Literature summary for 1.11.1.16 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.

Search for more literature for 1.11.1.16

Application

Application	Comment	Organism
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

Protein Variants

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

Organism

Organism	UniProt	Comment	Textmining
Pleurotus eryngii	O94753	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
additional information	versatile peroxidase is able to oxidize typical substrates of other peroxidases, these hybrid 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	?	-	?
Reactive Black 5 + H2O2	versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation	Pleurotus eryngii	?	-	?
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

Synonyms	Comment	Organism
versatile peroxidase	-	Pleurotus eryngii

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Release 2023.1 (January 2023)