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Article

Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.

The Journal of biological chemistry - 29 Apr 2005

Jones Limei H, Pearson Arwen R, Tang Yu, Wilmot Carrie M, Davidson Victor L

Abstract excerpt

The biosynthesis of methylamine dehydrogenase (MADH) requires formation of six intrasubunit disulfide bonds, incorporation of two oxygens into residue betaTrp57 and covalent cross-linking of betaTrp57 to betaTrp108 to form the protein-derived cofactor tryptophan tryptophylquinone (TTQ). Residues betaAsp76 and betaAsp32 are located in close proximity to the quinone oxygens of TTQ in the enzyme active site. These...

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PMID: 15734739
DOI: 10.1074/jbc.M500943200

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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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