A pluripotent polyphenol oxidase from the melanogenic marine Alteromonas sp shares catalytic capabilities of tyrosinases and laccases.
The recently characterized marine melanogenic bacterium MMB-1 contains a pluripotent polyphenol oxidase (PPO) which catalyzes the oxidation of a very wide range of substrates considered specific for tyrosinase or laccase. This range includes monophenols such as L-tyrosine, o-diphenols such as L-dopa, p-diphenols such as hydroquinone, o-aminophenols such as 3-hydroxyanthranilic acid, activated monophenols such as 2,6-dimethoxyphenol and syringaldazine, and chromophores such as ABTS. This is the first report of an enzyme that is able to catalyze the oxidation of compounds so far considered specific for tyrosinases (L-tyrosine) or laccase (syringaldazine), showing cresolase, catechol oxidase and laccase activities. Such PPO could be a very useful model to study the structural requirements, catalytic mechanisms and involvement of the copper sites existing in non-blue and blue copper-oxidases.
Sanchez-Amat
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Department of Genetics and Microbiology, University of Murcia, Spain.
Solano
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D004156:Catechol Oxidase / Q000737:chemistry / Q000378:metabolism*; D003300:Copper / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D016946:Gram-Negative Aerobic Rods and Cocci / Q000201:enzymology*; D042845:Laccase; D015394:Molecular Structure; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D010636:Phenols / Q000378:metabolism; D013053:Spectrophotometry; D013379:Substrate Specificity
D010636:Phenols; D003300:Copper; D010088:Oxidoreductases; D004156:Catechol Oxidase; D042845:Laccase; D014442:Monophenol Monooxygenase