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Trametes versicolor ligninase: Isozyme sequence homology and substrate specificity
Author(s) -
Jönsson Leif,
Karlsson Olov,
Lundquist Knut,
Nyman Per Olof
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81258-x
Subject(s) - phanerochaete , chrysosporium , isozyme , edman degradation , trametes versicolor , lignin peroxidase , biochemistry , biology , lignin , enzyme , microbiology and biotechnology , chemistry , peptide sequence , peroxidase , botany , gene , laccase
The substrate specificity of three ligninase isozymes from the white‐rot fungus Trametes versicolor has been investigated using stereochemically defined synthetic dimeric models for lignin. The isozymes have been found to attack non‐phenolic β‐ O ‐4 as well as β‐1 lignin model compounds. This finding confirms the classification of the isozymes from T. versicolor as ligninases. The amino‐terminal residues of the three isozymes from T. versicolor have been determined using Edman degradation. Minor differences found between the sequences suggest the existence of several structural genes for ligninase in T. versicolor . Comparisons have been made with the sequences of three previously reported ligninases from Phanerochaete chrysosporium , another lignin‐degrading fungus. One of the sequences from P. chrysosporium is distinctly more similar to the T. versicolor isozymes than to the other two sequences from P. chrysosporium .