Mutation of Trp(93) of MauG to tyrosine causes loss of bound Ca(2+) and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis.

Abstract excerpt

The dihaem enzyme MauG catalyses a six-electron oxidation required for post-translational modification of preMADH (precursor of methylamine dehydrogenase) to complete the biosynthesis of its TTQ (tryptophan tryptophylquinone) cofactor. Trp93 of MauG is positioned midway between its two haems, and in close proximity to a Ca2+ that is critical for MauG function. Mutation of Trp93 to tyrosine caused loss of bound...

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