The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis

The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. The crystal structure of the MauG-preMADH compl...

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Bibliographic Details
Main Authors: Shin, Sooim, Feng, Manliang, Chen, Yan, Jensen, Lyndal M. R., Tachikawa, Hiroyasu, Wilmot, Carrie M., Liu, Aimin, Davidson, Victor L.
Format: Artigo
Language:Inglês
Published: 2010
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Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC3061978/
https://ncbi.nlm.nih.gov/pubmed/21128656
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi101819m
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