TY - JOUR
T1 - Laccases of prokaryotic origin
T2 - Enzymes at the interface of protein science and protein technology
AU - Martins, Ligia Maria
AU - Durão, Paulo
AU - Brissos, Vania Sofia
AU - Lindley, Peter F.
PY - 2015/3/1
Y1 - 2015/3/1
N2 - 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.
AB - 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.
KW - Biotechnology
KW - Laccases
KW - Ligninolysis
KW - Metal resistance
KW - Metalloxidases
KW - Structure-function
UR - http://www.scopus.com/inward/record.url?scp=84926635382&partnerID=8YFLogxK
U2 - 10.1007/s00018-014-1822-x
DO - 10.1007/s00018-014-1822-x
M3 - Review article
C2 - 25572294
AN - SCOPUS:84926635382
SN - 1420-682X
VL - 72
SP - 911
EP - 922
JO - Cellular and Molecular Life Sciences
JF - Cellular and Molecular Life Sciences
IS - 5
ER -