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 :
a and .[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.
