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
-
+/-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
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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Purification
Purification on EC 1.3.1.20 - trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
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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