ArticleScientific reports2017
Inactivation mechanism of N61S mutant of human FMO3 towards trimethylamine.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 30 citations in OpenAlex.
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- Flavin-Containing Monooxygenase 3 (FMO3) Is Critical for Dioxin-Induced Reorganization of the Gut Microbiome and Host Insulin Sensitivity.Metabolites · 2022Article
- Molecular Lego of Human Cytochrome P450: The Key Role of Heme Domain Flexibility for the Activity of the Chimeric Proteins.International journal of molecular sciences · 2022Article
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- Targeting Trimethylamine N-Oxide: A New Therapeutic Strategy for Alleviating Atherosclerosis.Frontiers in cardiovascular medicine · 2022Review
- Carnitine Traffic in Cells. Link With Cancer.Frontiers in cell and developmental biology · 2020Review
- Drug metabolite synthesis by immobilized human FMO3 and whole cell catalysts.Microbial cell factories · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human flavin-containing monooxygenase 3 (hFMO3) catalyses the oxygenation of a wide variety of compounds including drugs as well as dietary compounds. It is the major hepatic enzyme involved in the production of the N-oxide of trimethylamine (TMAO) and clinical studies have uncovered a striking correlation between plasma TMAO concentration and cardiovascular disease. Certain mutations within the hFMO3 gene cause defective trimethylamine (TMA) N-oxygenation leading to trimethylaminuria (TMAU) also known as fish-odour syndrome. In this paper, the inactivation mechanism of a TMAU-causing polymorphic variant, N61S, is investigated. Transient kinetic experiments show that this variant has a > 170-fold lower NADPH binding affinity than the wild type. Thermodynamic and spectroscopic experiments reveal that the poor NADP
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