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.
MeSH terms
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Amino Acid Oxidoreductases / chemistry
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Amino Acid Oxidoreductases / genetics
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Amino Acid Oxidoreductases / metabolism*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Dipeptides / chemistry
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Dipeptides / metabolism*
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Escherichia coli / genetics
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Indolequinones / chemistry
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Indolequinones / metabolism*
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Marinomonas / chemistry
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Marinomonas / genetics
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Marinomonas / metabolism*
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Protein Interaction Maps
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Protein Multimerization
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
Substances
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Bacterial Proteins
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Dipeptides
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Indolequinones
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Recombinant Proteins
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cysteine tryptophylquinone
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Amino Acid Oxidoreductases
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glycine oxidase