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Biocatalytic Characterization of Human FMO5: Unearthing Baeyer–Villiger Reactions in Humans

https://doi.org/10.1021/acschembio.5b01016

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Type II Flavin‐Containing Monooxygenases: A New Class of Biocatalysts that Harbors Baeyer–Villiger Monooxygenases with a Relaxed Coenzyme Specificity

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Direct Room‐Temperature Lactonisation of Alcohols and Ethers onto Amides: An “Amide Strategy” for Synthesis

inferredcites →https://doi.org/10.1002/jbt.20176openalex-snapshot

Functional activity of the mouse flavin‐containing monooxygenase forms 1, 3, and 5

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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

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The Mammalian Flavin-Containing Monooxygenases: Molecular Characterization and Regulation of Expression

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Exploring the Substrate Specificity and Enantioselectivity of a Baeyer–Villiger Monooxygenase from Dietzia sp. D5: Oxidation of Sulfides and Aldehydes

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Some distinctions between flavin-containing and cytochrome P450 monooxygenases

inferredcites →https://doi.org/10.1016/j.bcp.2014.02.006openalex-snapshot

Mammalian flavin-containing monooxygenase (FMO) as a source of hydrogen peroxide

inferredcites →https://doi.org/10.1016/j.bcp.2015.05.013openalex-snapshot

The phenotype of a knockout mouse identifies flavin-containing monooxygenase 5 (FMO5) as a regulator of metabolic ageing

inferredcites →https://doi.org/10.1016/j.celrep.2014.12.036openalex-snapshot

The TMAO-Generating Enzyme Flavin Monooxygenase 3 Is a Central Regulator of Cholesterol Balance

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Application of the Amplex red/horseradish peroxidase assay to measure hydrogen peroxide generation by recombinant microsomal enzymes

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Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

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Biocatalyst assessment of recombinant whole-cells expressing the Baeyer-Villiger monooxygenase from Xanthobacter sp. ZL5

inferredcites →https://doi.org/10.1016/j.molcatb.2011.07.003openalex-snapshot

Extensive substrate profiling of cyclopentadecanone monooxygenase as Baeyer–Villiger biocatalyst reveals novel regiodivergent oxidations

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Expanding the biocatalytic toolbox of flavoprotein monooxygenases from Rhodococcus jostii RHA1

inferredcites →https://doi.org/10.1016/j.pharmthera.2005.01.001openalex-snapshot

Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism

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The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion

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Flavin-containing monooxygenases: mutations, disease and drug response

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Isoform specificity of trimethylamine N-oxygenation by human flavin-containing monooxygenase (FMO) and P450 enzymes

inferredcites →https://doi.org/10.1016/s0014-5793(02)02623-6openalex-snapshot

Identification of a Baeyer–Villiger monooxygenase sequence motif

inferredcites →https://doi.org/10.1016/s0021-9258(17)33523-8openalex-snapshot

Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase.

inferredcites →https://doi.org/10.1016/s0021-9258(19)69479-2openalex-snapshot

The reductive half-reaction of liver microsomal FAD-containing monooxygenase.

inferredcites →https://doi.org/10.1016/s0021-9258(19)69480-9openalex-snapshot

The oxidative half-reaction of liver microsomal FAD-containing monooxygenase.

inferredcites →https://doi.org/10.1016/s0021-9258(19)85592-8openalex-snapshot

Transient kinetic study of liver microsomal FAD-containing monooxygenase.

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The enantiomeric ratio: origin, determination and prediction

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Kinetic Mechanism of Phenylacetone Monooxygenase from Thermobifida fusca

inferredcites →https://doi.org/10.1021/cr1003437openalex-snapshot

Baeyer−Villiger Monooxygenases: More Than Just Green Chemistry

inferredcites →https://doi.org/10.1021/ja00293a054openalex-snapshot

Functional group diversity in enzymic oxygenation reactions catalyzed by bacterial flavin-containing cyclohexanone oxygenase

inferredcites →https://doi.org/10.1021/ja972942iopenalex-snapshot

Recombinant Baker's Yeast as a Whole-Cell Catalyst for Asymmetric Baeyer−Villiger Oxidations

inferredcites →https://doi.org/10.1021/jm5007098openalex-snapshot

Flavin Monooxygenase Metabolism: Why Medicinal Chemists Should Matter

inferredcites →https://doi.org/10.1021/jo026605qopenalex-snapshot

Access to Optically Pure 4- and 5-Substituted Lactones: A Case of Chemical−Biocatalytical Cooperation

inferredcites →https://doi.org/10.1021/jo980737vopenalex-snapshot

Enantio- and Regioselective Baeyer−Villiger Oxidations of 2- and 3-Substituted Cyclopentanones Using Engineered Bakers' Yeast

inferredcites →https://doi.org/10.1021/tx00016a016openalex-snapshot

Substrate specificities of rabbit lung and porcine liver flavin-containing monooxygenases: differences due to substrate size

inferredcites →https://doi.org/10.1038/ncomms7498openalex-snapshot

Flavin-containing monooxygenase 3 as a potential player in diabetes-associated atherosclerosis

inferredcites →https://doi.org/10.1038/nmeth.1318openalex-snapshot

Enzymatic assembly of DNA molecules up to several hundred kilobases

inferredcites →https://doi.org/10.1038/nrd4581openalex-snapshot

Predicting drug metabolism: experiment and/or computation?

inferredcites →https://doi.org/10.1039/c2cc17878hopenalex-snapshot

Expression of recombinant human flavin monooxygenase and moclobemide-N-oxide synthesis on multi-mg scale

inferredcites →https://doi.org/10.1039/c4cc02541eopenalex-snapshot

Broadening the scope of Baeyer–Villiger monooxygenase activities toward α,β-unsaturated ketones: a promising route to chiral enol-lactones and ene-lactones

inferredcites →https://doi.org/10.1039/c4cc06489eopenalex-snapshot

Synthesis of methyl propanoate by Baeyer–Villiger monooxygenases

inferredcites →https://doi.org/10.1073/pnas.0800859105openalex-snapshot

Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase

inferredcites →https://doi.org/10.1074/jbc.m110.161372openalex-snapshot

Joint Functions of Protein Residues and NADP(H) in Oxygen Activation by Flavin-containing Monooxygenase

inferredcites →https://doi.org/10.1080/00498250310001624627openalex-snapshot

S-oxidation ofS-methyl-esonarimod by flavin-containing monooxygenases in human liver microsomes

inferredcites →https://doi.org/10.1097/00008571-200402000-00006openalex-snapshot

Organization and evolution of the flavin-containing monooxygenase genes of human and mouse

inferredcites →https://doi.org/10.1111/j.1742-4658.2009.07006.xopenalex-snapshot

Thermo FAD, a Thermofluor ® ‐adapted flavin ad hoc detection system for protein folding and ligand binding

inferredcites →https://doi.org/10.1124/dmd.105.006171openalex-snapshot

QUANTITATIVE ANALYSIS OF FMO GENE mRNA LEVELS IN HUMAN TISSUES

inferredcites →https://doi.org/10.1124/dmd.110.035360openalex-snapshot

A Baeyer-Villiger Oxidation Specifically Catalyzed by Human Flavin-Containing Monooxygenase 5

inferredcites →https://doi.org/10.1124/dmd.114.061747openalex-snapshot

Metabolism of MRX-I, a Novel Antibacterial Oxazolidinone, in Humans: The Oxidative Ring Opening of 2,3-Dihydropyridin-4-One Catalyzed by Non-P450 Enzymes

inferredcites →https://doi.org/10.1126/science.aac9257openalex-snapshot

Cell nonautonomous activation of flavin-containing monooxygenase promotes longevity and health span

inferredcites →https://doi.org/10.1128/aem.69.1.419-426.2003openalex-snapshot

Substrate Specificity and Enantioselectivity of 4-Hydroxyacetophenone Monooxygenase

inferredcites →https://doi.org/10.1146/annurev.pharmtox.46.120604.141043openalex-snapshot

HUMAN FLAVIN-CONTAINING MONOOXYGENASES

inferredcites →https://doi.org/10.1186/s12934-015-0262-0openalex-snapshot

Human FMO2-based microbial whole-cell catalysts for drug metabolite synthesis

inferredcites →https://doi.org/10.1385/1-59259-266-x:1openalex-snapshot

UV-Visible Spectroscopy as a Tool to Study Flavoproteins

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Baeyer-Villiger Monooxygenases Using the FMO5 for the Detoxification of Testosterone and Dehydroepiandrosterone in LNCaP Cells

inferred← citeshttps://doi.org/10.1002/9783527830138.ch7openalex-snapshot

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Characterization of a thermostable flavin-containing monooxygenase from Nitrincola lacisaponensis (NiFMO)

inferred← citeshttps://doi.org/10.1007/s00253-020-10705-wopenalex-snapshot

Flavin-dependent N-hydroxylating enzymes: distribution and application

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Sn-based catalysts for Baeyer-Villiger oxidations by using hydrogen peroxide as oxidant

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Oxidative Modification Enzymes in Polyketide Biosynthetic Pathways

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inferred← citeshttps://doi.org/10.1016/j.bbadva.2023.100108openalex-snapshot

Investigating the biochemical signatures and physiological roles of the FMO family using molecular phylogeny

inferred← citeshttps://doi.org/10.1016/j.biotechadv.2017.11.007openalex-snapshot

Hot spots for the protein engineering of Baeyer-Villiger monooxygenases

inferred← citeshttps://doi.org/10.1016/j.cmet.2025.11.014openalex-snapshot

Endometrial stromal cell-derived TMAO sustains decidualization to prevent recurrent spontaneous abortion

inferred← citeshttps://doi.org/10.1016/j.eti.2023.103083openalex-snapshot

Investigation of process stability of a whole-cell biocatalyst with Baeyer–Villiger monooxygenase activity in continuous bioreactors

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Regulated methionine oxidation by monooxygenases

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2019.09.038openalex-snapshot

Uncoupled human flavin-containing monooxygenase 3 releases superoxide radical in addition to hydrogen peroxide

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Selenium-incorporated polymeric carbon nitride for visible-light photocatalytic regio-specific epoxidation of β-ionone

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Predicting Regioselectivity of AO, CYP, FMO, and UGT Metabolism Using Quantum Mechanical Simulations and Machine Learning

inferred← citeshttps://doi.org/10.1021/acs.jmedchem.9b01877openalex-snapshot

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Side-Chain Pruning Has Limited Impact on Substrate Preference in a Promiscuous Enzyme

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Baeyer–Villiger Monooxygenase FMO5 as Entry Point in Drug Metabolism

inferred← citeshttps://doi.org/10.1038/s41467-023-36181-0openalex-snapshot

FMO rewires metabolism to promote longevity through tryptophan and one carbon metabolism in C. elegans

inferred← citeshttps://doi.org/10.1038/s41467-023-36756-xopenalex-snapshot

Evolution of enzyme functionality in the flavin-containing monooxygenases

inferred← citeshttps://doi.org/10.1038/s41594-019-0347-2openalex-snapshot

Ancestral-sequence reconstruction unveils the structural basis of function in mammalian FMOs

inferred← citeshttps://doi.org/10.1038/s41594-019-0356-1openalex-snapshot

Flavin-containing monooxygenases: new structures from old proteins

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Fabrication of Se/C using carbohydrates as biomass starting materials: an efficient catalyst for regiospecific epoxidation of β-ionone with ultrahigh turnover numbers

inferred← citeshttps://doi.org/10.1039/c8np00054aopenalex-snapshot

Native roles of Baeyer–Villiger monooxygenases in the microbial metabolism of natural compounds

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Hydrothermal synthesis of γ-MnOOH nanowires using sapless leaves as the reductant: an effective catalyst for the regio-specific epoxidation of β-ionone

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Flavin-containing monooxygenases in aging and disease: Emerging roles for ancient enzymes

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Ancestral reconstruction of mammalian FMO1 enables structural determination, revealing unique features that explain its catalytic properties

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A metabolic pathway for the prodrug nabumetone to the pharmacologically active metabolite, 6-methoxy-2-naphthylacetic acid (6-MNA) by non-cytochrome P450 enzymes

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Biotransformation and bioactivation reactions – 2015 literature highlights

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Metabolomic and transcriptomic analyses of Fmo5 -/- mice reveal roles for flavin-containing monooxygenase 5 (FMO5) in NRF2-mediated oxidative stress, the unfolded protein response, lipid homeostasis, and carbohydrate and one-carbon metabolism

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Mice, rats, and guinea pigs differ in FMOs expression and tissue concentration of TMAO, a gut bacteria-derived biomarker of cardiovascular and metabolic diseases

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5. FLAVIN-CONTAINING MONOOXYGENASES (FMO) ARE PHASE I ENZYMES OF XENOBIOTIC BIOTRANSFORMATION. NOMENCLATURE, STRUCTURE, MOLECULAR DIVERSITY, FUNCTION, PARTICIPATION IN THE FUNCTIONING OF THE BIOTRANSFORMATION SYSTEM. A COMPARISON WITH CYTOCHROMES Р450 (A

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Enzymatically Produced Trimethylamine N-Oxide: Conserving It or Eliminating It

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NHR-49/PPAR-α and HLH-30/TFEB cooperate for C. elegans host defense via a flavin-containing monooxygenase

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