Biochem J. 1995 Mar 15;306 ( Pt 3):627-30.

Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor.

Hanlon SP, Carpenter K, Hassan A, Cooper RA.

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Department of Biochemistry, University of Leicester, U.K.

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.

PMID:: 7702553; [PubMed - indexed for MEDLINE]
PMCID:: PMC1136567

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Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor.
Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor.
Biochem J. 1995 Mar 15 ;306 ( Pt 3):627-30.

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