Information on EC 1.1.99.31 - (S)-mandelate dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.99.31
-
RECOMMENDED NAME
GeneOntology No.
(S)-mandelate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-mandelate + acceptor = phenylglyoxylate + reduced acceptor
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mandelate degradation I
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4-hydroxymandelate degradation
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Aminobenzoate degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
(S)-2-hydroxy-2-phenylacetate:acceptor 2-oxidoreductase
This enzyme is a member of the FMN-dependent alpha-hydroxy-acid oxidase/dehydrogenase family [1]. While all enzymes of this family oxidize the (S)-enantiomer of an alpha-hydroxy acid to an alpha-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. This enzyme transfers the electron pair from FMNH2 to a component of the electron transport chain, most probably ubiquinone [1,2]. It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy [2]. The enzyme has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate [1]. It also prefers substrates that, like (S)-mandelate, have beta unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate [1]. Esters of mandelate, such as methyl (S)-mandelate, are also substrates [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9067-95-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type strain NCIB 8250 has only L-mandelate dehydrogenase activity, some mutant strains evolve D-mandelate dehydrogenase activity
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-2-hydroxy-3-butenoic acid + acceptor
2-oxo-3-butenoic acid + reduced acceptor
show the reaction diagram
(R,S)-2-hydroxybutyrate + acceptor
2-oxobutyrate + reduced acceptor
show the reaction diagram
slow substrate
-
-
?
(R,S)-2-hydroxybutyric acid + acceptor
2-oxo-3-butynoic acid + reduced acceptor
show the reaction diagram
very low binding affinity for MDH
-
-
?
(R,S)-2-hydroxyhexanoate + acceptor
2-oxohexanoate + reduced acceptor
show the reaction diagram
-
-
-
?
(R,S)-2-hydroxyisocaproate + acceptor
2-oxoisocaproate + reduced acceptor
show the reaction diagram
-
-
-
?
(R,S)-2-hydroxyisovalerate + acceptor
2-oxo-isovalerate + reduced acceptor
show the reaction diagram
(R,S)-2-hydroxyoctanoate + acceptor
2-oxooctanoate + reduced acceptor
show the reaction diagram
slow substrate
-
-
?
(R,S)-2-hydroxyvalerate + acceptor
2-oxovalerate + reduced acceptor
show the reaction diagram
-
-
-
?
(R,S)-3-indolelactate + acceptor
3-(1H-indol-2-yl)-2-oxopropanoate + reduced acceptor
show the reaction diagram
-
-
-
?
(R,S)-3-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
slow substrate
-
-
?
(R,S)-indoleglycolate + acceptor
indol-2-yl(oxo)acetate + reduced acceptor
show the reaction diagram
-
-
-
?
(R,S)-mandelate + 2,6-dichlorophenolindophenol
2-oxo-2-phenylacetate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
(R,S)-mandelate + ferricyanide
2-oxo-2-phenylacetate + ferrocyanide
show the reaction diagram
-
-
-
?
(R,S)-p-chloromandelate + acceptor
?
show the reaction diagram
-
-
-
-
?
(S)-2-hydroxy-2-phenylacetate + O2
2-oxo-2-phenylacetate + H2O2
show the reaction diagram
-
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
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-
?
(S)-3-phenyllactate + acceptor
?
show the reaction diagram
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-
-
-
?
(S)-mandelate + 2 ferricyanide
2-oxo-2-phenylacetate + 2 ferrocyanide + 2 H+
show the reaction diagram
(S)-mandelate + 2 ferricyanide
benzoylformic acid + 2 ferrocyanide + 2 H+
show the reaction diagram
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-
-
-
?
(S)-mandelate + 2,6-dichloroindophenol
2-oxo-2-phenylacetate + ?
show the reaction diagram
-
-
-
-
?
(S)-mandelate + 2,6-dichlorophenolindophenol
2-oxo-2-phenylacetate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
(S)-mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
show the reaction diagram
(S)-mandelate + acceptor
benzoylformate + reduced acceptor
show the reaction diagram
-
-
-
-
?
(S)-mandelate + cytochrome c
2-oxo-2-phenylacetate + ?
show the reaction diagram
-
-
-
-
?
(S)-phenyllactate + 2,6-dichlorophenolindophenol
?
show the reaction diagram
-
-
-
-
?
2-hydroxy-3-butynoate + acceptor
2-oxo-3-butynoate + reduced acceptor
show the reaction diagram
2-hydroxybutyrate + acceptor
2-oxobutyrate + reduced acceptor
show the reaction diagram
-
-
-
-
?
2-hydroxyhexanoate + acceptor
2-oxohexanoate + reduced acceptor
show the reaction diagram
-
-
-
-
?
2-hydroxyisocaproate + acceptor
2-oxoisocaproate + reduced acceptor
show the reaction diagram
-
-
-
-
?
2-hydroxyoctanoate + acceptor
2-oxooctanoate + reduced acceptor
show the reaction diagram
-
-
-
-
?
2-hydroxyoctanoate + acceptor
? + reduced acceptor
show the reaction diagram
-
-
-
-
?
2-hydroxyvalerate + acceptor
2-oxovalerate + reduced acceptor
show the reaction diagram
-
-
-
-
?
3-hydroxy-DL-mandelate + ferricyanide
2-oxo-2-(3-hydroxyphenyl)acetate + ferrocyanide + H2O
show the reaction diagram
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-
-
-
?
3-indolelactate + acceptor
3-(1H-indol-2-yl)-2-oxopropanoate + reduced acceptor
show the reaction diagram
-
-
-
-
?
3-indolelactate + acceptor
? + reduced acceptor
show the reaction diagram
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-
-
-
?
3-methoxy-DL-mandelate + ferricyanide
2-oxo-2-(3-methoxyphenyl)acetate + ferrocyanide + H2O
show the reaction diagram
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-
-
-
?
3-phenyllactate + acceptor
2-oxo-3-phenylpropanoate + reduced acceptor
show the reaction diagram
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-
-
-
?
4-bromo-DL-mandelate + ferricyanide
2-oxo-2-(4-bromophenyl)acetate + ferrocyanide + H2O
show the reaction diagram
-
-
-
-
?
4-chloro-DL-mandelate + ferricyanide
2-oxo-2-(4-chlorophenyl)acetate + ferrocyanide + H2O
show the reaction diagram
-
-
-
-
?
4-chloromandelate + acceptor
2-oxo-2-(4-chlorophenyl)acetate + reduced acceptor
show the reaction diagram
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-
-
-
?
4-fluoro-D,L-mandelate + ferricyanide
2-oxo-2-(4-fluorophenyl)acetate + ferrocyanide + H2O
show the reaction diagram
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-
-
-
?
4-hydroxy-DL-mandelate + ferricyanide
2-oxo-2-(4-hydroxyphenyl)acetate + ferrocyanide + H2O
show the reaction diagram
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-
-
-
?
4-methoxy-DL-mandelate + ferricyanide
2-oxo-2-(4-methoxyphenyl)acetate + ferrocyanide + H2O
show the reaction diagram
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-
-
-
?
4-methyl-DL-mandelate + ferricyanide
2-oxo-2-(4-methylphenyl)acetate + ferrocyanide + H2O
show the reaction diagram
-
-
-
-
?
DL-mandelate + ferricyanide
2-oxo-2-phenylacetate + ferrocyanide + H2O
show the reaction diagram
ethyl-(S)-mandelate + acceptor
?
show the reaction diagram
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-
-
-
?
indoleglycolate + acceptor
indol-2-yl(oxo)acetate + reduced acceptor
show the reaction diagram
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-
-
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?
L-mandelate + ferricyanide
2-oxo-2-phenylacetate + ferrocyanide
show the reaction diagram
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-
-
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?
mandelate + acceptor
2-oxo-2-phenylacetate + reduced acceptor
show the reaction diagram
methyl-(S)-mandelate + acceptor
?
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-mandelate + 2 ferricyanide
benzoylformic acid + 2 ferrocyanide + 2 H+
show the reaction diagram
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-
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavocytochrome b2
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the enzyme is a flavocytochrome b2
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-mandelate
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-
(R,S)-2-hydroxy-3-butynoic acid
irreversible inactivation
(S)-1-phenyl-1,2-ethanediol
(S)-1-phenyl-2,2,2-trifluoroethanol
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competitive inhibitor
(S)-1-phenyl-2-propen-1-ol
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-
(S)-1-phenyl-2-propyn-1-ol
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-
(S)-2-methoxy-2-phenylacetate
competitive inhibitor
(S)-3-phenyllactate
competitive inhibitor
2-phenylacetate
competitive inhibitor
2-phenylethanoate
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-
L-Phenyllactate
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-
p-chloromercuribenzoate
-
10-20% inhibition at 0.01 mM
phenylethanediol
-
poor competitive inhibitor of wild-type enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
(R,S)-2-hydroxy-3-butynoic acid
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
32
(R,S)-2-hydroxybutyrate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
4.9
(R,S)-2-hydroxyhexanoate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
4.3
(R,S)-2-hydroxyisocaproate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
9.5
(R,S)-2-hydroxyisovalerate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
0.75
(R,S)-2-hydroxyoctanoate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
15.3
(R,S)-2-hydroxyvalerate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
0.9
(R,S)-3-indolelactate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
2
(R,S)-3-phenyllacetate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
-
0.4
(R,S)-indoleglycolate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
0.33
(R,S)-mandelate
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
0.074 - 4.3
(S)-3-phenyllactate
0.04 - 73
(S)-Mandelate
0.78 - 2.6
(S)-phenyllactate
10.3
2-Hydroxy-3-butenoate
-
pH 7.5, 20C, 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, 20C, 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, 25C, cosubstrate: ferricyanide
0.13 - 0.9
3-indolelactate
0.12
3-methoxy-D,L-mandelate
-
pH 7.5, 25C, cosubstrate: ferricyanide
0.37 - 2
3-Phenyllactate
0.26
4-bromo-D,L-mandelate
-
pH 7.5, 25C, 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, 25C, cosubstrate: ferricyanide
0.12
4-methoxy-D,L-mandelate
-
pH 7.5, 25C, cosubstrate: ferricyanide
0.17
4-methyl-D,L-mandelate
-
pH 7.5, 25C, cosubstrate: ferricyanide
0.35
D,L-Mandelate
-
pH 7.5, 25C, cosubstrate: ferricyanide
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 30C
0.24 - 0.63
indoleglycolate
0.04 - 0.24
Mandelate
7.4 - 11.3
methyl-(S)-mandelate
0.04 - 3.2
O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
(R,S)-p-chloromandelate
Pseudomonas putida
-
mutant enzyme H274G, in presence of 20 mM imidazole
201 - 270
(S)-3-phenyllactate
0.04 - 402
(S)-Mandelate
0.5
2-Hydroxy-3-butenoate
Pseudomonas putida
-
pH 7.5, 20C, 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
Pseudomonas putida
-
pH 7.5, 20C, 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
Pseudomonas putida
-
-
108
3-hydroxy-DL-mandelate
Rhodotorula graminis
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pH 7.5, 25C, cosubstrate: ferricyanide
0.27 - 3.9
3-indolelactate
68
3-methoxy-DL-mandelate
Rhodotorula graminis
-
pH 7.5, 25C, cosubstrate: ferricyanide
0.15 - 0.87
3-Phenyllactate
108
4-bromo-DL-mandelate
Rhodotorula graminis
-
pH 7.5, 25C, cosubstrate: ferricyanide
68 - 116
4-chloro-DL-mandelate
9.3 - 334
4-chloromandelate
98
4-fluoro-DL-mandelate
Rhodotorula graminis
-
pH 7.5, 25C, cosubstrate: ferricyanide
146
4-hydroxy-DL-mandelate
Rhodotorula graminis
-
pH 7.5, 25C, cosubstrate: ferricyanide
106
4-methoxy-DL-mandelate
Rhodotorula graminis
-
pH 7.5, 25C, cosubstrate: ferricyanide
80
4-methyl-DL-mandelate
Rhodotorula graminis
-
pH 7.5, 25C, cosubstrate: ferricyanide
225
cytochrome c
Rhodotorula graminis
-
pH 7.5, 25C
94
D,L-Mandelate
Rhodotorula graminis
-
pH 7.5, 25C, cosubstrate: ferricyanid
155 - 316
DL-[2-1H]-mandelate
88 - 99
DL-[2-2H]-mandelate
0.3 - 204
ethyl-(S)-mandelate
550
ferricyanide
Rhodotorula graminis
-
pH 7.5, 25C
1.2 - 122
indoleglycolate
114
L-Mandelate
Rhodotorula graminis
-
pH 7.5, 25C, cosubstrate: ferricyanide
2.3 - 350
Mandelate
2.5 - 151
methyl-(S)-mandelate
0.03 - 3.4
O2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9 - 700
(R)-mandelate
36
(R,S)-2-hydroxy-3-butynoic acid
in 0.1 M potassium phosphate buffer, pH 7.5 at 20C
53.8
(S)-1-phenyl-1,2-ethanediol
-
wild type enzyme, at 20C, in 0.1 M potassium phosphate, pH 7.5
2.6
(S)-1-phenyl-2,2,2-trifluoroethanol
-
wild type enzyme, at 20C, in 0.1 M potassium phosphate, pH 7.5
11 - 67
2-phenylethanoate
0.37
hexanoate
-
pH 7.5, 25C
0.4
L-lactate
-
pH 7.5, 25C
1.9
L-Phenyllactate
-
pH 7.5, 25C
0.078
oxalate
-
pH 7.5, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.68
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crude extract, at pH 6.5 and 30C
20.5
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after 7.65fold purification, at pH 6.5 and 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
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about 58% activity at 20C, about 50% activity at 40C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.35 A resolution structure of oxidized form and of the substrate-reduced form of MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
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hanging-drop vapor-diffusion method. Crystal structure of MDH-GOX2, a chimeric mutant of MDH with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
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mutant G81A of the catalytically similar, soluble chimera MDH-GOX2 (mandelate dehydrogenase/glycolate oxidase)
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freeze-thaw cycles cause significant loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, wild-type enzyme can be stored frozen in 20% ethanediol for weeks without loss of activity
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-70C, wild-type enzyme retains activity for more than 1 year. The single Arg165 mutant lose activity after 2-3 months, double mutants R165K/R277K and R165G/R277K are inactivated after 2-3 weeks in storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-tagged enzyme, Ni-resin column chromatography and Sephadex G-25 gel filtration
mutant enzymes H274G, H274A and H274N
-
mutant enzymes R277K, R277G, R277H and R277L
-
recombinant enzyme
-
Toyopearl DEAE-650M column chromatography
-
wild-type and mutant enzymes
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
H274D
-
inactive mutant
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
additional information
Show AA Sequence (144 entries)
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