| Literature DB >> 27064961 |
Esha Sehanobish1, Jonatan C Campillo-Brocal2, Heather R Williamson1, Antonio Sanchez-Amat2, Victor L Davidson1.
Abstract
GoxA is a glycine oxidase bearing a protein-derived cysteine tryptophylquinone (CTQ) cofactor that is formed by posttranslational modifications catalyzed by a flavoprotein, GoxB. Two forms of GoxA were isolated: an active form with mature CTQ and an inactive precursor protein that lacked CTQ. The active GoxA was present as a homodimer with no detectable affinity for GoxB, whereas the precursor was isolated as a monomer in a tight complex with one GoxB. Thus, the interaction of GoxA with GoxB and subunit assembly of mature GoxA are each dependent on the extent of CTQ biosynthesis.Entities:
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Year: 2016 PMID: 27064961 PMCID: PMC5076370 DOI: 10.1021/acs.biochem.6b00274
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162