Quercetin 2,3-dioxygenase

From Wikipedia, the free encyclopedia

In enzymology, a quercetin 2,3-dioxygenase (EC 1.13.11.24) is an enzyme that catalyzes the chemical reaction

quercetin + O₂ $\rightleftharpoons$ 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H⁺

Thus, the two substrates of this enzyme are quercetin and O₂, whereas its 3 products are 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate, CO, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O₂ as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O₂. The systematic name of this enzyme class is quercetin:oxygen 2,3-oxidoreductase (decyclizing). Other names in common use include quercetinase, and flavonol 2,4-oxygenase. It has 2 cofactors: iron, and Copper.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 6 crystal structures have been solved for this class of enzymes, with PDB accession codes 1GQG, 1GQH, 1H1I, 1H1M, 1JUH, and 2H0V.

[edit] References

IUBMB entry for 1.13.11.24
BRENDA references for 1.13.11.24 (Recommended.)
PubMed references for 1.13.11.24
PubMed Central references for 1.13.11.24
Google Scholar references for 1.13.11.24
Oka T, Simpson FJ (1971). "Quercetinase, a dioxygenase containing copper". Biochem. Biophys. Res. Commun. 43: 1–5. doi:10.1016/S0006-291X(71)80076-1. PMID 5579942.
Steiner RA, Kalk KH, Dijkstra BW (2002). "Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase". Proc. Natl. Acad. Sci. U. S. A. 99: 16625–30. doi:10.1073/pnas.262506299. PMID 12486225.
Bowater L, Fairhurst SA, Just VJ, Bornemann S (2004). "Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase". FEBS. Lett. 557: 45–8. doi:10.1016/S0014-5793(03)01439-X. PMID 14741339.