Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion‐dependent autooxidation of a specific tyrosyl residue
- 12 September 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 351 (3) , 360-364
- https://doi.org/10.1016/0014-5793(94)00884-1
Abstract
The quinone of 2,4,5-trihydroxyphenylalanine (topa), recently identified as the covalently bound redox cofactor in copper amine oxidases, is encoded by a specific tyrosine codon. To elucidate the mechanism of its formation, the recombinant phenylethylamine oxidase of Arthrobacter globiformis has been overproduced in Escherichia coli and purified in a Cu2+-deficient form. The inactive precursor enzyme thus obtained was dramatically activated upon incubation with Cu2+, concomitantly with the formation of the topa quinone at the position corresponding to Tyr382, occurring in the tetrapeptide sequence highly conserved in this class of enzymes. The topa quinone was produced only under aerobic conditions, but its formation required no external enzymatic systems. These findings demonstrate the Cu2+-dependent autooxidation of a specific tyrosyl residue to generate the topa quinone cofactor.Keywords
This publication has 15 references indexed in Scilit:
- Cloning and Sequencing of Phenylethylamine Oxidase from Arthrobacter globiformis and Implication of Tyr-382 as the Precursor to Its Covalently Bound Quinone CofactorBiochemical and Biophysical Research Communications, 1994
- Autocatalytic generation of Dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the Dopa-208 proteinBiochemistry, 1993
- Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotrophJournal of Bacteriology, 1993
- Identification of topaquinone and its consensus sequence in copper amine oxidasesBiochemistry, 1992
- Evidence for copper and 3,4,6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the gram-negative bacterium Escherichia coli K-12Biochemical Journal, 1992
- An investigation of bovine serum amine oxidase active site stoichiometry: evidence for an aminotransferase mechanism involving two carbonyl cofactors per enzyme dimerBiochemistry, 1991
- A New Redox Cofactor in Eukaryotic Enzymes: 6-Hydroxydopa at the Active Site of Bovine Serum Amine OxidaseScience, 1990
- Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorphaBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1989
- A simple approximation of weight-based protein measurement with HPLC apparatus.Agricultural and Biological Chemistry, 1989
- Enzymatic Determination of Total Serum CholesterolClinical Chemistry, 1974