Interaction of GoxA with Its Modifying Enzyme and Its Subunit Assembly Are Dependent on the Extent of Cysteine Tryptophylquinone Biosynthesis

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• 作者：Esha Sehanobish ; Jonatan C. Campillo-Brocal ; Heather R. Williamson ; Antonio Sanchez-Amat ; Victor L. Davidson
• 刊名：Biochemistry
• 出版年：2016
• 出版时间：April 26, 2016
• 年：2016
• 卷：55
• 期：16
• 页码：2305-2308
• 全文大小：242K
• 年卷期：0
• ISSN：1520-4995

文摘

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.