caa a22 4500 606176845 CHVBK 20210128100749.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00018-014-1822-x doi (NATIONALLICENCE)springer-10.1007/s00018-014-1822-x Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology [Elektronische Daten] [Lígia Martins, Paulo Durão, Vânia Brissos, Peter Lindley] 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. Springer Basel, 2015 Metalloxidases nationallicence Laccases nationallicence Structure-function nationallicence Metal resistance nationallicence Biotechnology nationallicence Ligninolysis nationallicence Martins Lígia Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal aut Durão Paulo Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal aut Brissos Vânia Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal aut Lindley Peter Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal aut Cellular and Molecular Life Sciences Springer Basel 72/5(2015-03-01), 911-922 1420-682X 72:5<911 2015 72 18 https://doi.org/10.1007/s00018-014-1822-x text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-014-1822-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Martins Lígia Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal aut NATIONALLICENCE 700 1- Durão Paulo Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal aut NATIONALLICENCE 700 1- Brissos Vânia Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal aut NATIONALLICENCE 700 1- Lindley Peter Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, 2781-901, Oeiras, Portugal aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/5(2015-03-01), 911-922 1420-682X 72:5<911 2015 72 18