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.

• Publication year

  1987

• Venue

  Journal of Biological Chemistry

• Publication date

  1987-01-05

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1016/s0021-9258(19)75943-2PMID 2432065
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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