Homology among multiple extracellular peroxidases from Phanerochaete chrysosporium.
The extracellular peroxidases of Phanerochaete chrysosporium were separated into 21 proteins by analytical isoelectric focusing. Fifteen of these enzymes oxidized veratryl alcohol (lignin peroxidases) in the presence of H2O2. Six enzymes were Mn(II)-dependent peroxidases. The Mn(II)-dependent enzymes appeared and reached their maximal activity earlier than the lignin peroxidases in the cultures. Peptide mapping, amino acid analysis, and reaction against specific antibodies showed that all the Mn(II)-dependent peroxidases were probably products of one gene. A great degree of homology was also present among the various lignin peroxidases.
D000596:Amino Acids / Q000032:analysis; D001592:Benzyl Alcohols / Q000378:metabolism; D000939:Epitopes / Q000276:immunology; D005658:Fungi / Q000201:enzymology*; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007525:Isoelectric Focusing; D007700:Kinetics; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D010105:Oxygenases / Q000276:immunology / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D010544:Peroxidases / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D010637:Phenolsulfonphthalein / Q000378:metabolism
D000596:Amino Acids; D001592:Benzyl Alcohols; D000939:Epitopes; D010446:Peptide Fragments; D008345:Manganese; D006861:Hydrogen Peroxide; D010544:Peroxidases; C042858:lignin peroxidase; D010105:Oxygenases; D010637:Phenolsulfonphthalein; C042197:veratryl alcohol