Lignin-degrading peroxidases of Phanerochaete chrysosporium.
Lignin and manganese peroxidases are secreted by the basidiomycete Phanerochaete chrysosporium during secondary metabolism. These enzymes play major roles in lignin degradation. The active site amino acid sequence of these lignin-degrading peroxidases is similar to that of horseradish peroxidase (HRP) and cytochrome c peroxidase (CcP). The mechanism by which they oxidize substrates also appears to be the similar. pH has a similar effect on lignin peroxidase compound I formation as on HRP or CcP; however, the pKa controlling compound I formation for lignin peroxidase appears to be much lower. Lignin-degrading peroxidases are able to catalyze the oxidation of substrates with high redox potential. This unique ability is consistent with a heme active site of low electron density, which is indicated by high redox potential.
Cai
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Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.
Tien
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D000595:Amino Acid Sequence; D001487:Basidiomycota / Q000201:enzymology*; D001665:Binding Sites; D006418:Heme / Q000737:chemistry; D007700:Kinetics; D008031:Lignin / Q000378:metabolism*; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*
D006418:Heme; D008031:Lignin; D010544:Peroxidases; C042858:lignin peroxidase; C051129:manganese peroxidase