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Flavin containing monooxygenase 4

FMO2, FMO4
Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in man resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: FMO3, FMO5, ACID, CAN, POLYMERASE
Papers on FMO2
Identification of Patients with Recurrent Glioblastoma Who May Benefit from Combined Bevacizumab and CCNU Therapy: A Report from the BELOB Trial.
New
French et al., Rotterdam, Netherlands. In Cancer Res, Feb 2016
In particular, expression of FMO4 and OSBPL3 was associated with treatment response.
Ab initio studies on the structure of and atomic interactions in cellulose IIII crystals.
New
Ueda et al., Yokohama, Japan. In Carbohydr Res, Dec 2015
Moreover, FMO4 calculation was also applied to the optimized crystal structure to estimate the strength of the interactions.
Assessment and acceleration of binding energy calculations for protein-ligand complexes by the fragment molecular orbital method.
New
Taiji et al., Kōbe, Japan. In J Comput Chem, Dec 2015
By testing the effects of specific FMO calculation conditions (including fragmentation size, basis sets, electron correlation, exchange-correlation functionals, and solvation effects) on the binding energies of the FK506-binding protein and 10 ligand complex molecule, we have found that the standard FMO calculation condition, FMO2-MP2/6-31G(d), is suitable for evaluating the protein-ligand interactions.
Human FMO2-based microbial whole-cell catalysts for drug metabolite synthesis.
Winkler et al., Graz, Austria. In Microb Cell Fact, 2014
The present work aimed for the generation of an efficient whole-cell catalyst based on the flavin monooxygenase isoform 2 (FMO2), which is part of the human phase I metabolism.
Efficient and accurate fragmentation methods.
Impact
Gordon et al., Ames, United States. In Acc Chem Res, 2014
The EFMO method is both more accurate and more computationally efficient than the most commonly used FMO implementation (FMO2), in which all dimers are explicitly included in the calculation.
Immunosuppressive potential of bardoxolone methyl using a modified murine local lymph node assay (LLNA).
Miyamoto et al., In J Toxicol Sci, 2014
In the modified LLNA, CDDO-Me showed a significant decrease in lymph node weight and changes in expressions of the immunosuppression-related genes, Zfp459 and Fmo2.
The phenotype of a flavin-containing monooyxgenase knockout mouse implicates the drug-metabolizing enzyme FMO1 as a novel regulator of energy balance.
Shephard et al., London, United Kingdom. In Biochem Pharmacol, 2014
In contrast to FMO2 and FMO4, FMO1 is highly expressed in metabolic tissues, including liver, kidney, WAT and BAT.
Mammalian flavin-containing monooxygenase (FMO) as a source of hydrogen peroxide.
Williams et al., United States. In Biochem Pharmacol, 2014
Two common FMO2 (the major isoform in the lung) genetic polymorphisms, S195L and N413K, were examined for generation of H₂O₂.
Development and molecular characterization of genic molecular markers for grain protein and calcium content in finger millet (Eleusine coracana (L.) Gaertn.).
Kumar et al., India. In Mol Biol Rep, 2014
The present study resulted in identification of highly polymorphic primers (FMO2E30, FMO2E33, FMO2-18 and FMO2-14) based on the parameters such as percentage of polymorphism, PIC values, gene diversity and number of alleles.
Fragment Molecular Orbital Molecular Dynamics with the Fully Analytic Energy Gradient.
Gordon et al., Ames, United States. In J Chem Theory Comput, 2013
An FMO-MD simulation that includes the fully analytic energy gradient and two body corrections (FMO2) gives improved energy conservation compared with a previously calculated FMO-MD simulation with an approximate energy gradient and including up to three body corrections (FMO3).
Characterization of sulfoxygenation and structural implications of human flavin-containing monooxygenase isoform 2 (FMO2.1) variants S195L and N413K.
GeneRIF
Williams et al., Corvallis, United States. In Drug Metab Dispos, 2009
Characterization of sulfoxygenation and structural implications of human flavin-containing monooxygenase isoform 2 (FMO2.1) variants S195L and N413K.
Differential localization of flavin-containing monooxygenase (FMO) isoforms 1, 3, and 4 in rat liver and kidney and evidence for expression of FMO4 in mouse, rat, and human liver and kidney microsomes.
GeneRIF
Elfarra et al., Madison, United States. In J Pharmacol Exp Ther, 2009
Data show a compelling visual demonstration of the isoform-specific localization patterns of FMO1, -3, and -4 in the rat liver and kidney and the first evidence for expression of FMO4 at the protein level in mouse and human liver and kidney microsomes.
The potentially deleterious functional variant flavin-containing monooxygenase 2*1 is at high frequency throughout sub-Saharan Africa.
GeneRIF
Phillips et al., London, United Kingdom. In Pharmacogenet Genomics, 2008
analysis of how the functional variant flavin-containing monooxygenase 2*1 is at high frequency throughout sub-Saharan Africa
Flavin-containing monooxygenases: mutations, disease and drug response.
Review
Shephard et al., London, United Kingdom. In Trends Pharmacol Sci, 2008
Most humans are homozygous for a nonsense mutation that inactivates FMO2.
Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism.
Review
Williams et al., Oregon, United States. In Pharmacol Ther, 2005
Three of the 5 expressed human FMO genes, FMO1, FMO2 and FMO3, exhibit genetic polymorphisms.
Haplotype and functional analysis of four flavin-containing monooxygenase isoform 2 (FMO2) polymorphisms in Hispanics.
GeneRIF
Williams et al., Corvallis, United States. In Pharmacogenet Genomics, 2005
analysis of flavin-containing monooxygenase isoform 2 (FMO2) polymorphisms in Hispanics
Identification and characterization of the FMO2 gene in Rattus norvegicus: a good model to study metabolic and toxicological consequences of the FMO2 polymorphism.
GeneRIF
Lattard et al., Lyon, France. In Pharmacogenetics, 2004
FMO2 genetic polymorphism was associated with major differences in the S-oxidative metabolism.
Genetic polymorphisms of flavin-containing monooxygenase (FMO).
Review
Phillips et al., Corvallis, United States. In Drug Metab Rev, 2002
A more recent ethnically related polymorphism in expression of the major FMO in lung, FMO2, has been described.
Potential role of the flavin-containing monooxygenases in the metabolism of endogenous compounds.
Review
Elfarra, Madison, United States. In Chem Biol Interact, 1995
Methionine, an endogenous homocysteine S-conjugate, was shown to be a substrate for cDNA-expressed rabbit FMO1, FMO2, and FMO3, however, the methionine sulfoxidation reaction was preferentially catalyzed by FMO3.
Trimethylaminuria in a girl with Prader-Willi syndrome and del(15)(q11q13).
Review
Aiello et al., Mobile, United States. In Am J Med Genet, 1993
However, recent development of mapping of flavin-containing monooxygenase 2 (FMO2), the likely enzyme that is defective in fish odor syndrome, to chromosome 1q probably excludes pathogenetic association of fish odor syndrome with the Prader-Willi syndrome.
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