Interaction Of Goxa With Its Modifying Enzyme And Its Subunit Assembly Are Dependent On The Extent Of Cysteine Tryptophylquinone Biosynthesis

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.

Publication Date

5-10-2016

Publication Title

Biochemistry

Volume

55

Issue

16

Number of Pages

2305-2308

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1021/acs.biochem.6b00274

Socpus ID

84969135988 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/84969135988

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