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Article

Influence of FAD structure on its binding and activity with the C406A mutant of recombinant human liver monoamine oxidase A.

The Journal of biological chemistry - 7 Jul 2000

Nandigama R K, Edmondson D E

Abstract excerpt

The FAD binding site of human liver monoamine oxidase A (MAO A) has been investigated by mutagenesis of the amino acid site of covalent FAD attachment (Cys-406) to an alanyl residue. Expression of the C406A mutant in Saccharomyces cerevisiae results in the formation of an active enzyme, as found previously with the rat liver enzyme. The activity of this mutant enzyme is labile to solubilization, thus requiring...

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PMID: 10877844
DOI: 10.1074/jbc.M002132200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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