FMO5

FMO5
Identifikatori
AlijasiFMO5
Spoljašnji IDOMIM: 603957 MGI: 1310004 HomoloGene: 68185 GeneCards: FMO5
Genska lokacija (miš)
Chromosome 3 (mouse)
Hr.Chromosome 3 (mouse)[1]
Chromosome 3 (mouse)
Genomska lokacija za FMO5
Genomska lokacija za FMO5
Band3|3 F2.2Start97,536,120 bp[1]
Kraj97,562,598 bp[1]
Obrazac RNK izražavanja


More reference expression data
Genska ontologija
Molecular function• oxidoreductase activity
• N,N-dimethylaniline monooxygenase activity
• NADP binding
• flavin adenine dinucleotide binding
• monooxygenase activity
Cellular component• organelle membrane
• саставни део мембране
• endoplasmic reticulum membrane
• ендоплазматични ретикулум
• мембрана
• intracellular membrane-bounded organelle
• цитосол
Biological process• GO:0022610 биолошки процес
Sources:Amigo / QuickGO
Ortolozi
VrsteČovekMiš
Entrez

2330

14263

Ensembl

ENSG00000131781

ENSMUSG00000028088

UniProt

P49326

P97872

RefSeq (mRNA)

NM_001144829
NM_001144830
NM_001461

NM_001161763
NM_001161765
NM_010232
NM_001355119

RefSeq (protein)

NP_001138301
NP_001138302
NP_001452

NP_001155235
NP_001155237
NP_034362
NP_001342048

Location (UCSC)n/aChr 3: 97.54 – 97.56 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Dimetilanilin monooksigenaza (N-oksid-formirajuća) 5 je enzim koji je kod ljudi kodiran FMO5 genom.[4][5][6]

Metabolička N-oksidacija amino-trimetilamina (TMA) iz hrane je posredovana monooksigenazom koja sadrži flavin. Ovaj gen ispoljava nasledni FMO3 polimorfizam kod ljudi koji rezultira u maloj potpopulaciji sa umanjenom TMA N-oksidacionom sposobnošću, posledica čega je sindrom zadaha ribe, trimetilaminurija. Tri forme ovog enzima, FMO1 u fetalnoj jetri, FMO2 u jetri odraslih osoba, i FMO3 su kodirani genima koji su grupisani u 1q23-q25 regionu. Monooksigenze koje sadrže flavin su NADPH zavisni flavoenzimi koji katalizuju oksidaciju nukleofilnih heteroatomskih centera ksenobiotika kao što su pesticidi i lekovi.[6]

Vidi još

  • Dimetilanilin monooksigenaza (formiranje N-oksida)

Reference

  1. ^ а б в GRCm38: Ensembl release 89: ENSMUSG00000028088 - Ensembl, May 2017
  2. ^ „Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  3. ^ „Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  4. ^ McCombie RR, Dolphin CT, Povey S, Phillips IR, Shephard EA (1996). „Localization of human flavin-containing monooxygenase genes FMO2 and FMO5 to chromosome 1q”. Genomics. 34 (3): 426—9. PMID 8786146. doi:10.1006/geno.1996.0308. 
  5. ^ Gelb BD, Zhang J, Cotter PD, Gershin IF, Desnick RJ (1997). „Physical mapping of the human connexin 40 (GJA5), flavin-containing monooxygenase 5, and natriuretic peptide receptor a genes on 1q21”. Genomics. 39 (3): 409—11. PMID 9119381. doi:10.1006/geno.1996.4516. 
  6. ^ а б „Entrez Gene: FMO5 flavin containing monooxygenase 5”. 

Literatura

  • Hines RN, Cashman JR, Philpot RM, et al. (1994). „The mammalian flavin-containing monooxygenases: molecular characterization and regulation of expression.”. Toxicol. Appl. Pharmacol. 125 (1): 1—6. PMID 8128486. doi:10.1006/taap.1994.1042. 
  • Phillips IR, Dolphin CT, Clair P, et al. (1995). „The molecular biology of the flavin-containing monooxygenases of man.”. Chem. Biol. Interact. 96 (1): 17—32. PMID 7720101. doi:10.1016/0009-2797(94)03580-2. 
  • Overby LH, Buckpitt AR, Lawton MP, et al. (1995). „Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog.”. Arch. Biochem. Biophys. 317 (1): 275—84. PMID 7872795. doi:10.1006/abbi.1995.1163. 
  • Maruyama K, Sugano S (1994). „Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.”. Gene. 138 (1–2): 171—4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8. 
  • Lawton MP, Cashman JR, Cresteil T, et al. (1994). „A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities”. Arch. Biochem. Biophys. 308 (1): 254—7. PMID 8311461. doi:10.1006/abbi.1994.1035. 
  • Overby LH, Carver GC, Philpot RM (1997). „Quantitation and kinetic properties of hepatic microsomal and recombinant flavin-containing monooxygenases 3 and 5 from humans”. Chem. Biol. Interact. 106 (1): 29—45. PMID 9305407. doi:10.1016/S0009-2797(97)00055-0. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). „Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library”. Gene. 200 (1–2): 149—56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3. 
  • Chung WG, Park CS, Roh HK, et al. (2001). „Oxidation of ranitidine by isozymes of flavin-containing monooxygenase and cytochrome P450”. Jpn. J. Pharmacol. 84 (2): 213—20. PMID 11128045. doi:10.1254/jjp.84.213. 
  • Janmohamed A, Dolphin CT, Phillips IR, Shephard EA (2001). „Quantification and cellular localization of expression in human skin of genes encoding flavin-containing monooxygenases and cytochromes P450”. Biochem. Pharmacol. 62 (6): 777—86. PMID 11551524. doi:10.1016/S0006-2952(01)00718-3. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). „Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899—903. PMC 139241 Слободан приступ. PMID 12477932. doi:10.1073/pnas.242603899. 
  • Krause RJ, Lash LH, Elfarra AA (2003). „Human kidney flavin-containing monooxygenases and their potential roles in cysteine s-conjugate metabolism and nephrotoxicity”. J. Pharmacol. Exp. Ther. 304 (1): 185—91. PMID 12490590. doi:10.1124/jpet.102.042911. 
  • Furnes B, Feng J, Sommer SS, Schlenk D (2003). „Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans”. Drug Metab. Dispos. 31 (2): 187—93. PMID 12527699. doi:10.1124/dmd.31.2.187. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). „Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40—5. PMID 14702039. doi:10.1038/ng1285. 
  • Zhang J, Cashman JR (2006). „Quantitative analysis of FMO gene mRNA levels in human tissues”. Drug Metab. Dispos. 34 (1): 19—26. PMID 16183778. doi:10.1124/dmd.105.006171. 
  • Gregory SG, Barlow KF, McLay KE, et al. (2006). „The DNA sequence and biological annotation of human chromosome 1”. Nature. 441 (7091): 315—21. PMID 16710414. doi:10.1038/nature04727. 
  • п
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1.14.11: 2-oksoglutarat1.14.13: NADH ili NADPH
1.14.14: redukuje flavin ili flavoprotein
1.14.15: redukuje gvožđe-sumporni protein
1.14.16: redukuje pteridin (BH4 zavisni)1.14.17: redukuje askorbat1.14.18-19: drugi
1.14.99 - razno
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Teme
Tipovi
  • B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6