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Information on EC 1.3.1.20 - trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
for references in articles please use BRENDA:EC1.3.1.20
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.20 trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
The enzyme appears in viruses and cellular organisms
- 1.3.1.20
- dihydrodiol
-
trans-dihydrodiols
- medicine
-
polycyclic
- catechols
-
nadp+-dependent
- benzenedihydrodiol
- indomethacin
-
penning
-
alpha-hydroxysteroids
- o-quinones
-
talalay
-
anti-diol
-
1.1.1.184
-
+/-trans-7,8-dihydroxy-7,8-dihydrobenzoapyrene
-
non-k-region
-
benzaanthracene
-
alicyclic
-
trans-1,2-dihydrodiols
- dicoumarol
- chrysene
-
benzoapyrene-7,8-dione
-
harvey
-
pah-induced
- androsterone
- diagnostics
showSynonyms
trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DD
DDH
dehydrogenase, trans-1,2-dihydrobenzene-1,2-diol
-
-
-
-
DHDH
dihydrodiol dehydrogenase
additional information
DDH
member of the aldo-keto reductases superfamily which plays a central role in the metabolism of steroid hormones, prostaglandins and xenobiotics
additional information
-
DD4 shows only 83% sequence homology to the other human DD isoforms
additional information
-
sequence analysis revealed high sequence homology between dimeric mammalian dihydrodiol dehydrogenases, but no homology with monomeric or cis-dihydrodiol-specific enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
overview about the regio- and stereospecificity for utilization of dihydrodiol derivatives as substrates
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
isoform DD3 probably identical with 3(17)alpha-hydroxysteroid dehydrogenase EC 1.1.1.59 and D-xylose dehydrogenase EC 1.1.1.179
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
structure analysis reveals that the enzyme belongs to the aldo-keto reductase superfamily, like 3alpha-hydroxysteroid dehydrogenase, 17beta-hydroxysteroid dehydrogenase, 20alpha-hydroxysteroid dehydrogenase, aldose reductase, and aldehyde reductase
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
structure analysis reveals that the enzyme belongs to the aldo-keto reductase superfamily, like 3alpha-hydroxysteroid dehydrogenase, 17beta-hydroxysteroid dehydrogenase, 20alpha-hydroxysteroid dehydrogenase, aldose reductase, and aldehyde reductase
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
enzyme termed 3alpha-hydroxysteroid/dihydrodiol dehydrogenase, structure-based catalytic mechanism analysis, ordered bi-bi mechanism
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
cofactor binding and catalytic triad, alpha/beta-barrel structure
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
enzyme is multifunctional: 3alpha-hydroxysteroid dehydrogenase activity, EC 1.1.1.50, dihydrodiol dehydrogenase activity, EC 1.3.1.20, and 9-, 11-, and15-hydroxyprostaglandin dehydrogenase activity, belongs to aldo-keto reductase superfamily
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
D-xylose dehydrogenase EC 1.1.1.179 and dihydrodiol dehydrogenase EC 1.3.1.20 both follow an ordered bi-bi mechanism and are thus considered the same enzyme
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
identical with D-xylose dehydrogenase EC 1.1.1.179
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
probably identical with aldehyde reductase EC 1.1.1.2
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
probably identical with D-xylose dehydrogenase EC 1.1.1.179
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
isoforms belong to aldo-keto reductase superfamily
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
termed AKR1C as member of the aldo-keto-superfamily, overview
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
the cytosolic, but not the microsomal, enzyme is identical with 3alpha-hydroxysteroid dehydrogenase EC 1.1.1.50
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
DD4 is identical with human chlordecone reductase and 3alpha-hydroxysteroid dehydrogenase type 1, EC 1.1.1.213, catalyzes the oxidoreduction of various 3alpha-hydroxysteroids including bile acids and belong to the aldo-keto reductase superfamily, in this concern termed AKR1C4
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
isoform DD1 is identical with 3alpha-hydroxysteroid dehydrogenase EC 1.1.1.50, while isoform DD3 is a unique benzene dihydrodiol-specific enzyme
-
trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
oxidation
redox reaction
-
-
-
-
reduction
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
trans-1,2-dihydrobenzene-1,2-diol:NADP+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
37255-32-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-acenaphthol + NADP+
acenaphthylen-1-ol + NADPH
-
Substrates: -
Products: -
Products: -
?
2-cyclohexen-1-ol + NADP+
2-cyclohexene-1-one + NADPH
-
Substrates: NAD+
Products: -
Products: -
?
3-nitrobenzaldehyde + NADPH
3-nitrobenzylalcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
5alpha-androstan-3,17-dione + NADPH
5alpha-androstan-3alpha-ol-17-one + NADP+
-
Substrates: isoform DD1, identical with 3alpha-hydroxysteroid dehydrogenase EC 1.1.1.50
Products: -
Products: -
?
5beta-pregnan-3,20-dione + NADPH
3alpha-hydroxy-5beta-pregnan-20-one + NADP+
-
Substrates: -
Products: -
Products: -
?
camphorquinone + NADPH + H+
?
Substrates: enzyme has dehydrogenase and reductase activities, enzyme is identical to NADP+-dependent D-xylose dehydrogenase
Products: -
Products: -
?
D-glucuronate + NADP+
D-glucurono-1,5-lactone + NADPH
-
Substrates: isoform DD4 no activity
Products: -
Products: -
r
DL-glyceraldehyde + NADPH
?
-
Substrates: probable identity with aldehyde reductase EC 1.1.1.2
Products: -
Products: -
?
epitestosterone + NAD(P)+
?
-
Substrates: isoform DD3: dihydrodiol dehydrogenase EC 1.3.1.20 and 3(17)alpha-hydroxysteroid dehydrogenase EC 1.1.1.59 activities reside on a single protein
Products: -
Products: -
?
glycolithocholic acid + NAD(P)+
3-oxo-glycocholanoic acid + NAD(P)H
-
Substrates: NAD+ preferred as cofactor
Products: -
Products: -
?
naphthalene dihydrodiol + NADP+
? + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
succinic semialdehyde + NADPH
?
-
Substrates: isoform DD4 low activity
Products: -
Products: -
?
testosterone + NADPH + H+
4-androsten-3alpha,17beta-diol + NADP+
-
Substrates: NAD+
Products: -
Products: -
?
tetrahydrodeoxycorticosterone + NAD(P)+
?
-
Substrates: isoform DD3: dihydrodiol dehydrogenase EC 1.3.1.20 and 3(17)alpha-hydroxysteroid dehydrogenase EC 1.1.1.59 activities reside on a single protein
Products: -
Products: -
?
trans-1,2-dihydroxy-1,2-dihydrophenanthrene + NADPH
?
-
Substrates: -
Products: -
Products: -
?
trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene + NADP+
benzo[a]-pyrene-7,8-dione + NADPH
Substrates: DD1, DD2, DD4, 3alpha-hydroxysteroid/dihydrodiol dehydrogenase
Products: product is potent carcinogen
Products: product is potent carcinogen
?
(R)-indan-1-ol + NADP+
?
-
Substrates: DD4, recombinant double mutant S145C/L311V
Products: -
Products: -
?
(R)-tetralol + NADP+
?
-
Substrates: DD4, recombinant double mutant S145C/L311V
Products: -
Products: -
?
(R)-tetralol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
(R)-tetralol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
(S)-(+)-1,2,3,4-tetrahydronaphth-1-ol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
(S)-(+)-1,2,3,4-tetrahydronaphth-1-ol + NADP+
? + NADPH
Substrates: -
Products: -
Products: -
?
(S)-indan-1-ol + NADP+
?
-
Substrates: DD4, wild-type and recombinant double mutant S145C/L311V
Products: -
Products: -
?
(S)-indan-1-ol + NADP+
?
-
Substrates: DD1, DD4, mutant CDD1-4, mutant CDD4-1
Products: -
Products: -
?
(S)-indan-1-ol + NADP+
?
Substrates: recombinant DD1, DD1, DD2
Products: -
Products: -
?
(S)-indan-1-ol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
(S)-indan-1-ol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
(S)-tetralol + NADP+
?
Substrates: DD1, DD2, recombinant DD1
Products: -
Products: -
?
(S)-tetralol + NADP+
?
-
Substrates: DD4, recombinant double mutant S145C/L311V
Products: -
Products: -
?
(S)-tetralol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
(S)-tetralol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
1-acenaphthenol + NAD(P)+
?
Substrates: recombinant: DD1, DD2, and 3alpha-hydroysteroid dehydrogenase/dihydrodiol dehydrogenase
Products: -
Products: -
?
17beta-estradiol + NAD(P)+
?
-
Substrates: isoform DD3: dihydrodiol dehydrogenase EC 1.3.1.20 and 3(17)alpha-hydroxysteroid dehydrogenase EC 1.1.1.59 activities reside on a single protein
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: low activity
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: low activity
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: low activity
Products: -
Products: -
?
2-deoxy-D-glucose + NADP+
2-deoxy-D-glucono-1,5-lactone + NADPH + H+
-
Substrates: low activity
Products: -
Products: -
?
3-keto steroid + NAD(P)H
3alpha-hydroxy steroid + NAD(P)+
-
Substrates: probably reversible reaction
Products: -
Products: -
?
3-keto steroid + NAD(P)H
3alpha-hydroxy steroid + NAD(P)+
-
Substrates: -
Products: -
Products: -
r
3-keto steroid + NAD(P)H
3alpha-hydroxy steroid + NAD(P)+
-
Substrates: reduces biologically important 3-oxo steroids of the androstane, pregnane, and cholane series
Products: -
Products: -
?
3alpha-hydroxy steroid + NADP+
3-keto steroid + NADPH
-
Substrates: not, DD3
Products: -
Products: -
?
3alpha-hydroxy steroid + NADP+
3-keto steroid + NADPH
-
Substrates: -
Products: -
Products: -
?
3alpha-hydroxy steroid + NADP+
3-keto steroid + NADPH
-
Substrates: -
Products: -
Products: -
?
3alpha-hydroxy steroid + NADP+
3-keto steroid + NADPH
-
Substrates: -
Products: -
Products: -
?
3alpha-hydroxy steroid + NADP+
3-keto steroid + NADPH
-
Substrates: -
Products: -
Products: -
?
4-chromanol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
4-chromanol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
4-nitrobenzaldehyde + NAD(P)H
4-nitrobenzylalcohol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NAD(P)H
4-nitrobenzylalcohol + NAD(P)+
-
Substrates: DD2, DD3
Products: -
Products: -
?
4-nitrobenzaldehyde + NAD(P)H
4-nitrobenzylalcohol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
4-nitrobenzaldehyde + NAD(P)H
4-nitrobenzylalcohol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
5alpha-dihydrotestosterone + NADPH + H+
5alpha-androstan-3alpha,17beta-diol + NADP+
-
Substrates: -
Products: -
Products: -
?
5alpha-dihydrotestosterone + NADPH + H+
5alpha-androstan-3alpha,17beta-diol + NADP+
-
Substrates: -
Products: -
Products: -
r
5beta-androstan-3,17-dione + NADPH
5beta-androstan-3alpha-ol-17-one + NADP+
-
Substrates: -
Products: -
Products: -
?
5beta-androstan-3,17-dione + NADPH
5beta-androstan-3alpha-ol-17-one + NADP+
-
Substrates: -
Products: -
Products: -
?
5beta-androstan-3alpha,17beta-diol + NADP+
5beta-androstan-3,17-dione + NADPH
-
Substrates: -
Products: -
Products: -
?
5beta-androstan-3alpha,17beta-diol + NADP+
5beta-androstan-3,17-dione + NADPH
Substrates: DD1, DD2, recombinant DD1
Products: -
Products: -
?
5beta-androstan-3alpha,17beta-diol + NADP+
5beta-androstan-3,17-dione + NADPH
-
Substrates: DD4 wild-type and mutants
Products: -
Products: -
?
5beta-pregnan-3,20-diol + NADP+
5beta-pregnan-20-ol-3-one + NADPH
-
Substrates: -
Products: -
Products: -
?
5beta-pregnan-3,20-diol + NADP+
5beta-pregnan-20-ol-3-one + NADPH
Substrates: DD1, DD2, recombinant DD1
Products: -
Products: -
?
androsterone + NADPH
?
-
Substrates: DD1, identical with 3alpha-hydroxysteroid dehydrogenase EC 1.1.1.50
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
Substrates: -
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
Substrates: -
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
Substrates: -
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
Substrates: -
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
Substrates: -
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
Substrates: -
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
Substrates: -
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
Substrates: -
Products: -
Products: -
?
camphorquinone + NAD(P)H
(1R)-1,7,7-trimethylbicyclo[2.2.1]heptane-2,3-diol + NADP+
-
Substrates: -
Products: -
Products: -
?
cholic acid + NADP+
?
-
Substrates: DD4, wild-type and recombinant double mutant S145C/L311V
Products: -
Products: -
?
cis-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: not:
Products: -
Products: -
?
cis-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: not:
Products: -
Products: -
?
cis-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
r
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
D-arabinose + NADP+
D-arabinono-1,4-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: only isoform DD3
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
D-galactose + NADP+
D-galactono-1,5-lactone + NADPH
-
Substrates: low activity
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: low activity
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: only isoform DD3
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: low activity
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: low activity
Products: -
Products: -
?
D-glucose + NADP+
D-glucono-1,5-lactone + NADPH + H+
-
Substrates: low activity
Products: -
Products: -
?
D-glyceraldehyde + NADPH
?
-
Substrates: DD2 and DD3 show high activity, DD4 only shows low activity
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: also low activity with L-xylose
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: also low activity with L-xylose
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: also low activity with L-xylose
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
Substrates: -
Products: -
Products: -
?
D-xylose + NADP+
D-xylono-1,5-lactone + NADPH + H+
-
Substrates: also low activity with L-xylose
Products: -
Products: -
?
L-glyceraldehyde + NADPH
?
-
Substrates: DD2 and DD3 show high activity, DD4 only shows low activity
Products: -
Products: -
?
pyridine-3-aldehyde + NADPH
?
-
Substrates: DD4 wild-type and mutants
Products: -
Products: -
?
S-(+)-1,2,3,4-tetrahydronaphth-1-ol + NADP+
? + NADPH
Substrates: -
Products: -
Products: -
?
S-(+)-1,2,3,4-tetrahydronaphth-1-ol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: DD3
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: DD3: specific for, no activity towards other alcohols, aldehydes, ketones and quinones
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
Substrates: -
Products: the reaction produces a ketol which then enolizes to the catechol
Products: the reaction produces a ketol which then enolizes to the catechol
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
r
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
Substrates: DD1, DD2, recombinant DD1
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: the reaction produces a ketol which then enolizes to the catechol
Products: the reaction produces a ketol which then enolizes to the catechol
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
r, ?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
Substrates: -
Products: the reaction produces a ketol which then enolizes to the catechol
Products: the reaction produces a ketol which then enolizes to the catechol
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
Substrates: -
Products: the reaction produces a ketol which then enolizes to the catechol
Products: the reaction produces a ketol which then enolizes to the catechol
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: the reaction produces a ketol which then enolizes to the catechol
Products: the reaction produces a ketol which then enolizes to the catechol
?
trans-benzene dihydrodiol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
trans-benzene dihydrodiol + NADP+
? + NADPH
Substrates: dehydrogenase activity
Products: -
Products: -
r
trans-naphthalene dihydrodiol + NAD(P)+
?
-
Substrates: -
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NAD(P)+
?
-
Substrates: -
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NAD(P)+
?
-
Substrates: -
Products: -
Products: -
?
trans-naphthalene dihydrodiol + NAD(P)+
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: metabolic inactivation of exogeneous xenobiotics
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the metabolism of steroid hormones and polycyclic aromatic hydrocarbons, and also in the reduction of ketone-containing drugs
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the metabolism of steroid hormones and polycyclic aromatic hydrocarbons, and also in the reduction of ketone-containing drugs
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme-mediated oxidative damage is involved in the hydroxychavicol and benzo[a]pyrene-induced toxic effects
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a member of the aldo-keto reductase superfamily, which normally reduces polycyclic aromatic hydrocarbons in the liver, it plays an important role in detoxification
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: befunolol, prostaglandin D2, progesterone
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: befunolol, prostaglandin D2, progesterone
Products: -
Products: -
?
additional information
?
-
-
Substrates: metabolic inactivation of dihydrodiols or dihydrodiol epoxides derived from carcinogenic polycylic hydrocarbons
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes formation of benz[a]anthracene-1,2-dihydrodiol which causes Cu[II]-mediated DNA damage including 8-oxo-7,8-dihydro-2-deoxyguanosine formation in the presence of NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: reduces biologically important 3-oxo steroids of the androstane, pregnane, and cholane series
Products: -
Products: -
?
additional information
?
-
-
Substrates: detoxification of polycyclic aromatic trans-hydrodiols by formation of o-quinones from the reaction product of dihydrodiol oxidation
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: hydroxy steroids
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: xenobiotic acyclic alcohols (Japanese monkey)
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: 3 forms: DD4 pI 4.2, DD3 pI 5.0 and DD2 pI 5.4, isoform DD4: strict specificity for benzene dihydrodiol and NADP+, and for reduced pyridine aldehydes, glyceraldehyde and, at low rate, for diacetyl, isoform DD3: oxidizes n-butanol, glycerol and sorbitol as well as benzene dihydrodiol in the presence of NADP+ or NAD+, and exhibits much higher reductase activity towards various aldehydes, aldoses and diacetyl
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: DD4 also catalyzes oxidoreduction of 3alpha-hydroxysteroids and bile acids and is thus thought to be identical with 3alpha-hydroxysteroid dehydrogenase EC 1.1.1.213
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: catalyzes oxidation of trans-dihydrodiols of aromatic hydrocarbons to corresponding catechols and oxidation of several pentoses
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: monomeric forms are identical with 3alpha-hydroxysteroid dehydrogenase EC 1.1.1.50 and provide a broad substrate specificity, while dimeric forms are identical with D-xylose dehydrogenase EC 1.1.1.179 and are active with trans-dihydrodiols and dicarbonyl compounds
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: hydroxy steroids
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: the enzyme transfers the 4-pro-R-hydrogen atom of NADPH to the carbonyl substrate
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: alcohols
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: NADP+ or NAD+ as cofactors
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: NADP+ or NAD+ as cofactors
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: regio- and stereospecificity
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: NADP+ or NAD+ as cofactors
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: oxidation of trans-dihydrodiols of polycyclic hydrocarbons and in this way suppression of formation of anti-diol epoxid carcinogens
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: overview about structure and utilization of trans-dihydrodiols as substrates
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: at least 2 proteins, monomeric form F2 and dimeric form F1, with both dihydrodiol dehydrogenase EC 1.3.1.20 and aldehyde reductase activity EC 1.1.1.2, F1: specifically oxidizes trans-hydrodiols of naphthalene and benzene strictly with NADP+ as cofactor, reduction of vicinal diketones, aromatic aldehydes and glyceraldes with NADPH as cofactor
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: not: hydroxy steroids
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: F2: high activity towards naphthalene dihydrodiol and some alcohols, low activity towards trans- and cis-benzene dihydrodiols and some alcohols, reduction of aldoses, vicinal diketones, aromatic aldehydes and glyceraldehydes with NADPH or NADH as cofactors
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5alpha-dihydrotestosterone + NADPH + H+
5alpha-androstan-3alpha,17beta-diol + NADP+
-
Substrates: -
Products: -
Products: -
r
camphorquinone + NADPH + H+
?
Substrates: enzyme has dehydrogenase and reductase activities, enzyme is identical to NADP+-dependent D-xylose dehydrogenase
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
r, ?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-1,2-dihydrobenzene-1,2-diol + NAD(P)+
catechol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: metabolic inactivation of exogeneous xenobiotics
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the metabolism of steroid hormones and polycyclic aromatic hydrocarbons, and also in the reduction of ketone-containing drugs
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the metabolism of steroid hormones and polycyclic aromatic hydrocarbons, and also in the reduction of ketone-containing drugs
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme-mediated oxidative damage is involved in the hydroxychavicol and benzo[a]pyrene-induced toxic effects
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a member of the aldo-keto reductase superfamily, which normally reduces polycyclic aromatic hydrocarbons in the liver, it plays an important role in detoxification
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: metabolic inactivation of dihydrodiols or dihydrodiol epoxides derived from carcinogenic polycylic hydrocarbons
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes formation of benz[a]anthracene-1,2-dihydrodiol which causes Cu[II]-mediated DNA damage including 8-oxo-7,8-dihydro-2-deoxyguanosine formation in the presence of NAD+
Products: -
Products: -
?
additional information
?
-
-
Substrates: reduces biologically important 3-oxo steroids of the androstane, pregnane, and cholane series
Products: -
Products: -
?
additional information
?
-
-
Substrates: detoxification of polycyclic aromatic trans-hydrodiols by formation of o-quinones from the reaction product of dihydrodiol oxidation
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chenodeoxycholic acid
DD2 very sensitive, DD1 less sensitive, recombinant DD1
chrysin
inhibits enzyme expression at concentrations higher than 0.01 mM; inhibits enzyme expression at concentrations higher than 0.01 mM
doxorubicin hydrochloride
-
50% inhibition at 0.000706 mM, parental 2008 cell, at 0.000377, 2008/C13* cell, at 0.000375 mM, 2008 cell expressing isoform 2
melphalan
-
50% inhibition at 0.009 mM, parental 2008 cell, at 0.0088, 2008/C13* cell, at 0.0057 mM, 2008 cell expressing isoform 2
paclitaxel
-
50% inhibition at 0.0000393 mM, parental 2008 cell, at 0.0000101, 2008/C13* cell, at 0.0000283 mM, 2008 cell expressing isoform 2
Ursodeoxycholic acid
very sensitiv: DD2, less sensitiv: DD1, recombinant DD1
vincristine
-
50% inhibition at 0.000021 mM, parental 2008 cell, at 0.000016, 2008/C13* cell, at 0.0000136 mM, 2008 cell expressing isoform 2
wogonin
inhibits enzyme expression at concentrations higher than 0.0025 mM; inhibits enzyme expression at concentrations higher than 0.0025 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
i.e. DTNB, inhibits wild-type enzyme and mutant C145S
5,5'-dithiobis(2-nitrobenzoic acid)
-
inhibits DD1 and DD3, inhibition can be overcome by androsterone for DD1 and by benzenedihydrodiol for DD3, not vice versa
carboplatin
-
50% inhibition at 0.0358 mM, parental 2008 cell, at 0.578, 2008/C13* cell, at 0.0974 mM, 2008 cell expressing isoform 1, at 0.0871 mM, 2008 cell expressing isoform 2
carboplatin
-
50% inhibition at 0.036 mM, 2008 cells, at 0.578 mM, 2008/C13* cells, at 0.097 mM, cells constitutively overexpressing enzyme
cisplatin
-
50% inhibition at 0.0021 mM, parental 2008 cell, at 0.0186, 2008/C13* cell, at 0.0161 mM, 2008 cell expressing isoform 1, at 0.0062 mM, 2008 cell expressing isoform 2
cisplatin
-
50% inhibition at 0.002 mM, 2008 cells, at 0.019 mM, 2008/C13* cells, at 0.016 mM, cells constitutively overexpressing enzyme
additional information
-
DD4 is inhibited by steroidal anti-inflammatory drugs
-
additional information
-
DD2, product inhibition and inhibition mechanism of bile acids and anti-inflammatory drugs
-
additional information
enzyme expression is not inhibited by baicalin and baicalein; enzyme expression is not inhibited by baicalin and baicalein
-
additional information
enzyme expression is not inhibited by baicalin and baicalein; enzyme expression is not inhibited by baicalin and baicalein
-
additional information
-
inhibition by nonsteroidal antiinflammatory drugs
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.32
trans-benzene dihydrodiol
3alpha-hydroxysteroid/dihydrodiol dehydrogenase
additional information
additional information
-
Km for diverse sugars
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
Camphorquinone
reduction reaction of mutant K97M, 0.1 mM NADPH
0.004
Camphorquinone
reduction reaction of mutant K79R, 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
0.015
trans-benzene dihydrodiol
3alpha-hydroxysteroid/dihydrodiol dehydrogenase
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00097
4-hydroxyacetophenone
Macaca fuscata
-
wild type enzyme, in 25 mM Tris-HCl pH 7.5, at 25°C
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 fuscata
-
mutant enzyme W254Y, in 25 mM Tris-HCl pH 7.5, at 25°C
0.075
4-hydroxyacetophenone
Macaca fuscata
-
mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C
0.078
4-hydroxyacetophenone
Macaca fuscata
-
mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C
0.083
4-hydroxyacetophenone
Macaca fuscata
-
mutant enzyme W254A, in 25 mM Tris-HCl pH 7.5, at 25°C
0.136
4-hydroxyacetophenone
Macaca fuscata
-
mutant enzyme W125Y, in 25 mM Tris-HCl pH 7.5, at 25°C
0.038
isoascorbic acid
Macaca fuscata
-
mutant enzyme W254Y, in 25 mM Tris-HCl pH 7.5, at 25°C
0.038
isoascorbic acid
Macaca fascicularis
determined in the camphorquinone reduction, inhibitor is uncompetitive with respect to camphorquinone
0.066
isoascorbic acid
Macaca fuscata
-
mutant enzyme W254A, in 25 mM Tris-HCl pH 7.5, at 25°C
0.288
isoascorbic acid
Macaca fuscata
-
mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C
3.94
isoascorbic acid
Macaca fuscata
-
mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C
4.176
isoascorbic acid
Macaca fuscata
-
mutant enzyme W125Y, in 25 mM Tris-HCl pH 7.5, at 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
0.73
-
DD4 recombinant double mutant S145C/L311V, purified, substrate (S)-indan-1-ol
26000
-
substrate 1-acenaphthol, 2008 cells constitutively overexpressing enzyme
3.9
71000
-
substrate camphorquinone, 2008 cells constitutively overexpressing enzyme
additional information
additional information
-
DDH expression in resected gastric cancer specimens correlated with mortality
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
5.8
-
F2: reduction of vicinal diketones, aromatic aldehydes and glyceraldehydes + NAD(P)H
6 - 8
-
F1: reduction of vicinal diketones, aromatic aldehydes and glyceraldehydes + NADPH
7.4
7.5
9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DD1, DD2, DD4, type 2 3alpha-hydroxysteroid/dihydrodiol dehydrogenase
UniProt
brenda
dihydrodiol dehydrogenase EC 1.3.1.20 and 3(17)alpha-hydroxysteroid dehydrogenase EC 1.1.1.59 activities reside on a single protein
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brenda
cytoplasm: dihydrodiol dehydrogenase EC 1.3.1.20 and 3alpha-hydroxysteroid dehydrogenase EC 1.1.1.5 are undistinguishable
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microsomes: dihydrodiol dehydrogenase and 3alpha-hydroxysteroid dehydrogenase are different enzymes, cytosol: dihydrodiol dehydrogenase and 3alpha-hydroxysteroid dehydrogenase activity is unseparable
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brenda
at least 2 proteins: monomeric form F2 and dimeric form F1 with both dihydrodiol dehydrogenase EC 1.3.1.20 and aldehyde reductase activity EC 1.1.1.2, F1 shows higher dihydrodiol activity, F2 shows higher aldehyde reductase activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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lung cancer cell line, high expression of enzyme isoform DDH1 and enzyme CYP1A1, and high level of DNA-benzo[a]pyrene adducts
brenda
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lung cancer cell line, high expression of enzyme isoform DDH1 and enzyme CYP1A1, and high level of DNA-benzo[a]pyrene adducts
brenda
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cisplatin-sensitive ovarian carcinoma cell line 2008 and its cisplatin-resistant variant 2008/C13*
brenda
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human oral epidermal carcinoma cell line OEC-M1, enzyme expression is induced by pretreatment with hydroxychavicol
brenda
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ovarian carcinoma cell A2780 and SKOV-3, cisplatin-sensitive and cisplatin-resistant cell 2008 and 2008/C13*, cervical carcinoma cell A431, germ-cell tumor Tera-2, lung adenocarcinoma cell Calu-6
brenda
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proximal and distal tubules of the cortex, loop of Henle of the medulla
brenda
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proximal and distal tubules of the cortex, loop of Henle of the medulla
brenda
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cisplatin-sensitive ovarian carcinoma cell line 2008 and its cisplatin-resistant variant 2008/C13*
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (1875 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
34000
35000
36000
37029
39000
65000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
the dissociation of DD into the monomer largely affects the stability rather than catalytic activity
dimer
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X-ray crystallography, the intact dimer is not essential for catalytic activity
dimer
site-directed mutagenesis has demonstrated that the intact dimer is not essential for catalytic activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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in complex with isoascorbic acid, vapour diffusion method with 2 M ammonium sulfate, 0.1 M sodium citrate buffer pH 5.0, at 20°C
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vapour diffusion at 295 K with NADPH, growth for 2 days, buffer A: 1.5 M ammoinum phosphate, 0.1 M sodium citrate, pH 5.6 + buffer B: 10 mM Tris-HCl, 2 mM 2-mercaptoethanol, pH 8.5, preliminary x-ray structure analysis
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complexed with NADP+ and testosterone, 10fold molar excess of NADP+, 'waterbug' dialysis method in 10 mM potassium phosphate buffer, pH 7.0, containing 1 mM EDTA, 1 mM 2-mrcapthoethanol, 5% acetonitrile and 0.2 mM testosterone, and crystallization in presence of polethylene glycol 8000 in hanging drops at room temperature, single crystals
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cryocrystallization: crystals were soaked in 21% polyethylene glycol 8000, 0.1 M sodium cacodylate, pH 6.4, 1.25 mM NADP+, 0.1 mM testosterone and 15% 2-methyl-2,4-pentanediol as cryoprotectant
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structure determination, cofactor and substrate binding site, and model building
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vapour diffusion at 22°C in 100 mM sodium citrate, polyethylene glycol 6000 25%, 120 mM ammonium sulfate, pH 5.8, x-ray analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y55H
-
decreased dehydrogenase activity, significant increased in reductase activity
L54V
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DD1 mutant, increase in activity towards (S)-indan-1-ol and bile-acids, increased Km for trans-benzene dihydrodiol
S145C
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native mutant with C to G replacement in DNA at position 434, no significant effect on activity
S145C/L311V
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constructed double mutant with 3 to 5fold decreased activity for xenobiotic and steroidal substrates
F279A
K97M
K97R
R148A
R148A/R202A
R202A
W254A
H79Q
C217A
-
4fold increase in Km for 5alpha-androstan-3,17-dione and 2fold increase in Km for NADH
additional information
K97M
-
mutant shows almost complete abrogation in activity for D-xylose oxidation and NADP+, and very poor activity with camphorquinone reduction and NADPH
K97R
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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
mutagenesis is performed using a QuickChange site-directed mutagenesis kit, dehydrogenase activity is comparable to that of the wild type
R148A/R202A
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very low activity, the Vmax value of the mutant enzyme is 3.7fold lower than the wild type enzyme, displays significant temperature sensitivity
R148A/R202A
mutagenesis is performed using a QuickChange site-directedmutagenesis kit
R202A
-
activity and temperature stability are similar to the wild type enzyme
R202A
mutagenesis is performed using a QuickChange site-directed mutagenesis kit, dehydrogenase activity is comparable to that of the wild type
H79Q
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site-directed mutagenesis, moderate activity with 190fold increase in Km-value, inhibition by MgCl2 and potassium phosphate
additional information
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CDD1-4 mutant consisting of DD1 with C-terminal end of DD4 shows 10-37fold increase in Km for indan-1-ol and 1,2,3,4-tetrahydronaphth-1-ol and significantly decreased activity towards androstanes, higher activity with bile-acids and 5beta-steroid than DD1
additional information
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CDD4-1 mutant consisting of DD4 with C-terminal end of DD1shows new stereospecificity toward indan-1-ol stereomers and increased Km-values with bile acids and 3-hydroxysteroids compared to DD4
additional information
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constitutive overexpression of enzyme in 2008 cells leads to induction of cisplatin resistance. In cisplatin-resistant cell-line 2008/C13*, differential expression of enzyme and four more genes is found
additional information
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knock down of enzyme isoform DHH1 expression by siRNA in CL-3 cells results in 1.4- to 2.2fold increase in DNA-benzo[a]pyrene adducts
additional information
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overexpression of enzyme in lung adenocarcinoma cell lines results in a much higher resistance to doxorubicin, cisplatin and irradiation. Isoforms DDH2 and DDH1 transfectants show higher drug and radiation resistance than DDH3 transfectants
additional information
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sequence analysis reveals high sequence homology between dimeric mammalian dihydrodiol dehydrogenases, but no homology with monomeric or cis-dihydrodiol-specific enzymes
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
45
-
dihydrodiol dehydrogenase and 3(17)alpha-hydroxysteroid dehydrogenase activity, pH 7.5, 5 min
50
-
dihydrodiol dehydrogenase and 3(17)alpha-hydroxysteroid dehydrogenase activity, pH 7.5, all activity lost
37
-
the wild type enzyme and mutant enzymes R148A and R202A are stable at 37°C
37
no activity of the 37°C-inactivated R148A/R202A mutant is recovered by the addition of 0.1 mM NADP+ and 40% glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Red Sepharose column chromatography, and Sephadex G-100 gel filtration
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at least 2 proteins: monomeric form F2 and dimeric form F1 with both dihydrodiol dehydrogenase EC 1.3.1.20 and aldehyde reductase activity EC 1.1.1.2
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co-purification of dihydrodiol and D-xylose dehydrogenase activities indicating that EC 1.1.1.179 and EC 1.3.1.20 are the same enzyme
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DD1, DD2, DD4 and 3alpha-hydroxysteroid dehydrogenase/dehydrodiol dehydrogenase, all recombinant from Escherichia coli
dihydrodiol dehydrogenase EC 1.3.1.20 and 3(17)alpha-hydroxysteroid dehydrogenase EC 1.1.1.59 activities reside on a single protein
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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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DD1, DD2, DD4, type 2 3alpha-hydroxysteroid/dihydrodiol dehydrogenase, expression in Escherichia coli
DD4, isolation of mRNA of native mutants isolated from a liver sample, synthesis of cDNA by RT-PCR, polymorphism of DD4 gene
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wild-type protein and mutants are expressed in Escherichia coli BL21 (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
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overexpression of dihydrodiol dehydrogenase as a prognostic marker in resected gastric cancer patients, patients with DDH overexpression have a significantly higher incidence of early tumor recurrence and distant metastasis
medicine
medicine
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enzyme can be used for screening of antiinflammatory potency of drugs
medicine
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enzyme overexpression is detected in 66.9% of pathological sections and in 41.6% of metastatic lymph nodes in patients with esophageal squamous cell carcinoma, the major isoform is DDH2. Enzyme overexpression is positively correlated with smoking habit, tumor stage, number of metastatic lymph nodes, lymphovascular invasion and COX-2 expression, and inversely correlated with glutathione-S-transferase and nm23-HI expression. Patients with low enzyme expression have significantly lower incidence of tumor recurrences and better survival
medicine
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expression of enzyme isoforms 1 and 2 is detected in 59.6% of pathologicla sections, enzyme expression is significantly higher in patients with tumor size over 2 cm, an in those who had early local recurrence. enzyme expression correlates with those of COX-2, interleukin-6, microsomal epoxide hydrolase and soluble epoxide hydrolase in patients. It is inversely correlated with expression of glutathione S-transferase and NADPH p450 reductase
medicine
-
enzyme may play an important role in benz[a]pyrene carcinogenesis via oxidative DNA damage
medicine
-
reduction of enzyme expression in lung tumors may contribute to an increase in DNA adduct levels and may partly be responsible for the higher susceptibility of female lung cancer patients to DNA damage. Detection of DNA adducts correlates with CYP1A1-positive tumors, but not with isoform DDH1-positive tumors
medicine
-
enzyme is expressed in a high percentage of primary ovarian tumors and may be associated with cisplatin-based chemotherapy resistance
medicine
-
resistance to doxorubicin and cisplatin in lung adenocarcinoma cell lines is closely associated with enzyme isoforms DDH1 and DDH2 activity
medicine
-
high expression level of enzyme in A431 squamous cell carcinoma, which is barely detectable in other normal or malignant cutaneous cells, including keratinocytes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Asada, Y.; Aoki, S.; Ishikura, S.; Usami, N.; Hara, A.
Roles of His-79 and Tyr-180 of D-xylose/dihydrodiol dehydrogenase in catalytic function
Biochem. Biophys. Res. Commun.
278
333-337
2000
Macaca fuscata
brenda
Aoki, S.; Ishikura, S.; Asada, Y.; Usami, N.; Hara, A.
Identity of dimeric dihydrodiol dehydrogenase as NADP+-dependent D-xylose dehydrogenase in pig liver
Chem. Biol. Interact.
130-132
775-784
2001
Canis sp., Homo sapiens, Macaca fuscata, Oryctolagus cuniculus, Sus scrofa
brenda
Nakagawa, M.; Tsukuda, F.; Nakayama, T.; Matsuura, K.; Hara, A.; Sawada, H.
Identification of two dihydrodiol dehydrogenases associated with 3(17)alpha-hydoxysteroid dehydrogenase activity in mouse kidney
J. Biochem.
106
633-638
1989
Mus musculus
brenda
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
Penning, T.M.; Sharp, R.B.; Smithgall, T.E.
Non-K-region o-quinones as enzyme-generated inactivators of dihydrodiol dehydrogenase
Biochemistry
28
4505-4511
1989
Rattus norvegicus
brenda
Hara, A.; Harada, T.; Nakagawa, M.; Matsuura, K.; Nakayama, T.; Sawada, H.
Isolation from pig lens of two proteins with dihydrodiol dehydrogenase and aldehyde reductase activities
Biochem. J.
264
403-407
1989
Sus scrofa
brenda
Smithgall, T.E.; Harvey, R.G.; Penning, T.M.
Spectroscopic identification of ortho-quinones as the products of polycyclic aromatic trans-dihydrodiol oxidation catalyzed by dihydrodiol dehydrogenase. A potential route of proximate carcinogen metabolism
J. Biol. Chem.
263
1814-1820
1988
Rattus norvegicus
brenda
Hara, A.; Mouri, K.; Sawada, H.
Purification and partial characterization of dimeric dihydrodiol dehydrogenase from monkey kidney
Biochem. Biophys. Res. Commun.
145
1260-1266
1987
Macaca fuscata
brenda
Matsuura, K.; Hara, A.; Nakayama, T.; Nakagawa, M.; Sawada, H.
Purification and properties of two multiple forms of dihydrodiol dehydrogenase from guinea-pig testis
Biochim. Biophys. Acta
912
270-277
1987
Cavia porcellus
brenda
Smithgall, T.E.; Harvey, R.G.; Penning, T.M.
Regio- and stereospecificity of homogeneous 3alpha-hydroxysteroid-dihydrodiol dehydrogenase for trans-dihydrodiol metabolites of polycyclic aromatic hydrocarbons
J. Biol. Chem.
261
6184-6191
1986
Rattus norvegicus
brenda
Boutin, J.A.; Shikita, M.; Talalay, P.
Rat liver microsomal 3alpha-hydroxysteroid dehydrogenase and dihydrodiol dehydrogenase: solubilization, separation and partial purification
Biochem. Biophys. Res. Commun.
135
795-801
1986
Rattus norvegicus
brenda
Bolcsak, L.E.; Nerland, D.E.
Purification of mouse liver benzene dihydrodiol dehydrogenases
J. Biol. Chem.
258
7252-7255
1983
Mus musculus
brenda
Vogel, K.; Bentley, P.; Platt, K.L.; Oesch, F.
Rat liver cytoplasmic dihydrodiol dehydrogenase. Purification to apparent homogeneity and properties
J. Biol. Chem.
255
9621-9625
1980
Rattus norvegicus
brenda
Terada, T.; Fujita, N.; Sugihara, Y.; Sato, R.; Takagi, T.; Maeda, M.
Site-directed mutagenesis studies of bovine liver cytosolic dihydrodiol dehydrogenase: the role of Asp-50, Tyr-55, Lys-84, His-117, Cys-145 and Cys-193 in enzymatic activity
Chem. Biol. Interact.
130-132
833-845
2001
Bos taurus
brenda
Nanjo, H.; Nishinaka, T.; Nagai, M.; Terada, T.; Mizoguchi, T.; Nishihara, T.
Unique dihydrodiol specific dehydrogenase of bovine liver: Inhibition studies and comparison with aldo/keto reductase
Adv. Exp. Med. Biol.
328
371-377
1993
Bos taurus
brenda
Kume, T.; Iwasa, H.; Shiraishi, H.; Yokoi, T.; Nagashima, K.; Otsuka, M.; Terada, T.; Takagi, T.; Hara, A.; Kamataki, T.
Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver
Pharmacogenetics
9
763-771
1999
Homo sapiens
brenda
Miyabe, Y.; Amano, T.; Deyashiki, Y.; Hara, A.; Tsukada, F.
Kinetic studies of the inhibition of a human liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase isozyme by bile acids and anti-inflammatory drugs
Biol. Pharm. Bull.
18
9-12
1995
Homo sapiens
brenda
Sato, K.; Nakanishi, M.; Deyashiki, Y.; Hara, A.; Matsuura, K.; Ohya, I.
Purification and characterization of dimeric dihydrodiol dehydrogenase from dog liver
J. Biochem.
116
711-717
1994
Canis sp.
brenda
Deyashiki, Y.; Tamada, Y.; Miyabe, Y.; Nakanishi, M.; Matsuura, K.; Hara, A.
Expression and kinetic properties of a recombinant 3alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzyme of human liver
J. Biochem.
118
285-290
1995
Homo sapiens
brenda
Nanjo, H.; Adachi, H.; Morihana, S.; Mizoguchi, T.; Nishihara, T.; Terada, T.
Enzymic characterization of a novel bovine liver dihydrodiol dehydrogenase - reaction mechanism and bile acid dehydrogenase activity
Biochim. Biophys. Acta
1244
53-61
1995
Bos taurus
brenda
Hoog, S.S.; Pawlowski, J.E.; Alzari, P.M.; Penning, T.M.; Lewis, M.
Three-dimensional structure of rat liver 3.alpha-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily
Proc. Natl. Acad. Sci. USA
91
2517-2521
1994
Rattus norvegicus
brenda
El-Kabbani, O.; Chung, R.P.T.; Ramsland, P.A.; Asada, Y.; Ishikura, S.; Usami, N.; Hara, A.
Crystallization and preliminary x-ray diffraction analysis of monkey dimeric dihydrodiol dehydrogenase
Acta Crystallogr. Sect. D
58
163-164
2002
Macaca fuscata
brenda
Hara, A.; Matsuura, K.; Tamada, Y.; Sato, K.; Miyabe, Y.; Deyashiki, Y.; Ishida, N.
Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells
Biochem. J.
313
373-376
1996
Homo sapiens (Q04828)
brenda
Burczynski, M.E.; Harvey, R.G.; Penning, T.M.
Expression and characterization of four recombinant human dihydrodiol dehydrogenase isoforms: oxidation of trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene to the activated o-quinone metabolite benzo[a]pyrene-7,8-dione
Biochemistry
37
6781-6790
1998
Homo sapiens (P42330)
brenda
Matsuura, K.; Hara, A.; Deyashiki, Y.; Iwasa, H.; Kume, T.; Ishikura, S.; Shiraishi, H.; Katagiri, Y.
Roles of the C-terminal domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: probing with chimeric enzymes
Biochem. J.
336
429-436
1998
Homo sapiens
brenda
Matsuura, K.; Deyashiki, Y.; Sato, K.; Ishida, N.; Miwa, G.; Hara, A.
Identification of amino acid residues responsible for differences in substrate specificity and inhibitor sensitivity between two human liver dihydrodiol dehydrogenase isoenzymes by site-directed mutagenesis
Biochem. J.
323
61-64
1997
Homo sapiens
brenda
Bennett, M.J.; Albert, R.H.; Jez, J.M.; Ma, H.; Penning, T.M.; Lewis, M.
Steroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3alpha-hydroxysteroid/dihydrodiol dehydrogenase
Structure
5
799-812
1997
Rattus norvegicus
brenda
Deng, H.B.; Adikari, M.; Parekh, H.K.; Simpkins, H.
Ubiquitous induction of resistance to platinum drugs in human ovarian, cervical, germ-cell and lung carcinoma tumor cells overexpressing isoforms 1 and 2 of dihydrodiol dehydrogenase
Cancer Chemother. Pharmacol.
54
301-307
2004
Homo sapiens
brenda
Seike, K.; Murata, M.; Hirakawa, K.; Deyashiki, Y.; Kawanishi, S.
Oxidative DNA damage induced by benz[a]anthracene dihydrodiols in the presence of dihydrodiol dehydrogenase
Chem. Res. Toxicol.
17
1445-1451
2004
Mus musculus
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
Wang, L.S.; Chow, K.C.; Wu, Y.C.; Lin, T.Y.; Li, W.Y.
Inverse expression of dihydrodiol dehydrogenase and glutathione-S-transferase in patients with esophageal squamous cell carcinoma
Int. J. Cancer
111
246-251
2004
Homo sapiens
brenda
Deng, H.B.; Parekh, H.K.; Chow, K.C.; Simpkins, H.
Increased expression of dihydrodiol dehydrogenase induces resistance to cisplatin in human ovarian carcinoma cells
J. Biol. Chem.
277
15035-15043
2002
Homo sapiens
brenda
Yang, M.D.; Wu, C.C.; Chiou, S.H.; Chiu, C.F.; Lin, T.Y.; Chiang, I.P.; Chow, K.C.
Reduction of dihydrodiol dehydrogenase expression in resected hepatocellular carcinoma
Oncol. Rep.
10
271-276
2003
Homo sapiens
brenda
Tang, D.W.; Chang, K.W.; Chi, C.W.; Liu, T.Y.
Hydroxychavicol modulates benzo[a]pyrene-induced genotoxicity through induction of dihydrodiol dehydrogenase
Toxicol. Lett.
152
235-243
2004
Homo sapiens
brenda
Hung, J.J.; Chow, K.C.; Wang, H.W.; Wang, L.S.
Expression of dihydrodiol dehydrogenase and resistance to chemotherapy and radiotherapy in adenocarcinoma cells of lung
Anticancer Res.
26
2949-2956
2006
Homo sapiens
brenda
Cheng, Y.W.; Tsai, H.J.; Wu, J.Y.; Hsu, Y.F.; Chen, C.Y.; Hao, N.J.; Lee, H.
A possible role for dihydrodiol dehydrogenase in the formation of benzo[a]pyrene-DNA adducts in lung cancer cells and tumor tissues
Environ. Mol. Mutagen.
48
14-21
2006
Homo sapiens
brenda
Chen, Y.J.; Yuan, C.C.; Chow, K.C.; Wang, P.H.; Lai, C.R.; Yen, M.S.; Wang, L.S.
Overexpression of dihydrodiol dehydrogenase is associated with cisplatin-based chemotherapy resistance in ovarian cancer patients
Gynecol. Oncol.
97
110-117
2005
Homo sapiens
brenda
Chow, K.C.; Lu, M.P.; Wu, M.T.
Expression of dihydrodiol dehydrogenase plays important roles in apoptosis- and drug-resistance of A431 squamous cell carcinoma
J. Dermatol. Sci.
41
205-212
2006
Homo sapiens
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
Pan, B.F.; Nelson, J.A.
Dihydrodiol dehydrogenase in drug resistance and sensitivity of human carcinomas
Cancer Chemother. Pharmacol.
59
697-702
2007
Homo sapiens
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
Wang, H.W.; Lin, C.P.; Chiu, J.H.; Chow, K.C.; Kuo, K.T.; Lin, C.S.; Wang, L.S.
Reversal of inflammation-associated dihydrodiol dehydrogenases (AKR1C1 and AKR1C2) overexpression and drug resistance in nonsmall cell lung cancer cells by wogonin and chrysin
Int. J. Cancer
120
2019-2027
2007
Homo sapiens (P52895), Homo sapiens (Q04828)
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
Chang, H.C.; Chen, Y.L.; Chan, C.P.; Yeh, K.T.; Kuo, S.J.; Ko, C.J.; Fang, H.Y.
Overexpression of dihydrodiol dehydrogenase as a prognostic marker in resected gastric cancer patients
Digest. Dis. Sci.
54
342-347
2009
Homo sapiens
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
Liu, D.; Pan, L.; Li, Z.; Cai, Y.; Miao, J.
Metabolites analysis, metabolic enzyme activities and bioaccumulation in the clam Ruditapes philippinarum exposed to benzo[a]pyrene
Ecotoxicol. Environ. Saf.
107
251-259
2014
Ruditapes philippinarum
brenda
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Release 2026.1 (March 2026)
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