1.3.1.20: trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
This is an abbreviated version!
For detailed information about trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, go to the full flat file.
Word Map on EC 1.3.1.20
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1.3.1.20
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dihydrodiol
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trans-dihydrodiols
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medicine
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polycyclic
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catechols
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nadp+-dependent
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benzenedihydrodiol
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indomethacin
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penning
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alpha-hydroxysteroids
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o-quinones
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talalay
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anti-diol
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1.1.1.184
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+/-trans-7,8-dihydroxy-7,8-dihydrobenzoapyrene
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non-k-region
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benzaanthracene
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alicyclic
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trans-1,2-dihydrodiols
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dicoumarol
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chrysene
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benzoapyrene-7,8-dione
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harvey
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pah-induced
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androsterone
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diagnostics
- 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
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+/-trans-7,8-dihydroxy-7,8-dihydrobenzoapyrene
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non-k-region
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benzaanthracene
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alicyclic
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trans-1,2-dihydrodiols
- dicoumarol
- chrysene
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benzoapyrene-7,8-dione
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harvey
-
pah-induced
- androsterone
- diagnostics
Reaction
Synonyms
AKR1C1, AKR1C2, DD, DDH, DDH1, DDH2, dehydrogenase, trans-1,2-dihydrobenzene-1,2-diol, DHDH, dihydrodiol dehydrogenase, More
ECTree
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Engineering
Engineering on EC 1.3.1.20 - trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
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Y55H
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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
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4fold increase in Km for 5alpha-androstan-3,17-dione and 2fold increase in Km for NADH
additional information
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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
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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
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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
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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
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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
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site-directed mutagenesis, moderate activity with 190fold increase in Km-value, inhibition by MgCl2 and potassium phosphate
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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