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Literature summary for 1.11.1.14 extracted from

  • Houtman, C.J.; Maligaspe, E.; Hunt, C.G.; Fernandez-Fueyo, E.; Martinez, A.T.; Hammel, K.E.
    Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant (2018), J. Biol. Chem., 293, 4702-4712 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene LPOA, recombinant expression of the codon-optimized gene in Escherichia coli strain W3110. The cloned expression vector pFLAG1 and the resulting plasmid pFLAG1-Y00262 are directly used for expression, Escherichia coli strain DH5x02alpha is used for plasmid propagation. The apoenzyme accumulates in inclusion bodies Phanerodontia chrysosporium

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 veratryl alcohol + H2O2 Phanerodontia chrysosporium
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2 veratryl aldehyde + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium P06181 isozyme LPOA
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Purification (Commentary)

Purification (Comment) Organism
active solubilized recombinant enzyme expressed from Escherichia coli strain W3110 is purified by anion exchange chromatography using a 0-300 mM NaCl gradient (20 min, 2 ml/min flow rate) in 10 mM sodium tartrate, pH 5.5, containing 1 mM CaCl2 Phanerodontia chrysosporium

Renatured (Commentary)

Renatured (Comment) Organism
recombinant apoenzyme from inclusion bodies after expression in Escherichia coli strain W3110 by solubilization with 8 M urea. Subsequent in vitro refolding of the enzyme LP is performed using 2.1 M urea, 5 mM Ca2+, 0.01 mM hemin, 0.7 mM oxidized glutathione, 0.1 mM dithiothreitol, and 0.2 mg/ml protein, at pH 8.0 Phanerodontia chrysosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 veratryl alcohol + H2O2
-
Phanerodontia chrysosporium 2 veratryl aldehyde + 2 H2O
-
?
4-methoxymandelic acid + veratryl alcohol
-
Phanerodontia chrysosporium ?
-
?
additional information the fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant. Reaction-diffusion model and solution-phase model, overview. The oxidation of veratryl alcohol (VA) by the enzyme in air at physiological pH 4.5 consumes O2 and produces about 1.1 veratraldehyde per H2O2 supplied. This finding suggests that some VAx02cation radical may escape oxidation at the enzyme's active site, hydrolyzing instead to give benzylic radicals that rapidly add O2. The resulting alpha-hydroxyperoxyl radicals would in turn eliminate the H2O2 precursor HO2 radical, thus accounting for the enhancement in veratraldehyde yield. VA is required for the enzyme to oxidize 4-methoxymandelic acid, which quenches the ESR signal of the VA produced, and veratraldehyde production during these reactions occurs only after all of the 4-methoxymandelic acid has been consumed. Moreover, the rate of 4-methoxymandelic acid oxidation by the enzyme exhibits saturation kinetics as the concentration of VA is increased. Enzymatic oxidations of dye-functionalized beads Phanerodontia chrysosporium ?
-
-

Subunits

Subunits Comment Organism
? x * 42000, SDS-PAGE Phanerodontia chrysosporium

Synonyms

Synonyms Comment Organism
fungal lignin peroxidase
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Phanerodontia chrysosporium
ligninase H8 UniProt Phanerodontia chrysosporium
LPA
-
Phanerodontia chrysosporium
LPOA UniProt Phanerodontia chrysosporium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Phanerodontia chrysosporium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
assay at Phanerodontia chrysosporium

Cofactor

Cofactor Comment Organism Structure
heme
-
Phanerodontia chrysosporium

General Information

General Information Comment Organism
evolution isozyme lignin peroxidase A, LPA, is the major isozyme of the LP H8 family Phanerodontia chrysosporium
physiological function peroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. Low-molecularweight oxidants likely have a primary role in lignin breakdown because many of these fungi delignify wood before its porosity has sufficiently increased for enzymes to infiltrate. It has been proposed that lignin peroxidases fulfill this role by oxidizing the secreted fungal metabolite veratryl alcohol to its aryl cation radical, releasing it to act as a one-electron lignin oxidant within woody plant cell walls, but the fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant. Isozyme LPA releases insignificant quantities of VA cation radical, and a different mechanism produces small ligninolytic oxidants during white rot Phanerodontia chrysosporium