Title
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
Copyright Status
Unknown
Socpus ID
84969135988 (Scopus)
Source API URL
https://api.elsevier.com/content/abstract/scopus_id/84969135988
STARS Citation
Sehanobish, Esha; Campillo-Brocal, Jonatan C.; Williamson, Heather R.; Sanchez-Amat, Antonio; and Davidson, Victor L., "Interaction Of Goxa With Its Modifying Enzyme And Its Subunit Assembly Are Dependent On The Extent Of Cysteine Tryptophylquinone Biosynthesis" (2016). Scopus Export 2015-2019. 2927.
https://stars.library.ucf.edu/scopus2015/2927