Изворни код странице FMO3

{{Infobox_gene}}
'''Monooksigenaza koja sadrži flavin 3''' ('''FMO3'''), takođe poznata kao '''dimetilanilinska monooksigenaza [N-oksid-formirajuća] 3''' i '''trimetilaminska monooksigenaza''', [[flavoprotein]]ski je [[enzim]] ({{EC broj-lat|1.14.13.148}}) koji je kod ljudi koriran ''FMO3'' [[gen]]om.<ref name="pmid8486388">{{cite journal |vauthors=Shephard EA, Dolphin CT, Fox MF, Povey S, Smith R, Phillips IR | title = Localization of genes encoding three distinct flavin-containing monooxygenases to human chromosome 1q | journal = Genomics | volume = 16 | issue = 1 | pages = 85–9 |date= 1993 | pmid = 8486388 | pmc =  | doi = 10.1006/geno.1993.1144 }}</ref><ref name="pmid9417913">{{cite journal |vauthors=Dolphin CT, Riley JH, Smith RL, Shephard EA, Phillips IR | title = Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA | journal = Genomics | volume = 46 | issue = 2 | pages = 260–7 |date= 1998 | pmid = 9417913 | pmc =  | doi = 10.1006/geno.1997.5031 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FMO3 flavin containing monooxygenase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2328| accessdate = }}</ref><ref name="BRENDA FMO3 Homo sapiens" /> Ovaj enzim [[kataliza|katalizuje]] sledeću [[hemijska reakcija|hemijsku reakciju]]:<ref name="BRENDA FMO3 Homo sapiens" />
: ''N'',''N'',''N''-trimetilamin + NADPH + H<sup>+</sup> + O<sub>2</sub> <math>\rightleftharpoons</math> ''N'',''N'',''N''-trimetilamin ''N''-oksid + NADP<sup>+</sup> + H<sub>2</sub>O

FMO3 je glavni [[izoenzim]] [[Dimetilanilin monooksigenaza (formiranje N-oksida)|monooksigenaze koja sadrži flavin]] koja je izražena u jetri odraslih osoba.<ref name="BRENDA FMO3 Homo sapiens" /><ref name="FMO" /><ref name="FMO3 2007 review" /> Ljudski FMO3 enzim katalizuje nekoliko tipova reakcija, uključujući: ''N''-oksigenaciju primarnih, sekundarnih, i tercijarnih [[amin]]a;<ref name="FMO" /><ref name="FMO3 2000 review" /> ''S''-oksigenaciju [[nukleofil]]nih jedinjenja koja sadrže [[sumpor]];<ref name="FMO" /><ref name="FMO3 2000 review" /> i 6-metilhidroksilaciju [[Vadimezan|DMXAA]].<ref name="FMO" /><ref name="DMXAA primary">{{cite journal | vauthors = Zhou S, Kestell P, Paxton JW | title = 6-methylhydroxylation of the anti-cancer agent 5,6-dimethylxanthenone-4-acetic acid (DMXAA) by flavin-containing monooxygenase 3 | journal = Eur J Drug Metab Pharmacokinet | volume = 27 | issue = 3 | pages = 179–183 |year=2002| pmid = 12365199 | doi = | quote = Only FMO3 formed 6-OH-MXAA at a similar rate to that in cDNA-expressed cytochromes P-450 (CYP)1A2. The results of this study indicate that human FMO3 has the capacity to form 6-OH-MXAA, but plays a lesser important role for this reaction than CYP1A2 that has been demonstrated to catalyse 6-OH-MXAA formation.}}</ref> 

FMO3 je primarni enzim kod ljudi koji katalizuje [[N-oksidacija|''N''-oksidaciju]] [[trimetilamin]]a u [[trimetilamin N-oksid|trimetilamin ''N''-oksid]];<ref name="BRENDA FMO3 Homo sapiens" /><ref name="FMO3 2007 review" /> [[FMO1]] takođe ''N''-oksigeniše trimetilamin, mada u znatno manjoj meri od FMO3.<ref name="Review - TMA1+TMA2 N-oxygenate TMA">{{cite journal | vauthors = Tang WH, Hazen SL | title = The contributory role of gut microbiota in cardiovascular disease | journal = J. Clin. Invest. | volume = 124 | issue = 10 | pages = 4204–4211 |year=2014| pmid = 25271725 | pmc = 4215189 | doi = 10.1172/JCI72331 | quote = In recent studies each of the FMO family members were cloned and expressed, to determine which possessed synthetic capacity to use TMA as a substrate to generate TMAO. FMO1, FMO2, and FMO3 were all capable of forming TMAO, though the specific activity of FMO3 was at least 10-fold higher than that the other FMOs (54). Further, FMO3 overexpression in mice significantly increased plasma TMAO levels, while silencing FMO3 decreased TMAO levels (54). In both humans and mice, hepatic FMO3 expression was observed to be reduced in males compared with females (25, 54) and could be induced by dietary bile acids through a mechanism that involves FXR (54). }}</ref><ref name="FMO1 also metabolizes TMA - primary source">{{cite journal | vauthors = Bennett BJ, de Aguiar Vallim TQ, Wang Z, Shih DM, Meng Y, Gregory J, Allayee H, Lee R, Graham M, Crooke R, Edwards PA, Hazen SL, Lusis AJ | title = Trimethylamine-N-oxide, a metabolite associated with atherosclerosis, exhibits complex genetic and dietary regulation | journal = Cell Metab. | volume = 17 | issue = 1 | pages = 49–60 | year = 2013 | pmid = 23312283 | pmc = 3771112 | doi = 10.1016/j.cmet.2012.12.011 | quote = Circulating trimethylamine-N-oxide (TMAO) levels are strongly associated with atherosclerosis. We now examine genetic, dietary, and hormonal factors regulating TMAO levels. We demonstrate that two flavin mono-oxygenase family members, FMO1 and FMO3, oxidize trimethylamine (TMA), derived from gut flora metabolism of choline, to TMAO. Further, we show that FMO3 exhibits 10-fold higher specific activity than FMO1.}}</ref> Genetičke deficijencije FMO3 enzima uzrokuju [[primarna trimetilaminurija|primarnu trimetilaminuriju]], takođe poznatu kao "sindrom ribljeg zadaha".<ref name="BRENDA FMO3 Homo sapiens" /><ref name="FMO3, trimethylamine, and fish-odor syndrome">{{cite journal | vauthors = Dolphin CT, Janmohamed A, Smith RL, Shephard EA, Phillips IR | title = Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome | journal = Nat. Genet. | volume = 17 | issue = 4 | pages = 491–4 | year = 1997 | pmid = 9398858 | doi = 10.1038/ng1297-491 | url = }}</ref> FMO3 isto tako učestvuje u metabolizmu mnogih [[ksenobiotik]]a (i.e., egzogenih jedinjenja koja nisu normalno prisutn u telu),<ref name="FMO" /><ref name="FMO3 2007 review" /> kao što je [[oksidativna deaminacija]] [[amfetamin]]a.<ref name="FMO">{{cite journal |vauthors=Krueger SK, Williams DE | title = Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism | journal = Pharmacol. Ther. | volume = 106 | issue = 3 | pages = 357–387 |date= 2005 | pmid = 15922018 | pmc = 1828602 | doi = 10.1016/j.pharmthera.2005.01.001|quote=A second precaution with respect to predicting FMO enzyme substrate specificity is that factors other than size and charge must play a role, but these parameters are not well understood. An example is the high selectivity observed with human FMO3, compared to the other FMO enzymes, in the N-oxygenation of the important constitutive substrate trimethylamine (Lang et al., 1998).&nbsp;... The most efficient human FMO in phenethylamine N-oxygenation is FMO3, the major FMO present in adult human liver; the Km is between 90 and 200 μM (Lin & Cashman, 1997b).&nbsp;... Of particular significance for this review is that individuals homozygous for certain FMO3 allelic variants (e.g., null variants) also demonstrate impaired metabolism toward other FMO substrates including ranitidine, nicotine, thio-benzamide, and phenothiazine derivatives (Table 4; Cashman et al., 1995, 2000; Kang et al., 2000; Cashman, 2002; Park et al., 2002; Lattard et al., 2003a, 2003b).&nbsp;... The metabolic activation of ethionamide by the bacterial FMO is the same as the mammalian FMO activation of thiobenzamide to produce hepatotoxic sulfinic and sulfinic acid metabolites. Not surprisingly, Dr. Ortiz de Montellano’s laboratory and our own have found ethionamide to be a substrate for human FMO1, FMO2, and FMO3 (unpublished observations).}}<br />[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1828602/table/T5/ Table 5: N-containing drugs and xenobiotics oxygenated by FMO]<br />[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1828602/table/T6/ Table 6: S-containing drugs and xenobiotics oxygenated by FMO]<br />[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1828602/table/T7/ Table 7: FMO activities not involving S- or N-oxygenation]</ref><ref name="Substituted amphetamines, FMO, and DBH">{{cite book | author = Glennon RA |veditors=Lemke TL, Williams DA, Roche VF, Zito W | title=Foye's principles of medicinal chemistry | date=2013 | publisher=Wolters Kluwer Health/Lippincott Williams & Wilkins | location=Philadelphia, USA | isbn=9781609133450 | pages=646–648 | edition=7th | section-url=https://books.google.com/books?id=Sd6ot9ul-bUC&pg=PA646&q=substituted%20derivatives%20substituents%20hydroxyamphetamine%20flavin%20monooxygenase#v=onepage | accessdate = 11. 09. 2015 | section=Phenylisopropylamine stimulants: amphetamine-related agents | quote=The simplest unsubstituted phenylisopropylamine, 1-phenyl-2-aminopropane, or amphetamine, serves as a common structural template for hallucinogens and psychostimulants. Amphetamine produces central stimulant, anorectic, and sympathomimetic actions, and it is the prototype member of this class (39).&nbsp;... The phase 1 metabolism of amphetamine analogs is catalyzed by two systems: cytochrome P450 and flavin monooxygenase.}}</ref><ref name="FMO3-Primary">{{cite journal |vauthors=Cashman JR, Xiong YN, Xu L, Janowsky A | title = N-oxygenation of amphetamine and methamphetamine by the human flavin-containing monooxygenase (form 3): role in bioactivation and detoxication | journal = J. Pharmacol. Exp. Ther. | volume = 288 | issue = 3 | pages = 1251–1260 |year=1999|pmid = 10027866 }}</ref>

== Ligandi ==

{| class="wikitable"
|+'''Spisak ljudskih FMO3 supstrata, inhibitora, pobu]ivača, i aktivatora'''
|-
! FMO3 [[Supstrat (hemija)|substrati]]
! FMO3 [[Inhibitor enzima|inhibitori]]
! FMO3 [[Enzimski pobuđivač|pobuđivači]]
! FMO3 [[Enzimski aktivator|aktivatori]]
|- style="vertical-align: top;"
|<!--below this line is the list of FMO3 substrates-->
;Endogeni [[biomolekul]]i
* [[Epinefrin]]<ref name="FMO3 catecholamines">{{cite journal | vauthors = Robinson-Cohen C, Newitt R, Shen DD, Rettie AE, Kestenbaum BR, Himmelfarb J, Yeung CK | title = Association of FMO3 Variants and Trimethylamine N-Oxide Concentration, Disease Progression, and Mortality in CKD Patients | journal = PLoS ONE | volume = 11 | issue = 8 | pages = e0161074 |year=2016| pmid = 27513517 | pmc = 4981377 | doi = 10.1371/journal.pone.0161074 | quote = TMAO is generated from trimethylamine (TMA) via metabolism by hepatic flavin-containing monooxygenase isoform 3 (FMO3).&nbsp;... FMO3 catalyzes the oxidation of catecholamine or catecholamine-releasing vasopressors, including tyramine, phenylethylamine, adrenaline, and noradrenaline [32, 33].}}</ref>
* [[Norepinefrin]]<ref name="FMO3 catecholamines" />
* [[Fenetilamin]]<sup>†</sup><ref name="FMO" /><ref name="FMO3 catecholamines" />
* [[Trimetilamin]]<sup>†</sup><ref name="FMO" /><ref name="FMO3 2007 review" /><ref name="FMO3 catecholamines" />
* [[Tiramin]]<ref name="BRENDA FMO3 Homo sapiens" /><ref name="FMO" /><ref name="FMO3 catecholamines" />
;Značajni egogeni [[ksenobiotik|ksenobiotici]]
* [[Amfetamin]]<sup>†</sup> i njegovi hidroksilaminski [[Metabolički intermedijer|intermedijari]]<ref name="FMO" /><ref name="FMO3-Primary" />
* [[Benzidamin]]<ref name="BRENDA FMO3 Homo sapiens" /><ref name="FMO" />
* [[Cimetidin]]<ref name="FMO3 2007 review">{{cite journal | vauthors = Hisamuddin IM, Yang VW | title = Genetic polymorphisms of human flavin-containing monooxygenase 3: implications for drug metabolism and clinical perspectives | journal = Pharmacogenomics | volume = 8 | issue = 6 | pages = 635–643 | date= 2007 | pmid = 17559352 | pmc = 2213907 | doi = 10.2217/14622416.8.6.635 | quote = Other drug substrates have been used for both in vitro and in vivo analyses.&nbsp;... FMO3 is the most abundantly expressed FMO in the adult human liver [12]. Its structure and function and the implications of its polymorphisms have been widely studied [8,12,13]. This enzyme has a wide substrate specificity, including the dietary-derived tertiary amines trimethylamine, tyramine and nicotine; commonly used drugs including cimetidine, ranitidine, clozapine, methimazole, itopride, ketoconazole, tamoxifen and sulindac sulfide; and agrichemicals, such as organophosphates and carbamates [14–22].}}</ref><ref name="FMO3 2000 review">{{cite journal | vauthors = Cashman JR | title = Human flavin-containing monooxygenase: substrate specificity and role in drug metabolism | journal = Curr. Drug Metab. | volume = 1 | issue = 2 | pages = 181–191 |year=2000| pmid = 11465082 | doi = | quote = Human FMO3 N-oxygenates primary, secondary and tertiary amines whereas human FMO1 is only highly efficient at N-oxygenating tertiary amines. Both human FMO1 and FMO3 S-oxygenate a number of nucleophilic sulfur-containing substrates and in some cases, does so with great stereoselectivity.&nbsp;... For amines with smaller aromatic substituents such as phenethylamines, often these compounds are efficiently N-oxygenated by human FMO3.&nbsp;... (S)-Nicotine N-1'-oxide formation can also be used as a highly stereoselective probe of human FMO3 function for adult humans that smoke cigarettes. Finally, cimetidine S-oxygenation or ranitidine N-oxidation can also be used as a functional probe of human FMO3. With the recent observation of human FMO3 genetic polymorphism and poor metabolism phenotype in certain human populations, variant human FMO3 may contribute to adverse drug reactions or exaggerated clinical response to certain medications.}}</ref>
* [[Klozapin]]<ref name="FMO" /><ref name="FMO3 2007 review" />
* ''N''-Deacetil [[ketokonazol]]<ref name="FMO" />
* [[DMXAA]]<sup>†</sup><ref name="FMO" /><ref name="DMXAA primary" />
* [[Etionamid]]<ref name="BRENDA FMO3 Homo sapiens" /><ref name="FMO" />
* [[Itoprid]]<ref name="FMO" /><ref name="FMO3 2007 review" />
* [[Metamfetamin]] i njegovi hidroksilaminski intermedijari<ref name="FMO" /><ref name="FMO3-Primary" />
* [[Metimazol]]<ref name="BRENDA FMO3 Homo sapiens" /><ref name="FMO3 2007 review" />
* [[Nikotin]] – only the (''S'')-(&minus;)-nicotine [[enantiomer]]<ref name="FMO" /><ref name="FMO3 2000 review" />
* [[Olopatadin]]<ref name="FMO" />
* [[Fenotiazin]]i – 2-(Trifluorometilni) [[strukturni analog|analozi]]<ref name="FMO" />
* [[Ranitidin]]<ref name="FMO" /><ref name="FMO3 2000 review" />
* [[Sulindak]] sulfide<ref name="BRENDA FMO3 Homo sapiens" /><ref name="FMO" />
* [[Tamoksifen]]<ref name="FMO" /><ref name="FMO3 2007 review" />
* [[Tiobenzamid]]<ref name="FMO" />
* [[Ksanomelin]]<ref name="FMO" />
|| <!--below this line is the list of FMO3 inhibitors-->
* [[Tioureja]]<ref name="BRENDA FMO3 Homo sapiens">{{cite encyclopedia | title=Trimethylamine monooxygenase (Homo sapiens)| url=http://www.brenda-enzymes.info/enzyme.php?ecno=1.14.13.148&Suchword=&reference=&organism%5B%5D=Homo+sapiens&show_tm=0 | work=BRENDA | publisher=Technische Universität Braunschweig | accessdate = 18. 09. 2016 | date= 2016 | quote = trimethylaminuria (fish-odor syndrome) is associated with defective hepatic N-oxidation of dietary-derived trimethylamine catalyzed by flavin-containing monooxygenase&nbsp;... FMO3 deficiency results in trimethylaminuria or the fish-like odour syndrome&nbsp;... isozyme FMO3 regulates the conversion of N,N,N-trimethylamine into its N-oxide and hence controls the release of volatile N,N,N-trimethylamine from the individual}}</ref>
*
|| <!--below this line is the list of FMO3 inducers-->
*
*
||<!--below this line is the list of FMO3 activators-->
* [[Hlorpromazin]]<ref name="BRENDA FMO3 Homo sapiens" />
* [[Imipramin]]<ref name="BRENDA FMO3 Homo sapiens" />
|-
! scope="col" colspan="4" style="text-align:center; background:papayawhip" | <small>{{nobold|Simbol <sup>†</sup> označava umerenu do kompletne selektivnosti za FMO3 relativno na druge [[Dimetilanilin monooksigenaza (formiranje N-oksida)|FMO]] izoenzime.}}</small>
|}

== Vidi još ==
* [[Dimetilanilin monooksigenaza (formiranje N-oksida)|Monooskigenaze koje sadrže flavin]]
* [[Trimetilaminurija]]
* [[Dimetilanilin monooksigenaza (formiranje N-oksida)]]

== Reference ==
{{reflist|2}}

== Literatura ==
{{Литература | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  |vauthors=Cashman JR, Park SB, Berkman CE, Cashman LE |title=Role of hepatic flavin-containing monooxygenase 3 in drug and chemical metabolism in adult humans. |journal=Chem. Biol. Interact. |volume=96 |issue= 1 |pages= 33–46 |year= 1995 |pmid= 7720103 |doi=10.1016/0009-2797(94)03581-R  }}
*{{cite journal  | author=Cashman JR |title=The implications of polymorphisms in mammalian flavin-containing monooxygenases in drug discovery and development. |journal=Drug Discov. Today |volume=9 |issue= 13 |pages= 574–81 |year= 2004 |pmid= 15203093 |doi= 10.1016/S1359-6446(04)03136-8 }}
*{{cite journal  |vauthors=Zhou J, Shephard EA |title=Mutation, polymorphism and perspectives for the future of human flavin-containing monooxygenase 3. |journal=Mutat. Res. |volume=612 |issue= 3 |pages= 165–71 |year= 2006 |pmid= 16481213 |doi= 10.1016/j.mrrev.2005.09.001 }}
*{{cite journal  |vauthors=Lomri N, Gu Q, Cashman JR |title=Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1685–9 |year= 1992 |pmid= 1542660 |doi=10.1073/pnas.89.5.1685  | pmc=48517  }}
*{{cite journal  |vauthors=Humbert JA, Hammond KB, Hathaway WE |title=Trimethylaminuria: the fish-odour syndrome. |journal=Lancet |volume=2 |issue= 7676 |pages= 770–1 |year= 1970 |pmid= 4195988 |doi=10.1016/S0140-6736(70)90241-2  }}
*{{cite journal  |vauthors=Higgins T, Chaykin S, Hammond KB, Humbert JR |title=Trimethylamine N-oxide synthesis: a human variant. |journal=Biochemical medicine |volume=6 |issue= 4 |pages= 392–6 |year= 1972 |pmid= 5048998 |doi=10.1016/0006-2944(72)90025-7  }}
*{{cite journal  |vauthors=Lomri N, Gu Q, Cashman JR |title=Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 21 |pages= 9910 |year= 1995 |pmid= 7568243 |doi=10.1073/pnas.92.21.9910  | pmc=40912  }}
*{{cite journal  |vauthors=Bhamre S, Bhagwat SV, Shankar SK |title=Flavin-containing monooxygenase mediated metabolism of psychoactive drugs by human brain microsomes. |journal=Brain Res. |volume=672 |issue= 1–2 |pages= 276–80 |year= 1995 |pmid= 7749747 |doi=10.1016/0006-8993(94)01135-5  |display-authors=etal}}
*{{cite journal  |vauthors=Cashman JR, Park SB, Yang ZC |title=Chemical, enzymatic, and human enantioselective S-oxygenation of cimetidine |journal=Drug Metab. Dispos. |volume=21 |issue= 4 |pages= 587–97 |year= 1993 |pmid= 8104117 |doi=  |display-authors=etal}}
*{{cite journal  |vauthors=Park SB, Jacob P, Benowitz NL, Cashman JR |title=Stereoselective metabolism of (S)-(−)-nicotine in humans: formation of trans-(S)-(−)-nicotine N-1'-oxide |journal=Chem. Res. Toxicol. |volume=6 |issue= 6 |pages= 880–8 |year= 1994 |pmid= 8117928 |doi=10.1021/tx00036a019  }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  |vauthors=Dolphin CT, Cullingford TE, Shephard EA |title=Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04 |journal=Eur. J. Biochem. |volume=235 |issue= 3 |pages= 683–9 |year= 1996 |pmid= 8654418 |doi=10.1111/j.1432-1033.1996.00683.x  |display-authors=etal}}
*{{cite journal  |vauthors=Chung WG, Cha YN |title=Oxidation of caffeine to theobromine and theophylline is catalyzed primarily by flavin-containing monooxygenase in liver microsomes |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 685–8 |year= 1997 |pmid= 9207220 |doi= 10.1006/bbrc.1997.6866 }}
*{{cite journal  |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |display-authors=etal}}
*{{cite journal  |vauthors=Treacy EP, Akerman BR, Chow LM |title=Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication |journal=Hum. Mol. Genet. |volume=7 |issue= 5 |pages= 839–45 |year= 1998 |pmid= 9536088 |doi=10.1093/hmg/7.5.839  |display-authors=etal}}
*{{cite journal  |vauthors=Akerman BR, Forrest S, Chow L |title=Two novel mutations of the FMO3 gene in a proband with trimethylaminuria |journal=Hum. Mutat. |volume=13 |issue= 5 |pages= 376–9 |year= 1999 |pmid= 10338091 |doi= 10.1002/(SICI)1098-1004(1999)13:5<376::AID-HUMU5>3.0.CO;2-A |display-authors=etal}}
}}
{{Литература крај}}

== Spoljašnje veze ==
* {{MeshName|Trimethylamine+monooxygenase}}
* [http://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=trimethylaminuria Primary Trimethylaminuria (FMO3 Deficiency)] – NCBI bookshelf [[GeneReviews]] entry

{{Dioxygenases}}
{{Enzimi-lat}}
{{Portal bar-lat|Molekularna i ćelijska biologija|Hemija}}

{{normativna kontrola}}

[[Категорија:Супституисани амфетамини]]
[[Категорија:Флавопротеински ензими]]
[[Категорија:Амфетамин]]