Group C segregates from the LMP groups A and B
(Fig. 2), and comprises basidiomycetous class II POXs
with variant primary structures and mostly unknown
functions. It is likely that with emerging POX and LMP
sequences predicted from fungal genomes, this group
will further diverge into new enzyme sub-families and
clades.
The best characterised group C enzyme is the CIP
(ARP) from Coprinopsis (Coprinus) cinerea [81, 91], which
readily oxidizes phenols and smaller dye molecules [92]
likewise the class III plant peroxidase HRP (EC 1.11.1.7),
but is unable to oxidize Mn2+ or high-redox potential
substrates like lignin-model compounds or veratryl
alcohol, and is thereby not considered as LMP or LME.
CIP has been adopted for e.g. removal of phenolic compounds
from aqueous solutions and waste waters [92].
Some of group C peroxidases contain a Trp in a sequence
position similar to LIPs and VPs (Ganoderma
POXs) or a catalytically postulated tyrosine (Tyr) near
this location (Trametes cervina POX). The latter, TcPOX
was originally depicted as LIP [93] but the apparent lack
of the exposed tryptophan and phylogenetic positioning
in group C excludes true LIP-like catalytic function for
the enzyme.