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Discovery and Characterization of New O-methyltransferase From the Genome of the Lignin-Degrading Fungus Phanerochaete Chrysosporium for Enhanced Lignin Degradation

Discovery and Characterization of New O-methyltransferase From the Genome of the Lignin-Degrading Fungus Phanerochaete Chrysosporium for Enhanced Lignin Degradation

Le Thanh Mai Pham, Yong Hwan Kim

Enzyme Microb Technol. 2016 Jan;82:66-73.

PMID: 26672450

Abstract:

Using bioinformatic homology search tools, this study utilized sequence phylogeny, gene organization and conserved motifs to identify members of the family of O-methyltransferases from lignin-degrading fungus Phanerochaete chrysosporium. The heterologous expression and characterization of O-methyltransferases from P. chrysosporium were studied. The expressed protein utilized S-(5'-adenosyl)-L-methionine p-toluenesulfonate salt (SAM) and methylated various free-hydroxyl phenolic compounds at both meta and para site. In the same motif, O-methyltransferases were also identified in other white-rot fungi including Bjerkandera adusta, Ceriporiopsis (Gelatoporia) subvermispora B, and Trametes versicolor. As free-hydroxyl phenolic compounds have been known as inhibitors for lignin peroxidase, the presence of O-methyltransferases in white-rot fungi suggested their biological functions in accelerating lignin degradation in white-rot basidiomycetes by converting those inhibitory groups into non-toxic methylated phenolic ones.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP52248030	S-(5′-Adenosyl)-L-methionine p-toluenesulfonate salt		52248-03-0	Price

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