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| {{enzyme
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| | Name = quinine 3-monooxygenase
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| | EC_number = 1.14.13.67
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| | CAS_number =
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| | IUBMB_EC_number = 1/14/13/67
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| | GO_code = 0050591
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| In [[enzymology]], a '''quinine 3-monooxygenase''' ({{EC number|1.14.13.67}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :quinine + NADPH + H<sup>+</sup> + O<sub>2</sub> <math>\rightleftharpoons</math> 3-hydroxyquinine + NADP<sup>+</sup> + H<sub>2</sub>O | | [http://Www.Twitpic.com/tag/I+enjoy I enjoy] [http://www.twitpic.com/tag/Figure+skating Figure skating].<br>[http://www.burkettdesign.com/old/pdf/pres.php?casual=adidas-forum-lo-shoes adidas forum lo shoes]<br><br>Visit my web site; [http://www.twmotor.com.tw/upload/files/pres.php?asics=2014-nike-shoes 2014 nike shoes] |
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| The 4 [[substrate (biochemistry)|substrates]] of this enzyme are [[quinine]], [[nicotinamide adenine dinucleotide phosphate|NADPH]], [[hydrogen ion|H<sup>+</sup>]], and [[oxygen|O<sub>2</sub>]], whereas its 3 [[product (chemistry)|products]] are [[3-hydroxyquinine]], [[nicotinamide adenine dinucleotide phosphate|NADP<sup>+</sup>]], and [[water|H<sub>2</sub>O]].
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| This enzyme belongs to the family of [[oxidoreductase]]s, 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'''.
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| ==Structural studies==
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| As of late 2007, 5 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1W0E}}, {{PDB link|1W0F}}, {{PDB link|1W0G}}, {{PDB link|2J0D}}, and {{PDB link|2V0M}}.
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| ==References== | |
| {{reflist|1}}
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| * {{cite journal | author = Relling MV, Evans R, Dass C, Desiderio DM, Nemec J | date = 1992 | title = Human cytochrome P450 metabolism of teniposide and etoposide | journal = J. Pharmacol. Exp. Ther. | volume = 261 | pages = 491–6 | pmid = 1578365 | issue = 2 }}
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| * {{cite journal | author = S | date = 1997 | title = Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine | journal = Br. J. Clin. Pharmacol. | volume = 43 | pages = 245–52 | pmid = 9088578 | doi = 10.1046/j.1365-2125.1997.00556.x | last2 = Coville | first2 = PF | last3 = Walker | first3 = RJ | last4 = Miners | first4 = JO | last5 = Birkett | first5 = DJ | last6 = Wanwimolruk | first6 = S | issue = 3 | pmc = 2042745 }}
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| * {{cite journal | author = Zhao XJ, Kawashiro T, Ishizaki T | date = 1998 | title = Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways | journal = Drug. Metab. Dispos. | volume = 26 | pages = 188–91 | pmid = 9456308 | issue = 2 }}
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| * {{cite journal | author = Zhao XJ, Yokoyama H, Chiba K, Wanwimolruk S, Ishizaki T | date = 1996 | title = Identification of human cytochrome P450 isoforms involved in the 3-hydroxylation of quinine by human live microsomes and nine recombinant human cytochromes P450 | journal = J. Pharmacol. Exp. Ther. | volume = 279 | pages = 1327–34 | pmid = 8968357 | issue = 3 }}
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| {{1.14.13-enzyme-stub}}
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| [[Category:EC 1.14.13]]
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| [[Category:NADPH-dependent enzymes]]
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| [[Category:Enzymes of known structure]]
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I enjoy Figure skating.
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