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A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre‐methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis
Author(s) -
Abu Tarboush Nafez,
Jensen Lyndal M.R.,
Wilmot Carrie M.,
Davidson Victor L.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.04.047
Subject(s) - chemistry , methylamine , biosynthesis , tryptophan , cofactor , biochemistry , electron transfer , stereochemistry , enzyme , amino acid , photochemistry
MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor (preMADH) to complete the biosynthesis of its protein‐derived tryptophan tryptophylquinone (TTQ) cofactor. Trp199 is present at the site of interaction between MauG and preMADH and is critical to this process as it mediates hole hopping during the inter‐protein electron transfer that is required for catalysis. Trp199 was converted to Glu and the structure and reactivity of the W199E/preMADH complex were characterized. The results reveal that the nature of residue 199 is also important for productive complex formation between preMADH and MauG.