1998 journal article

Identification of amino acid residues associated with modulation of flavin-containing monooxygenase (FMO) activity by imipramine: Structure/function studies with FMO1 from pig and rabbit

BIOCHEMISTRY, 37(17), 5930–5938.

By: M. Wyatt n, L. Overby n, M. Lawton n & R. Philpot n

MeSH headings : Amino Acid Substitution / genetics; Amino Acids / chemistry; Amino Acids / genetics; Amino Acids / metabolism; Animals; Catalysis; Enzyme Activation / drug effects; Enzyme Activation / genetics; Genetic Vectors / biosynthesis; Imipramine / metabolism; Imipramine / pharmacology; Methimazole / metabolism; Mutagenesis, Site-Directed; Oxygenases / biosynthesis; Oxygenases / chemistry; Oxygenases / genetics; Oxygenases / metabolism; Rabbits; Recombinant Fusion Proteins / biosynthesis; Recombinant Fusion Proteins / chemistry; Structure-Activity Relationship; Swine
TL;DR: The results suggest that the response of FMO1 to imipramine involves a distribution between two sites that is regulated by structural features that do not alter the overall binding, and inhibition observed, although it appears to be competitive, likely does not involve competition for a binding site. (via Semantic Scholar)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1998 journal article

Molecular cloning, sequence, and expression of mouse flavin-containing monooxygenases 1 and 5 (FMO1 and FMO5)

Journal of Biochemical and Molecular Toxicology, 12(1998), 205–212.

By: N. Cherrington n, J. Falls n, R. Rose n, K. Clements n, R. Philpot*, P. Levi n, E. Hodgson n

Source: NC State University Libraries
Added: August 6, 2018

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