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Article

Investigation of structure and function of a catalytically efficient variant of the human flavin-containing monooxygenase form 3.

Drug metabolism and disposition: the biological fate of chemicals - 1 Dec 2006

Borbás Tímea, Zhang Jun, Cerny Matt A, Likó István, Cashman John R

Abstract excerpt

To characterize the contribution of amino acid 360 to the functional activity of the human flavin-containing monooxygenase form 3 (FMO3) and form 1 (FMO1) in the oxygenation of drugs and chemicals, we expressed four FMO3 variants (i.e., Ala360-FMO3, His360-FMO3, Gln360-FMO3, and Pro360-FMO3) and...

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Share to Amino Acid Substitution
Share to FMO3 gene
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16985102
DOI: 10.1124/dmd.106.010827

Genes

FMO3
FMO1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16985102-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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