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Trametes versicolor ligninase: isozyme sequence homology and substrate specificity
L Jönson1, O Karlsson, K Lundquist
1Division of Biochemistry, University of Lund, Sweden.
FEBS Letters
|April 10, 1989
Summary
Three ligninase isozymes from Trametes versicolor degrade non-phenolic lignin models. Sequence analysis reveals distinct structural genes for ligninase in T. versicolor, with one P. chrysosporium sequence showing high similarity.
Area of Science:
- Biochemistry
- Mycology
- Enzymology
Background:
- Lignin degradation is crucial for carbon cycling.
- White-rot fungi possess enzymes like ligninases to break down lignin.
- Understanding ligninase function and diversity is key to biotechnological applications.
Purpose of the Study:
- To investigate the substrate specificity of three ligninase isozymes from Trametes versicolor.
- To analyze the amino-terminal sequences of these isozymes and compare them with other lignin-degrading fungi.
Main Methods:
- Utilized stereochemically defined synthetic dimeric lignin model compounds.
- Performed Edman degradation to determine amino-terminal sequences.
- Comparative sequence analysis with ligninases from Phanerocompaete chrysosporium.
Main Results:
- Trametes versicolor ligninases attack both non-phenolic beta-O-4 and beta-1 lignin model compounds.
- Amino-terminal sequencing revealed minor sequence differences, suggesting multiple ligninase genes in T. versicolor.
- One Phanerocompaete chrysosporium ligninase sequence showed significant similarity to the T. versicolor isozymes.
Conclusions:
- The studied isozymes from T. versicolor are confirmed as ligninases based on their substrate specificity.
- Evidence supports the existence of diverse ligninase structural genes within T. versicolor.
- Comparative genomics suggests evolutionary relationships among lignin-degrading enzymes in different fungal species.