title: Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
abstract: The ubiquitous members of the multicopper oxidase family of enzymes oxidize a range of aromatic substrates such as polyphenols, methoxy-substituted phenols, amines and inorganic compounds, concomitantly with the reduction of molecular dioxygen to water. This family of enzymes can be broadly divided into two functional classes: metalloxidases and laccases. Several prokaryotic metalloxidases have been described in the last decade showing a robust activity towards metals, such as Cu(I), Fe(II) or Mn(II) and have been implicated in the metal metabolism of the corresponding microorganisms. Many laccases, with a superior efficiency for oxidation of organic compounds when compared with metals, have also been identified and characterized from prokaryotes, playing roles that more closely conform to those of intermediary metabolism. This review aims to present an update of current knowledge on prokaryotic multicopper oxidases, with a special emphasis on laccases, anticipating their enormous potential for industrial and environmental applications.
authors.affiliation: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal, lmartins@itqb.unl.pt.
authors.forename: Lígia O
authors.initials: LO
authors.lastname: Martins
authors.forename: Paulo
authors.initials: P
authors.lastname: Durão
authors.forename: Vânia
authors.initials: V
authors.lastname: Brissos
authors.forename: Peter F
authors.initials: PF
authors.lastname: Lindley
mesh_terms: D001419:Bacteria / Q000201:enzymology; D042845:Laccase / Q000737:chemistry / Q000378:metabolism*; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D011387:Prokaryotic Cells / Q000201:enzymology*; D017434:Protein Structure, Tertiary
chemical_list: D008670:Metals; D042845:Laccase