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

1.13.11.24

flavonols

dioxygenation

bicupins

o-heterocycle

oxygenolysis

synthesis

Reaction

2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate

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

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Results	in table
5	Activating Compound
2671	AA Sequence
1	Application
1	CAS Registry Number
11	Cloned(Commentary)
1	Cofactor
4	Crystallization (Commentary)
71	Disease/ Diagnostics
2	Expression
28	General Information
1	General Stability
48	Inhibitors
1	kcat/KM [mM/s]
7	Ki Value [mM]
23	KM Value [mM]
16	Localization
70	Metals/Ions
19	Molecular Weight [Da]
42	Natural Substrates/ Products (Substrates)
160	Organism
1	Pathway
58	PDB ID
7	pH Optimum
5	pH Range
1	pH Stability
3	pI Value
7	Posttranslational Modification
9	Protein Variants
12	Purification (Commentary)
8	Reaction
3	Reaction Type
56	Reference
8	Source Tissue
18	Specific Activity [micromol/min/mg]
3	Storage Stability
95	Substrates and Products (Substrate)
18	Subunits
76	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
12	Turnover Number [1/s]

Engineering

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Engineering on EC 1.13.11.24 - quercetin 2,3-dioxygenase

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E76A

Streptomyces sp.

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

702220

E76D

Streptomyces sp. FLA

A2VA43

site-directed mutagenesis, the mutant retains marginal activity

742192

E76H

Streptomyces sp. FLA

A2VA43

site-directed mutagenesis, the mutation results in Ni- and Co-QueD variants that retain the native fold and show residual catalytic activity

742192

H69A

Streptomyces sp. FLA

A2VA43

site-directed mutagenesis, the mutant retains marginal activity

742192

H71A

Streptomyces sp. FLA

A2VA43

site-directed mutagenesis, the mutant retains marginal activity

742192

E76A

Streptomyces sp. FLA / DSM 41951

additional information

4 entries