| EC |
1.13.11.24 |
| Accepted name: |
quercetin 2,3-dioxygenase |
| Reaction: |
quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+ |
|
For diagram of reaction, click here |
| Other name(s): |
quercetinase; flavonol 2,4-oxygenase; quercetin:oxygen 2,3-oxidoreductase (decyclizing) |
| Systematic name: |
quercetin:oxygen 2,3-oxidoreductase (ring-opening) |
| Comments: |
The enzyme from Aspergillus sp. is a copper protein whereas that from Bacillus subtilis contains iron. Quercetin is a flavonol (5,7,3′,4′-tetrahydroxyflavonol). |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-67-6 |
| References: |
| 1. |
Oka, T. and Simpson, F.J. Quercetinase, a dioxygenase containing copper. Biochem. Biophys. Res. Commun. 43 (1971) 1–5. [DOI] [PMID: 5579942] |
| 2. |
Steiner, R.A., Kalk, K.H. and Dijkstra, B.W. Anaerobic enzyme·substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc. Natl. Acad. Sci. USA 99 (2002) 16625–16630. [DOI] [PMID: 12486225] |
| 3. |
Bowater, L., Fairhurst, S.A., Just, V.J. and Bornemann, S. Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase. FEBS Lett. 557 (2004) 45–48. [DOI] [PMID: 14741339] |
|
| [EC 1.13.11.24 created 1972] |
| |
|
| |
|
Printable version