Crystallization (Comment) | Organism |
---|---|
copper-containing quercetin 2,3-dioxygenase, X-ray diffraction structure determination and analysis at 1.6 A resolution | Aspergillus japonicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | required, enzyme-bound, structure, overview. Manual docking, different geometries of the copper site | Aspergillus japonicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Aspergillus japonicus | quercetin 2,3-dioxygenase is a copper-containing enzyme that catalyzes the insertion of molecular oxygen into polyphenolic flavonols | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus japonicus | Q7SIC2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | quercetin 2,3-dioxygenase is a copper-containing enzyme that catalyzes the insertion of molecular oxygen into polyphenolic flavonols | Aspergillus japonicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | he enzyme forms homodimers, which are stabilized by an N-linked heptasaccharide at the dimer interface. The mononuclear type 2 copper center displays two distinct geometries: a distorted tetrahedral coordination, formed by His66, His68, His112, and a water molecule, and a distorted trigonal bipyramidal environment, which additionally comprises Glu73. Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance | Aspergillus japonicus |
General Information | Comment | Organism |
---|---|---|
additional information | Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance | Aspergillus japonicus |