1.13.11.24: quercetin 2,3-dioxygenase

This is an abbreviated version!
For detailed information about quercetin 2,3-dioxygenase, go to the full flat file.

Word Map on EC 1.13.11.24

Reaction

quercetin
+
O2
=
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate
+
CO
+
H+

Synonyms

2,3-QD, 2,3QD, 2,4-QD, Co-QDO, Co-QueD, Cu2+-containing 2,4-QD, cupin domain-containing protein, Fe-QDO, Fe-QueD, flavonol 2,4-dioxygenase, flavonol 2,4-oxygenase, manganese quercetin 2,3-dioxygenase, manganese quercetin dioxygenase, Mn-QDO, Mn-QueD, Ni-QueD, nickel quercetinase, pirin, QDO, QdoI, QueD, quercetin 2,4-dioxygenase, quercetin dioxygenase, quercetinase, type III extradiol dioxygenase, VdQase, YxaG

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.24 quercetin 2,3-dioxygenase

Engineering

Engineering on EC 1.13.11.24 - quercetin 2,3-dioxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E76A
-
site-directed mutagenesis of Ni-QueD, exhibits marginal quercetinase activity of 0.014 unit/mg, corresponding to a more than 10000fold decrease in specific activity, Glu76 of QueD is part of the strictly conserved cupin motif and thus is assumed to be a ligand to the metal center
E76D
site-directed mutagenesis, the mutant retains marginal activity
E76H
site-directed mutagenesis, the mutation results in Ni- and Co-QueD variants that retain the native fold and show residual catalytic activity
H69A
site-directed mutagenesis, the mutant retains marginal activity
H71A
site-directed mutagenesis, the mutant retains marginal activity
E76A
Streptomyces sp. FLA / DSM 41951
-
site-directed mutagenesis of Ni-QueD, exhibits marginal quercetinase activity of 0.014 unit/mg, corresponding to a more than 10000fold decrease in specific activity, Glu76 of QueD is part of the strictly conserved cupin motif and thus is assumed to be a ligand to the metal center
-
additional information