Title

A Trp199Glu Maug Variant Reveals A Role For Trp199 Interactions With Pre-Methylamine Dehydrogenase During Tryptophan Tryptophylquinone Biosynthesis

Keywords

Cofactor biosynthesis; Electron transfer; Kinetic mechanism; Protein-protein interaction

Abstract

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. © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Publication Date

6-19-2013

Publication Title

FEBS Letters

Volume

587

Issue

12

Number of Pages

1736-1741

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1016/j.febslet.2013.04.047

Socpus ID

84878783265 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/84878783265

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