Laccase
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Function
CotA laccase belong to the multi-copper oxidase family. The multi-copper oxidases constitute a family of enzymes whose principal members are laccase (benzenediol oxygen oxidoreductase, EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) oxygen oxidoreductase, EC 1.16.3.1). Similar to the other laccases the three dimensional structure of CotA 1w6l comprises three cupredoxin domains and four copper ions organised in Two copper centers: a mononuclear blue type 1 copper center and a trinuclear center[1]
Structural highlights
The trinuclear center has two type 3 copper ions, that can be anti-ferromagnetically coupled through an hydroxyl moiety in between them, and one type 2 copper ion.‡ The mononuclear copper is able to accept an electron from a variety of phenolic substrates and then transmit it to the trinuclear centre.
3D structures of CotA laccase
Updated on 14-December-2015
References
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Michal Harel, Isabel Bento, Alexander Berchansky, Jaime Prilusky, David Canner