PMID:7702553

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Citation

Hanlon, SP, Carpenter, K, Hassan, A and Cooper, RA (1995) Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor. Biochem. J. 306 ( Pt 3):627-30

Abstract

An Escherichia coli K-12 2-phenylethylamine oxidase gene with a mutated leader sequence region produced a largely inactive form of the enzyme in the cytoplasm. This form of the enzyme was activated 30-50-fold on incubation at 30 degrees C in the absence of any added cofactors. After activation the enzyme contained a quinone which was not detected in the non-activated form. This is the first report of the formation in vitro of any quinoenzyme cofactor.

Links

PubMed PMC1136567

Keywords

Amine Oxidase (Copper-Containing)/biosynthesis; Amine Oxidase (Copper-Containing)/genetics; Base Sequence; Cloning, Molecular; DNA Primers; Dihydroxyphenylalanine/analogs & derivatives; Dihydroxyphenylalanine/biosynthesis; Dihydroxyphenylalanine/genetics; Enzyme Activation; Escherichia coli/enzymology; Molecular Sequence Data; Mutation

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