Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Reaction

trans-1,2-Dihydrobenzene-1,2-diol
+
NADP+
=
catechol
+
NADPH
+
H+

Synonyms

AKR1C1, AKR1C2, DD, DDH, DDH1, DDH2, dehydrogenase, trans-1,2-dihydrobenzene-1,2-diol, DHDH, dihydrodiol dehydrogenase, More

ECTree

     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

Purification

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Red Sepharose column chromatography, and Sephadex G-100 gel filtration
-
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
-
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
-
DD1 and DD3
-
DD1, DD2, DD3, DD4
-
DD1, DD2, DD4 and 3alpha-hydroxysteroid dehydrogenase/dehydrodiol dehydrogenase, all recombinant from Escherichia coli
DD1, DD4, CDD1-4, CDD4-1, all recombinant from Escherichia coli
-
DD1, recombinant from Escherichia coli
DD3, recombinant, His-tagged protein from Escherichia coli
-
DD4 double mutant S145C/L311V 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
-
enzyme forms: DD1, DD3
-
purified from microsomes
-
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
wild-type and mutant protein recombinant from Escherichia coli
-