A new versatile peroxidase from Pleurotus.
Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanerochaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn(2+), hydroquinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn(2+)-binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn(2+)-binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed.
Ruiz-Dueñas
F J
FJ
Centro de Investigaciones Biológicas, CSIC, Velázquez 144, E-28006 Madrid, Spain.
Camarero
S
S
Pérez-Boada
M
M
Martínez
M J
MJ
Martínez
A T
AT
D001665:Binding Sites; D003001:Cloning, Molecular; D008031:Lignin / Q000378:metabolism*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020076:Pleurotus / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D013379:Substrate Specificity
D008031:Lignin; D010544:Peroxidases; C042858:lignin peroxidase; C051129:manganese peroxidase