Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates.
A versatile ligninolytic peroxidase has been cloned from Pleurotus eryngii and its allelic variant MnPL2 expressed in Aspergillus nidulans, with properties similar to those of the mature enzyme from P. eryngii. These include the ability to oxidize Mn(2+) and aromatic substrates, confirming that this is a new peroxidase type sharing catalytic properties of lignin peroxidase and manganese peroxidase.
Ruiz-Dueñas
F J
FJ
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, E-28006 Madrid, Spain.
Martínez
M J
MJ
Martínez
A T
AT
D001230:Aspergillus / Q000235:genetics; D008345:Manganese / Q000378:metabolism*; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D020076:Pleurotus / Q000201:enzymology*; D011994:Recombinant Proteins / Q000378:metabolism
D011994:Recombinant Proteins; D008345:Manganese; D010544:Peroxidases; C042858:lignin peroxidase; C051129:manganese peroxidase