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Article

Identification of the oxygen activation site in monomeric sarcosine oxidase: role of Lys265 in catalysis.

Biochemistry - 2 Sept 2008

Zhao Guohua, Bruckner Robert C, Jorns Marilyn Schuman

Abstract excerpt

Monomeric sarcosine oxidase (MSOX) catalyzes the oxidation of N-methylglycine and contains covalently bound FAD that is hydrogen bonded at position N(5) to Lys265 via a bridging water. Lys265 is absent in the homologous but oxygen-unreactive FAD site in heterotetrameric sarcosine oxidase. Isolated preparations of Lys265 mutants contain little or no flavin but can be covalently reconstituted with FAD. Mutation of...

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Identifiers

PMID: 18693755
DOI: 10.1021/bi8008642
PMCID: PMC2764408

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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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