
514
-
D270N mutant
0.018
-
mutant A25V, pH 7.5, 25°C
13
-
mutant E317Q
0.11
-
mutant enzyme F52W
159
-
mutant enzyme F52W/Y64W
1
-
mutant enzyme Y54W
10
-
mutant K166R
0.21
-
-
514
-
mutant V22A, pH 7.5, 25°C
82
-
mutant V22F, pH 7.5, 25°C
98
-
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
1150
-
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
1010
-
mutant V26A, pH 7.5, 25°C
304
-
mutant V26A/V29L, pH 7.5, 25°C
106
-
mutant V26F, pH 7.5, 25°C
33
-
mutant V26L, pH 7.5, 25°C
3
6
mutant V29A, pH 7.5, 25°C
240
-
mutant V29F, pH 7.5, 25°C
53
-

KM Value (56 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
at pH 7.0 and 37°C
3
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.76
-
pH 7.5, 30°C
0.9
-
pH 7.0, 27°C
3.05
-
pH 9.5, 27°C
0.325
-
pH 8.5, 30°C
0.02
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26F
1.8
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29L
1.7
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
1.4
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A
0.91
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I/V29L
2.8
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I
2.9
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22F
4.4
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22A
4.4
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant T24S
2.8
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V
1.1
-
pH 7.5 at 25°C, 20 mM Mg2+, wild-type
1.47
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26L
1.7
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A
5
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F
0.9
-
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
1.47
-
pH 7.5 at 25°C, 3.3 mM Mg2+, wild-type
1.2
-
pH 7.5, 25°C, recombinant wild-type enzyme
1.2
-
pH 8.7
2.02
-
wild type
0.34
-
wild type enzyme
0.4
-
wild-type enzyme
0.7
-
wild-type, pH 7.5, 25°C
1.2
-
-
0.81
-
mutant T24S, pH 7.5, 25°C
2.8
-
25°C, pH 7.5, mutant enzyme N197A
5.4
-
25°C, pH 7.5, wild-type enzyme
0.81
-
4-chloro-D-mandelate
0.1
-
D270N mutant
1.5
-
E317Q mutant
2.4
-
in presence of 1 mM Mg2+
0.1
-
L-mandelate
0.25
-
mutant A25V, pH 7.5, 25°C
1.1
-
mutant enzyme F52W
2.5
-
mutant enzyme F52W/Y64W
0.29
-
mutant enzyme Y54W
1.1
-
pH 7.5
0.44
-
mutant V22A, pH 7.5, 25°C
4.4
-
mutant V22F, pH 7.5, 25°C
4.4
-
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
2.9
-
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
2.8
-
mutant V26A, pH 7.5, 25°C
0.91
-
mutant V26A/V29L, pH 7.5, 25°C
1.4
-
mutant V26F, pH 7.5, 25°C
1.8
-
mutant V26L, pH 7.5, 25°C
1.7
-
mutant V29A, pH 7.5, 25°C
5
-
mutant V29F, pH 7.5, 25°C
0.9
-
mutant V29L, pH 7.5, 25°C
1.7
-
pH 6.3
0.95
-

Ki Value (20 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
pH 7.5, 20°C, wild-type enzyme
2.9
-
pH 7.5, 20°C, mutant enzyme R165G
73
-
pH 7.5, 20°C, mutant enzyme R165G/R277K
700
-
pH 7.5, 20°C, mutant enzyme R165K
3.1
-
pH 7.5, 20°C, mutant enzyme R277G
19.5
-
pH 7.5, 20°C, mutant enzyme R277K
7.2
-
-
11
-
substrate glycyl-S-(3-[[(1R)-2-[[(1R)-1-carboxyethyl]sulfanyl]-1-methyl-2-oxoethyl]amino]-3-oxopropyl)-L-cysteine
11.6
-
substrate 3-[[N-(phenylacetyl)glycyl]oxy]benzoic acid
11.6
-
substrate 3-[[N-(phenylacetyl)-D-alanyl]oxy]benzoic acid
11.6
-
substrate (2R)-2-[[N-(phenylacetyl)glycyl]sulfanyl]propanoic acid
11.6
-
pH 7.5, 25°C
11.6
-
wild-type, pH 7.0, 30°C
31
-
mutant F24A, pH 7.0, 30°C
3.5
-
mutant F146Y/F24A, pH 7.0, 30°C
6.2
-
mutant F146Y, pH 7.0, 30°C
13
-
pH 6.5, wild-type enzyme
1
-
pH 6.5, mutant enzyme S26A
100
-
pH 6.5, mutant enzyme H70A
40
-
pH 6.5, mutant enzyme H281A
40
-

References & Links

Links to other databases for (R)-mandelate

ChEBI
PubChem
-
PubChem