Quinine 3-monooxygenase - Misplaced Pages

Class of enzymes

This article is an orphan, as no other articles link to it. Please introduce links to this page from related articles; try the Find link tool for suggestions. (February 2022)

quinine 3-monooxygenase

Identifiers

Databases

PDB structures

Search
PMC	articles
PubMed	articles
NCBI	proteins

In enzymology, a quinine 3-monooxygenase (EC 1.14.13.67) is an enzyme that catalyzes the chemical reaction

quinine + NADPH + H + O₂

\rightleftharpoons

3-hydroxyquinine + NADP + H₂O

The 4 substrates of this enzyme are quinine, NADPH, H, and O₂, whereas its 3 products are 3-hydroxyquinine, NADP, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is quinine,NADPH:oxygen oxidoreductase. This enzyme is also called quinine 3-hydroxylase.

Structural studies

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

References

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. PMID 1578365.
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.
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.
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. PMID 8968357.

v t e Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate	Prolyl hydroxylase HIF prolyl-hydroxylase EGLN1 EGLN2 EGLN3 P4HTM Lysyl hydroxylase AlkB ALKBH1 FTO
1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 14α-demethylase 24-hydroxycholesterol 7α-hydroxylase
1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1
1.14.15: reduced iron–sulfur protein	11B1 11B2 11A1
1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase
1.14.17: reduced ascorbate	Dopamine beta-hydroxylase
1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1
1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2 Ecdysone 20-monooxygenase Deoxyhypusine monooxygenase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

This EC 1.14.13 enzyme-related article is a stub. You can help Misplaced Pages by expanding it.

Categories: