Article
Formation in vitro of the 3,4,6-trihydroxyphenylalanine quinone cofactor.
The Biochemical journal - 15 Mar 1995
Hanlon S P, Carpenter K, Hassan A, Cooper R A
Abstract excerpt
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...
Topics
- Amine Oxidase (Copper-Containing)
- Base Sequence
- Cloning, Molecular
- DNA Primers
- Dihydroxyphenylalanine
- Enzyme Activation
- Escherichia coli
- Molecular Sequence Data
- Mutation