FMO2

FMO2
Identifikatori
AlijasiFMO2
Spoljašnji IDOMIM: 603955 MGI: 1916776 HomoloGene: 86882 GeneCards: FMO2
Genska lokacija (miš)
Chromosome 1 (mouse)
Hr.Chromosome 1 (mouse)[1]
Chromosome 1 (mouse)
Genomska lokacija za FMO2
Genomska lokacija za FMO2
Band1|1 H2.1Start162,701,886 bp[1]
Kraj162,726,295 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
endoplasmic reticulum membrane
мембрана
ендоплазматични ретикулум
intracellular membrane-bounded organelle
Biological process xenobiotic metabolic process
toxin metabolic process
NADPH oxidation
NADP metabolic process
oxygen metabolic process
organic acid metabolic process
Sources:Amigo / QuickGO
Ortolozi
VrsteČovekMiš
Entrez

2327

55990

Ensembl

ENSG00000094963

ENSMUSG00000040170

UniProt

Q99518

Q8K2I3

RefSeq (mRNA)

NM_001301347
NM_001460
NM_001365900

NM_018881
NM_001360913
NM_001360914

RefSeq (protein)

NP_001288276
NP_001451
NP_001352829

NP_061369
NP_001347842
NP_001347843

Location (UCSC)n/aChr 1: 162.7 – 162.73 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Dimetilanilin monooksigenaza (N-oksid-formirajuća) 2 je enzim koji je kod ljudi kodiran FMO2 genom.[4][5][6]

Monooksigenaze koje sarže flavin su NADPH zavisni enzimi koji katalizuju oksidaciju mnogih lekova i ksenobiotika. Kod većine sisara, monooksigenaze koje sadrže flavin katalizuju N-oksidaciju primarnih alkilamina putem N-hidroksilaminskih intermedijera. Međutim, kod ljudi ovaj enzim je okrnjen i verovatno se brzo ralaže. Protein kodiran ovim genom predstavlja skraćenu formu is stoga nema kataličko dejstvo. Objavljeno je da je kod afričkih amerikanaca funkcionalni alil prisutan, ali evidencija u vidu sekvence nije dostupna u prilog toj tvrdnji. Ovaj gen je lociran u klasteru sa FMO1, FMO3, i FMO4 genima na hromozomu 1.[6]

Vidi još

  • Dimetilanilin monooksigenaza (formiranje N-oksida)

Reference

  1. ^ а б в GRCm38: Ensembl release 89: ENSMUSG00000040170 - 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. ^ Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR (1992). „Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family”. Biochem J. 287. ( Pt 1): 261—7. PMC 1133153 Слободан приступ. PMID 1417778. 
  5. ^ Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, Phillips IR (1998). „The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a truncated, nonfunctional protein”. J Biol Chem. 273 (46): 30599—607. PMID 9804831. doi:10.1074/jbc.273.46.30599. 
  6. ^ а б „Entrez Gene: FMO2 flavin containing monooxygenase 2 (non-functional)”. 

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. 
  • Lomri N, Gu Q, Cashman JR (1992). „Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.”. Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1685—9. PMC 48517 Слободан приступ. PMID 1542660. doi:10.1073/pnas.89.5.1685. 
  • 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. 
  • 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. 
  • McCombie RR, Dolphin CT, Povey S, et al. (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. 
  • Bonaldo MF, Lennon G, Soares MB (1997). „Normalization and subtraction: two approaches to facilitate gene discovery.”. Genome Res. 6 (9): 791—806. PMID 8889548. doi:10.1101/gr.6.9.791. 
  • Whetstine JR, Yueh MF, McCarver DG, et al. (2000). „Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans.”. Toxicol. Appl. Pharmacol. 168 (3): 216—24. PMID 11042094. doi:10.1006/taap.2000.9050. 
  • Krueger SK, Martin SR, Yueh MF, et al. (2002). „Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein.”. Drug Metab. Dispos. 30 (1): 34—41. PMID 11744609. doi:10.1124/dmd.30.1.34. 
  • 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. 
  • 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. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). „The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”. Genome Res. 14 (10B): 2121—7. PMC 528928 Слободан приступ. PMID 15489334. doi:10.1101/gr.2596504. 
  • Krueger SK, Siddens LK, Henderson MC, et al. (2005). „Haplotype and functional analysis of four flavin-containing monooxygenase isoform 2 (FMO2) polymorphisms in Hispanics.”. Pharmacogenet. Genomics. 15 (4): 245—56. PMC 1351039 Слободан приступ. PMID 15864117. doi:10.1097/01213011-200504000-00008. 
  • 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