Quinine 3-monooxygenase

Quinine 3-monooxygenase
Identifiers
EC no.1.14.14.55
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

A Quinine 3-monooxygenase (EC 1.14.14.55) is an enzyme that catalyzes the chemical reaction

 
 
O2 + H+
H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27102531.
3-hydroxyquinine
 

In humans, the multi-function protein CYP3A4 catalyzes this reaction, along with many others. The four substrates of this enzyme are quinine, reduced nicotinamide adenine dinucleotide phosphate (NADPH), oxygen, and a proton. Its products are 3-hydroxyquinine, oxidised NADP+, and water.[1][2][3]

This enzyme is a cytochrome P450 protein containing heme. This oxidoreductase, which uses molecular oxygen as oxidant is in a group with systematic name quinine,NADPH:oxygen oxidoreductase. This enzyme is also called quinine 3-hydroxylase.[1] It is present in human liver, where it is involved in the metabolism of quinine.[4][5]

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1W0E​, PDB: 1W0F​, PDB: 1W0G​, PDB: 2J0D​, and PDB: 2V0M​.

References

  1. 1 2 Enzyme 1.14.14.55 at KEGG Pathway Database.
  2. ↑ Relling MV, Evans R, Dass C, Desiderio DM, Nemec J (1992). "Human cytochrome P450 metabolism of teniposide and etoposide". J. Pharmacol. Exp. Ther. 261 (2): 491–6. doi:10.1016/S0022-3565(25)11065-3. PMID 1578365.
  3. ↑ Zhao XJ, Yokoyama H, Chiba K, Wanwimolruk S, Ishizaki T (1996). "Identification of human cytochrome P450 isoforms involved in the 3-hydroxylation of quinine by human live microsomes and nine recombinant human cytochromes P450". J. Pharmacol. Exp. Ther. 279 (3): 1327–34. doi:10.1016/S0022-3565(25)21293-9. PMID 8968357.
  4. ↑ S; Coville, PF; Walker, RJ; Miners, JO; Birkett, DJ; Wanwimolruk, S (1997). "Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine". Br. J. Clin. Pharmacol. 43 (3): 245–52. doi:10.1046/j.1365-2125.1997.00556.x. PMC 2042745. PMID 9088578.
  5. ↑ Zhao XJ, Kawashiro T, Ishizaki T (1998). "Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways". Drug Metab. Dispos. 26 (2): 188–91. PMID 9456308.