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EC Tree
The taxonomic range for the selected organisms is: Macaca fascicularis The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
trans-1,2-dihydrobenzene-1,2-diol dehydrogenase,
more
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dihydrodiol dehydrogenase
-
dehydrogenase, trans-1,2-dihydrobenzene-1,2-diol
-
-
-
-
dihydrodiol dehydrogenase
-
-
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trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase
-
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camphorquinone + NADPH + H+
?
enzyme has dehydrogenase and reductase activities, enzyme is identical to NADP+-dependent D-xylose dehydrogenase
-
-
?
(R)-tetralol + NADP+
?
-
-
-
?
(R)-tetralol + NADP+
? + NADPH
dehydrogenase activity
-
-
r
(S)-indan-1-ol + NADP+
?
-
-
-
?
(S)-indan-1-ol + NADP+
? + NADPH
dehydrogenase activity
-
-
r
(S)-tetralol + NADP+
?
-
-
-
?
(S)-tetralol + NADP+
? + NADPH
dehydrogenase activity
-
-
r
4-chromanol + NADP+
?
-
-
-
r
4-chromanol + NADP+
? + NADPH
dehydrogenase activity
-
-
r
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
-
-
-
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
-
-
-
?
S-(+)-1,2,3,4-tetrahydronaphth-1-ol + NADP+
? + NADPH
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
trans-benzene dihydrodiol + NADP+
? + NADPH
dehydrogenase activity
-
-
r
additional information
?
-
S-(+)-1,2,3,4-tetrahydronaphth-1-ol + NADP+
? + NADPH
-
-
-
?
S-(+)-1,2,3,4-tetrahydronaphth-1-ol + NADP+
? + NADPH
dehydrogenase activity
-
-
r
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
-
-
-
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
-
-
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
-
the reaction produces a ketol which then enolizes to the catechol
-
?
additional information
?
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dihydrodiol dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
-
-
?
additional information
?
-
dimeric dihydrodiol dehydrogenase catalyses the nicotinamide adenine dinucleotide phosphate NADP+-dependent oxidation of trans-dihydrodiols of aromatic hydrocarbons to their corresponding catechols, dimeric dihydrodiol dehydrogenase is also competent in the NADPH-driven reduction of a limited number of aldehyde and dicarbonyl compounds such as 3-deoxyglucosone, camphorquinone, and 3-nitrobenzaldehyde
-
-
?
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camphorquinone + NADPH + H+
?
enzyme has dehydrogenase and reductase activities, enzyme is identical to NADP+-dependent D-xylose dehydrogenase
-
-
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
-
-
-
?
additional information
?
-
additional information
?
-
dihydrodiol dehydrogenase catalyzes the NADP+-linked oxidation of dihydrodiols of aromatic hydrocarbons to their corresponding catechols and is regarded as a toxication enzyme in the metabolism of carcinogenic polycyclic aromatic hydrocarbons because oxidation by the enzyme yields reactive and redox-active ortho-quinones and reactive oxygen species, broad substrate specificity indicates additional roles of the enzyme in the metabolism of endogenous and xenobiotic carbonyl compounds and the prevention of the development of glycation
-
-
?
additional information
?
-
dimeric dihydrodiol dehydrogenase catalyses the nicotinamide adenine dinucleotide phosphate NADP+-dependent oxidation of trans-dihydrodiols of aromatic hydrocarbons to their corresponding catechols, dimeric dihydrodiol dehydrogenase is also competent in the NADPH-driven reduction of a limited number of aldehyde and dicarbonyl compounds such as 3-deoxyglucosone, camphorquinone, and 3-nitrobenzaldehyde
-
-
?
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NADP+
-
-
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isoascorbic acid
competitive inhibitor
2,6-dihydroxyanthraquinone
-
competitive inhibitor
isoascorbic acid
-
competitive inhibitor
L-ascorbic acid
-
competitive inhibitor
4-hydroxyacetophenone
-
-
4-hydroxyacetophenone
-
competitive inhibitor
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0.056
(R)-tetralol
pH 7.4, 25°C
0.076
(S)-indan-1-ol
pH 7.4, 25°C
0.029
(S)-tetralol
pH 7.4, 25°C
0.073
4-chromanol
pH 7.4, 25°C
0.72
trans-benzene dihydrodiol
pH 7.4, 25°C
0.84
Camphorquinone
reduction reaction of mutant W254Y, using 0.1 mM NADPH as coenzyme
1.5
Camphorquinone
reduction reaction of mutant F154A, using 0.1 mM NADPH as coenzyme
2.4
Camphorquinone
reduction reaction of mutant R41D, using 0.1 mM NADPH as coenzyme
2.6
Camphorquinone
reduction reaction of mutant F279A, using 0.1 mM NADPH as coenzyme
3.1
Camphorquinone
reduction reaction of mutant R37D, using 0.1 mM NADPH as coenzyme
3.6
Camphorquinone
reduction reaction of mutant W254A, using 0.1 mM NADPH as coenzyme
5.1
Camphorquinone
reduction reaction of mutant H76Q, using 0.1 mM NADPH as coenzyme
5.2
Camphorquinone
reduction reaction of mutant R37A, using 0.1 mM NADPH as coenzyme
8.1
Camphorquinone
reduction reaction of mutant A36D, using 0.1 mM NADPH as coenzyme
11
Camphorquinone
reduction reaction of wild type enzyme, using 0.1 mM NADPH as coenzyme
12
Camphorquinone
reduction reaction of mutant H79Q, using 0.1 mM NADPH as coenzyme
13
Camphorquinone
reduction reaction of mutant W125Y, using 0.1 mM NADPH as coenzyme
17
Camphorquinone
reduction reaction of mutant K97M, using 0.1 mM NADPH as coenzyme
21
Camphorquinone
reduction reaction of mutant K79R, using 0.1 mM NADPH as coenzyme
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0.004 - 20
Camphorquinone
84
(R)-tetralol
pH 7.4, 25°C
2040
(S)-indan-1-ol
pH 7.4, 25°C
1320
(S)-tetralol
pH 7.4, 25°C
2880
4-chromanol
pH 7.4, 25°C
24.6
trans-benzene dihydrodiol
pH 7.4, 25°C
0.004
Camphorquinone
reduction reaction of mutant K79R, 0.1 mM NADPH
0.004
Camphorquinone
reduction reaction of mutant K97M, 0.1 mM NADPH
0.02
Camphorquinone
reduction oxidation reaction of mutant A36D, 0.1 mM NADPH
0.05
Camphorquinone
reduction oxidation reaction of mutante R37D, 0.1 mM NADPH
0.6
Camphorquinone
reduction reaction of mutant H79Q, 0.1 mM NADPH
0.9
Camphorquinone
oxidation reaction of mutant R41D, 0.1 mM NADPH
2.1
Camphorquinone
reduction reaction of mutant R37A, 0.1 mM NADPH
3.6
Camphorquinone
reduction reaction of mutant H76Q, 0.1 mM NADPH
20
Camphorquinone
reduction reaction of wild type enzyme, 0.1 mM NADPH
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0.00097 - 0.136
4-hydroxyacetophenone
0.038 - 4.176
isoascorbic acid
0.00097
4-hydroxyacetophenone
Macaca fascicularis
-
wild type enzyme
0.00097
4-hydroxyacetophenone
Macaca fascicularis
determined in the camphorquinone reduction, inhibitor is uncompetitive with respect to camphorquinone
0.00097
4-hydroxyacetophenone
Macaca fascicularis
the hydroxyl group of 4-hydroxyacetophenone forms hydrogen bond interactions with the side-chain oxygen and the main chain nitrogen of Asp280, the benzene ring and methyl group make a number of hydrophobic contacts with Phe279, Leu158 and Leu177
0.006
4-hydroxyacetophenone
Macaca fascicularis
mutant W254Y
0.075
4-hydroxyacetophenone
Macaca fascicularis
rmutant F279A
0.078
4-hydroxyacetophenone
Macaca fascicularis
mutant F154A
0.083
4-hydroxyacetophenone
Macaca fascicularis
mutant W254A
0.136
4-hydroxyacetophenone
Macaca fascicularis
mutant W125Y
0.038
isoascorbic acid
Macaca fascicularis
determined in the camphorquinone reduction, inhibitor is uncompetitive with respect to camphorquinone
0.038
isoascorbic acid
Macaca fascicularis
mutant W254Y
0.066
isoascorbic acid
Macaca fascicularis
mutant W254A
0.288
isoascorbic acid
Macaca fascicularis
mutant F154A
3.94
isoascorbic acid
Macaca fascicularis
mutant F279A
4.176
isoascorbic acid
Macaca fascicularis
mutant W125Y
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0.04
R148A and R202A mutant, 25 mM Tris-HCl, pH 7.5, 0.25 mM NADP+
0.05
wild type enzyme in dimeric form, 25 mM Tris-HCl, pH 7.5, 0.25 mM NADP+
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25
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assay at
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UniProt
brenda
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brenda
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brenda
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proximal and distal tubules of the cortex, loop of Henle of the medulla
brenda
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DHDH_MACFA
334
0
36435
Swiss-Prot
Secretory Pathway (Reliability: 4 )
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70000
determined by gel filtration
36000
x * 36000, SDS-PAGE
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additional information
the dissociation of DD into the monomer largely affects the stability rather than catalytic activity
dimer
-
dimer
site-directed mutagenesis has demonstrated that the intact dimer is not essential for catalytic activity
dimer
-
x-ray crystallography
dimer
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X-ray crystallography, the intact dimer is not essential for catalytic activity
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crystals are obtained at 19.9°C in a culture plate via the vapour-diffusion method, crystal structure of dimeric dihydrodiol dehydrogenase complexed with the inhibitor isoascorbic acid is determined at 2.59 A resolution
dimeric apoenzyme (at 2.0 A resolution) and enzyme-inhibitor complex (at 2.9 A resolution), crystals are grown using droplets consisting of the dihydrodiol dehydrogenase/NADPH solution mixed with a matching volume containing 1.5 M ammonium phosphate and 0.1 M sodium citrate at pH 5.6, tertiary structure is formed by a classical dinucleotide binding fold comprising of 2 beta-alpha-beta-alpha-beta motifs at the N-terminus and an eight-stranded, predominantly antiparallel beta-sheet at the C-terminus
vapour diffusion method with 2 M ammonium phosphate and 0.1 M sodium citrate buffer (pH 5.6) and 20% glycerol
-
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A36D
production by site-directed mutagenesis
D280A
production by site-directed mutagenesis
F154A
production by site-directed mutagenesis
F279A
production by site-directed mutagenesis
H76Q
production by site-directed mutagenesis
H79Q
production by site-directed mutagenesis
K97M
production by site-directed mutagenesis
K97R
production by site-directed mutagenesis
R148A
mutagenesis is performed using a QuickChange site-directed mutagenesis kit, dehydrogenase activity is comparable to that of the wild type
R148A/R202A
mutagenesis is performed using a QuickChange site-directedmutagenesis kit
R202A
mutagenesis is performed using a QuickChange site-directed mutagenesis kit, dehydrogenase activity is comparable to that of the wild type
R37A
production by site-directed mutagenesis
R37D
production by site-directed mutagenesis
R41A
production by site-directed mutagenesis
R41D
production by site-directed mutagenesis
W125Y
production by site-directed mutagenesis
W254A
production by site-directed mutagenesis
W254Y
production by site-directed mutagenesis
F279A
-
the mutation affects inhibition and substrate affinity
K97M
-
mutant shows almost complete abrogation in activity for D-xylose oxidation and NADP+, and very poor activity with camphorquinone reduction and NADPH
K97R
-
mutant shows almost complete abrogation in activity for D-xylose oxidation and NADP+, and very poor activity with camphorquinone reduction and NADPH
R148A
-
activity and temperature stability are similar to the wild type enzyme
R148A/R202A
-
very low activity, the Vmax value of the mutant enzyme is 3.7fold lower than the wild type enzyme, displays significant temperature sensitivity
R202A
-
activity and temperature stability are similar to the wild type enzyme
W125A
-
the mutation affects inhibition and substrate affinity
W254A
-
the mutation affects inhibition and substrate affinity
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37
no activity of the 37°C-inactivated R148A/R202A mutant is recovered by the addition of 0.1 mM NADP+ and 40% glycerol
37
-
the wild type enzyme and mutant enzymes R148A and R202A are stable at 37°C
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recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells, the single mutant enzymes are partially purified by the ammonium sulphate fractionation and chromatography on a Sephadex G-100 column, the wild type and double mutant enzyme are further purified by chromatography on a Red Sepharose column
the recombinant enzymes are purified from the 12000g supernatants of the homogenates of the cells
ammonium sulfate precipitation, Red Sepharose column chromatography, and Sephadex G-100 gel filtration
-
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in Escherichia coli BL21(DE3)
wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3)
expressed in Escherichia coli BL21(DE3) cells
-
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Nakagawa, M.; Matsuura, K.; Hara, A.; Sawada, H.; Bunai, H.; Ohya, I.
Dimeric dihydrodiol dehydrogenase in monkey kidney. Substrate specificity, stereospecificity of hydrogen transfer, and distribution
J. Biochem.
106
1104-1109
1989
Macaca fascicularis, Macaca fuscata
brenda
Higaki, Y.; Kamiya, T.; Usami, N.; Shintani, S.; Shiraishi, H.; Ishikura, S.; Yamamoto, I.; Hara, A.
Molecular characterization of two monkey dihydrodiol dehydrogenases
Drug Metab. Pharmacokinet.
17
348-356
2002
Macaca fascicularis (Q95JH5), Macaca fascicularis (Q95JH7), Macaca fuscata fuscata (Q95JH4), Macaca fuscata fuscata (Q95JH6)
brenda
Carbone, V.; Sumii, R.; Ishikura, S.; Asada, Y.; Hara, A.; El-Kabbani, O.
Structure of monkey dimeric dihydrodiol dehydrogenase in complex with isoascorbic acid
Acta Crystallogr. Sect. D
64
532-542
2008
Macaca fascicularis (Q9TQS6), Macaca fuscata
brenda
Carbone, V.; Hara, A.; El-Kabbani, O.
Structural and functional features of dimeric dihydrodiol dehydrogenase
Cell. Mol. Life Sci.
65
1464-1474
2008
Bos taurus (Q148L6), Macaca fascicularis, Mus musculus (Q9DBB8), Pongo abelii (Q5R5J5), Sus scrofa
brenda
Carbone, V.; Endo, S.; Sumii, R.; Chung, R.P.; Matsunaga, T.; Hara, A.; El-Kabbani, O.
Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: probing the subunit interface with site-directed mutagenesis
Proteins Struct. Funct. Bioinform.
70
176-187
2007
Macaca fascicularis
-
brenda
Carbone, V.; Endo, S.; Sumii, R.; Chung, R.; Matsunaga, T.; Hara, A.; El-Kabbani, O.
Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: Probing the subunit interface with site-directed mutagenesis
Proteins Struct. Funct. Genet.
70
176-187
2008
Macaca fascicularis (Q9TQS6)
brenda