FMO1

FMO1
Identifikatori
AlijasiFMO1
Spoljašnji IDOMIM: 136130 MGI: 1310002 HomoloGene: 55520 GeneCards: FMO1
Genska lokacija (miš)
Chromosome 1 (mouse)
Hr.Chromosome 1 (mouse)[1]
Chromosome 1 (mouse)
Genomska lokacija za FMO1
Genomska lokacija za FMO1
Band1 H2.1|1 70.34 cMStart162,657,130 bp[1]
Kraj162,694,179 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
• GO:0001948, GO:0016582 везивање за протеине плазме
Cellular component• organelle membrane
• саставни део мембране
• endoplasmic reticulum lumen
• endoplasmic reticulum membrane
• ендоплазматични ретикулум
• мембрана
• intracellular membrane-bounded organelle
Biological process• response to osmotic stress
• xenobiotic metabolic process
• toxin metabolic process
• реакција на липополисахарид
• NADPH oxidation
• organic acid metabolic process
Sources:Amigo / QuickGO
Ortolozi
VrsteČovekMiš
Entrez

2326

14261

Ensembl

ENSG00000010932

ENSMUSG00000040181

UniProt

Q01740

P50285

RefSeq (mRNA)

NM_001282692
NM_001282693
NM_001282694
NM_002021

NM_010231
NM_001330291
NM_001330318

RefSeq (protein)

NP_001269621
NP_001269622
NP_001269623
NP_002012

NP_001317220
NP_001317247
NP_034361

Location (UCSC)n/aChr 1: 162.66 – 162.69 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Dimetilanilin monooksigenaza (N-oksid-formirajuća) 1 je enzim koji je kod ljudi kodiran FMO1 genom.[4]

Monooksigenaze koje sarže flavin su NADPH zavisni enzimi koji katalizuju oksidaciju mnogih lekova i ksenobiotika. Ovaj gen sadrži 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.[4][4]

Vidi još

  • Dimetilanilin monooksigenaza (formiranje N-oksida)

Reference

  1. ^ а б в GRCm38: Ensembl release 89: ENSMUSG00000040181 - 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. ^ а б в „Entrez Gene: FMO1 flavin containing monooxygenase 1”. 

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. 
  • Cashman JR (2004). „The implications of polymorphisms in mammalian flavin-containing monooxygenases in drug discovery and development”. Drug Discov. Today. 9 (13): 574—581. PMID 15203093. doi:10.1016/S1359-6446(04)03136-8. 
  • Dolphin C, Shephard EA, Povey S, et al. (1991). „Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1)”. J. Biol. Chem. 266 (19): 12379—85. PMID 1712018. 
  • 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—257. PMID 8311461. doi:10.1006/abbi.1994.1035. 
  • Shephard EA, Dolphin CT, Fox MF, et al. (1993). „Localization of genes encoding three distinct flavin-containing monooxygenases to human chromosome 1q”. Genomics. 16 (1): 85—89. PMID 8486388. doi:10.1006/geno.1993.1144. 
  • Hay JC, Chao DS, Kuo CS, Scheller RH (1997). „Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells”. Cell. 89 (1): 149—158. PMID 9094723. doi:10.1016/S0092-8674(00)80191-9. 
  • Yeung CK, Lang DH, Thummel KE, Rettie AE (2000). „Immunoquantitation of FMO1 in human liver, kidney, and intestine”. Drug Metab. Dispos. 28 (9): 1107—11. PMID 10950857. 
  • Washio T, Arisawa H, Kohsaka K, Yasuda H (2002). „Identification of human drug-metabolizing enzymes involved in the metabolism of SNI-2011”. Biol. Pharm. Bull. 24 (11): 1263—1266. PMID 11725960. doi:10.1248/bpb.24.1263. 
  • Koukouritaki SB, Simpson P, Yeung CK, et al. (2002). „Human hepatic flavin-containing monooxygenases 1 (FMO1) and 3 (FMO3) developmental expression”. Pediatr. Res. 51 (2): 236—243. PMID 11809920. doi:10.1203/00006450-200202000-00018. 
  • 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—16903. 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—193. PMID 12527699. doi:10.1124/dmd.31.2.187. 
  • Attar M, Dong D, Ling KH, Tang-Liu DD (2003). „Cytochrome P450 2C8 and flavin-containing monooxygenases are involved in the metabolism of tazarotenic acid in humans”. Drug Metab. Dispos. 31 (4): 476—481. PMID 12642475. doi:10.1124/dmd.31.4.476. 
  • Hines RN, Luo Z, Hopp KA, et al. (2003). „Genetic variability at the human FMO1 locus: significance of a basal promoter yin yang 1 element polymorphism (FMO1*6)”. J. Pharmacol. Exp. Ther. 306 (3): 1210—1218. PMID 12829732. doi:10.1124/jpet.103.053686. 
  • 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—45. 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—2127. PMC 528928 Слободан приступ. PMID 15489334. doi:10.1101/gr.2596504. 
  • 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. 
  • Bartsch M, Gobbato E, Bednarek P, et al. (2006). „Salicylic acid-independent ENHANCED DISEASE SUSCEPTIBILITY1 signaling in Arabidopsis immunity and cell death is regulated by the monooxygenase FMO1 and the Nudix hydrolase NUDT7”. Plant Cell. 18 (4): 1038—1051. PMC 1425861 Слободан приступ. PMID 16531493. doi:10.1105/tpc.105.039982. 
  • п
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  • у
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