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Literature summary extracted from

  • Ruiz-Duenas, F.J.; Morales, M.; Garcia, E.; Miki, Y.; Martinez, M.J.; Martinez, A.T.
    Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases (2009), J. Exp. Bot., 60, 441-452.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.11.1.16 degradation versatile peroxidase presents particular interest due to its catalytic versatility including the degradation of compounds that other peroxidases are not able to oxidize directly, versatile peroxidase versatility permits its application in Mn3+-mediated or Mn-independent reactions on both low and high redox-potential aromatic substrates and dyes, versatile peroxidase can be used to reoxidize Mn-containing polyoxometalates, which are efficient oxidizers in paper pulp delignification Pleurotus eryngii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.13 manganese peroxidase crystallizes in the presence of Mn2+, where three homologous residues (Glu35, Glu39, and Asp179) participate in metal co-ordination, opening of the glutamate side-chains is not observed in manganese peroxidase crystals grown in the absence of Mn2+ Phanerodontia chrysosporium

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.16 A260F/R257A site-directed mutagenesis Pleurotus eryngii
1.11.1.16 R257D versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation Pleurotus eryngii

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.13 Phanerodontia chrysosporium Q02567
-
-
1.11.1.14 Phanerodontia chrysosporium P49012
-
-
1.11.1.16 Pleurotus eryngii O94753
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.13 Mn2+ + H2O2
-
 Phanerodontia chrysosporium Mn3+ + H2O
-
 ?
1.11.1.14 additional information lignin peroxidase is not able to oxidize phenolic compounds efficiently because of inactivation in the absence of veratryl alcohol or related substrates Phanerodontia chrysosporium ?
-
 ?
1.11.1.14 Reactive Black 5 + H2O2 lignin peroxidase can only oxidize Reactive Black 5 in the presence of redox mediators such as veratryl alcohol Phanerodontia chrysosporium ?
-
 ?
1.11.1.14 veratryl alcohol + H2O2 + H+
-
 Phanerodontia chrysosporium veratraldehyde + H2O
-
 ?
1.11.1.16 Mn2+ + H2O2 the Mn2+-binding site in versatile peroxidase is formed by the side-chains of Glu36, Glu40, and Asp175 located in front of the internal (i.e. more distant from the main haem access-channel) propionate of haem, and connected to the solvent by a narrow access-channel that presents a variable geometry during catalysis Pleurotus eryngii Mn3+ + H2O
-
 ?
1.11.1.16 additional information versatile peroxidase is able to oxidize typical substrates of other peroxidases, these ย‘hybridย’ properties are due to the coexistence in a single protein of different catalytic sites reminiscent of those present in the other basidiomycete peroxidase families Pleurotus eryngii ?
-
 ?
1.11.1.16 Reactive Black 5 + H2O2 versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation Pleurotus eryngii ?
-
 ?
1.11.1.16 veratryl alcohol + H2O2 + H+ a solvent-exposed tryptophan is the catalytically-active residue in veratryl alcohol oxidation, initiating an electron transfer pathway to haem Pleurotus eryngii veratraldehyde + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.13 manganese peroxidase
-
 Phanerodontia chrysosporium
1.11.1.14 lignin peroxidase
-
 Phanerodontia chrysosporium
1.11.1.14 LIP
-
 Phanerodontia chrysosporium
1.11.1.16 versatile peroxidase
-
 Pleurotus eryngii