Trametes cervina

A few years ago, a different LiP-type peroxidase was reported in the white-rot basidiomycete Trametes cervina. This enzyme has an exposed tyrosine residue that seems to be involved in catalysis [73]. Curiously, this catalytic tyrosine occupies the equivalent position to that of an aspartate residue forming the Mn2+ oxidation site in MnP and VP. Additional work is necessary to confirm the catalytic role of this amino acid residue. 

Miki Y, Tanaka H, Nakamura M et al (2006) Isolation and characterization of a novel lignin peroxidase from the white-rot basidiomycete Trametes cervina. J Fac Agr Kyushu Univ 51 99-104... 

In some enzymes, the protein radical appears to participate in substrate oxidation. Evidence exists for the involvement of a surface tryptophan in the oxidation of veratryl alcohol by the ligninase from Phanerochaete chrysosporium [33]. Similarly, tryptophan radicals on the surface of the versatile peroxidases from Pleurotus eryngii and Bjerkandera adjusta [34—36], and a tyrosine in the LiP from Trametes cervina [33], are thought to be involved in substrate oxidation. 

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