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Figure 6.12 Crystal structures of lignin peroxidase from Phanerochaete chrysosporium
[104] (RCSB PDB Entry: 1LGA, top left), manganese peroxidase from P. chrysosporium
[106] (RCSB PDB Entry: 3M5Q, top right), versatile peroxidase from Pleurotus eryngii
[121] (RCSB PDB Entry: 2BOQ, bottom left), and dye-decolorizing peroxidase from
Bjerkandera adusta [77] (RCSB PDB Entry: 3AFV, bottom right).
extracellular fluid of numerous white rot fungi, including Pleurotus spp.,
Trametes ( Coriolus ) spp., and Bjerkandera spp. [114]. Later it was found that
some isozymes from P. ostreatus and P. eryngii could exhibit both MnP and
LiP activities [115,116]. These enzymes were called by a number of names,
such as Mn-independent peroxidase and hybrid peroxidase; however, it
is currently described as versatile peroxidase (reactive-black-5:hydrogen-
peroxide oxidoreductase; EC 1.11.1.16) [115]. This new enzyme can oxi-
dize a diazo dye Reactive Black 5 (Figure 6.3) that cannot be oxidized by
Mn 3+ , as well as hydroquinones and other dye molecules [116]. Versatile
peroxidase is closely related to LiP and MnP and is a member of class II
peroxidases in the non-animal peroxidase group.
More recently, another new type of fungal peroxidase called DyP
(reactive-blue-5:hydrogen-peroxide oxidoreductase; EC 1.11.1.19) that is
able to decolorize a large number of synthetic dyes has been isolated from
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