Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor.
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.
Hanlon
S P
SP
Department of Biochemistry, University of Leicester, U.K.
Carpenter
K
K
Hassan
A
A
Cooper
R A
RA
D006631:Amine Oxidase (Copper-Containing) / Q000096:biosynthesis* / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000235:genetics; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology*; D008969:Molecular Sequence Data; D009154:Mutation
C092737:3,4,6-trihydroxyphenylalanine quinone; D017931:DNA Primers; D004295:Dihydroxyphenylalanine; C086534:phenylethylamine oxidase; D006631:Amine Oxidase (Copper-Containing)