Laccases: structure, reactions, distribution.
Laccases (EC 1.10.3.2, p-diphenol: dioxygen oxidoreductases) are multi-copper proteins that use molecular oxygen to oxidize various aromatic and non-aromatic compounds by a radical-catalyzed reaction mechanism. The enzymes are involved in the pathogenicity, immunity and morphogenesis of organisms and in the metabolic turnover of complex organic substances such as lignin or humic matter. Owing to their high non-specific oxidation capacity, laccases are useful biocatalysts for diverse biotechnological applications. Until recently, laccases were only found in eukaryotes (fungi, higher plants, insects), but now there is strong evidence for their widespread distribution in prokaryotes and the first crystal structure of a bacterial laccase is already available. Phylogenetically, laccases are members of the multi-copper protein family including ascorbate oxidase, ceruloplasmin and bilirubin oxidase.
Claus
Harald
H
Institut für Molekulare Biophysik, University of Mainz Jakob-Welder-Weg 26, 55128 Mainz, Germany. hcdclaus@t-online.de
D000818:Animals; D002384:Catalysis; D003300:Copper / Q000737:chemistry; D042845:Laccase / Q000737:chemistry* / Q000378:metabolism
D003300:Copper; D042845:Laccase