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Literature summary for 1.11.1.16 extracted from

  • Hernandez-Bueno, N.S.; Suarez-Rodríguez, R.; Balcazar-Lopez, E.; Folch-Mallol, J.L.; Ramirez-Trujillo, J.A.; Iturriaga, G.
    A versatile peroxidase from the fungus Bjerkandera adusta confers abiotic stress tolerance in transgenic tobacco plants (2021), Plants (Basel), 10, 859 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.11.1.16

Activating Compound

Activating Compound Comment Organism Structure
additional information veratryl alcohol, which increases the ability of LiP to oxidize high-redox-potential substrates, does not affect oxidation of these by versatile peroxidases of Bjerkandera adusta Bjerkandera adusta

Application

Application Comment Organism
agriculture overproducing the VP gene in plants increases significantly their biomass and the abiotic stress tolerance. The versatile peroxidase enzyme is an effective biotechnological tool to protect organisms against ROS. In transgenic tobacco plants, it improves drought, salt, and oxidative stress tolerance. Thus, the versatile peroxidase gene represents a great potential for obtaining stress-tolerant crops. The enzyme from Bjerkandera adusta can mitigate oxidative stress induced by paraquat, salt- (NaCl), drought- and osmotic-stress (sorbitol) Bjerkandera adusta
environmental protection versatile peroxidases form an attractive ligninolytic enzyme group due to their dual oxidative ability to oxidize Mn(II) and also phenolic and nonphenolic aromatic compounds, and can be used in programs for phytoremediation Bjerkandera adusta

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant enzyme expression in Nicotiana tabacum cv. Petite Havana via an Agrobacterium tumefaciens strain LBA4404 transformation procedure, expression under control of the CaMV 35S promoter. Selection of the VP lines VP22, VP24, and VP27 with higher MnP (EC 1.11.1.13) activities Bjerkandera adusta

Protein Variants

Protein Variants Comment Organism
additional information versatile peroxidase from the fungus Bjerkandera adusta confers abiotic stress tolerance in transgenic tobacco plants. Thirty independent T2 transgenic VP lines overexpressing the fungal Bjerkandera adusta VP gene are selected on kanamycin. The VP22, VP24, and VP27 lines show significant manganese peroxidase (MnP) activity. The highest is VP22, which shows 10.87fold more manganese peroxidase activity than the wild-type plants and leads to a 34% increase in plant height and 28% more biomass. The VP22, VP24, and VP27 lines show enhanced tolerance to drought, 200 mM NaCl, and 400 mM sorbitol. Also, these transgenics display significant tolerance to methyl viologen, an active oxygen-generating compound. The average stem length of transgenic tobacco plants expressing the VP gene is approximately 34% taller than the wild-type plants, and there is a 28% average increase in fresh weight after three months in greenhouse conditions. Phenotypes, detailed overview Bjerkandera adusta

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Bjerkandera adusta
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2 Bjerkandera adusta
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 2 Mn(III) + 2 H2O
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 ?
2 Mn(II) + 2 H+ + H2O2 Bjerkandera adusta UAMH8258
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 2 Mn(III) + 2 H2O
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 ?
additional information Bjerkandera adusta ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds ?
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additional information Bjerkandera adusta UAMH8258 ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds ?
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Organism

Organism UniProt Comment Textmining
Bjerkandera adusta Q3SC77
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Bjerkandera adusta UAMH8258 Q3SC77
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Reaction

Reaction Comment Organism Reaction ID
2 manganese(II) + 2 H+ + H2O2 = 2 manganese(III) + 2 H2O the versatile peroxidase catalytic mechanism is similar to classic peroxidases, in which substrate oxidation is carried out by a two-electron multistep reaction at the expense of hydrogen peroxide. Versatile peroxidases oxidize Mn2+ (as MnP), degrade the lignin model dimer veratryl glycerol-guaiacylether to yield veratraldehyde, and oxidize veratryl alcohol and dimethoxybenzene to veratraldehyde and p-benzoquinone, respectively Bjerkandera adusta
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2
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 Bjerkandera adusta 2 Mn(III) + 2 H2O
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 ?
2 Mn(II) + 2 H+ + H2O2
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 Bjerkandera adusta UAMH8258 2 Mn(III) + 2 H2O
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 ?
additional information ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds Bjerkandera adusta ?
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additional information versatile peroxidase has a high affinity for H2O2, Mn2+, ferulic acid, naphthol, and different hydroquinones and dyes, but their affinities for veratryl alcohol and substituted phenols are lower Bjerkandera adusta ?
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additional information ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds Bjerkandera adusta UAMH8258 ?
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additional information versatile peroxidase has a high affinity for H2O2, Mn2+, ferulic acid, naphthol, and different hydroquinones and dyes, but their affinities for veratryl alcohol and substituted phenols are lower Bjerkandera adusta UAMH8258 ?
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Subunits

Subunits Comment Organism
More the enzyme structure includes 12 alpha-helices (Phe3-Gln20, Leu44-Phe57, Glu63-His74, Val114-Val125, Ala131-Cys147, Val178-Ala188, Thr193-Ala207, Thr229-Leu237, Gln263-Ala269, Ser271-Asn283, Gln285-Ile301, Ile338-Ala341), and two short beta-sheets (Gly-Ile100, Glu51-Val52) Bjerkandera adusta

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
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 with aromatic compounds and dyes Bjerkandera adusta
5
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 with substrate Mn2+ Bjerkandera adusta

Cofactor

Cofactor Comment Organism Structure
heme the predicted heme-binding residues are His66, Glu67, Leu69, Arg70, Phe73, Pro172, Glu173, Pro174, Ile181, Phe185, Leu199, Leu200, Ser202, His203, Ile205, Ala206, Ala207, Ala208, Asp209, His210, Val211, Phe220, Leu262, Ser264, Phe292, and Met296 Bjerkandera adusta

General Information

General Information Comment Organism
evolution the most important ligninolytic enzymes of white-rot fungi, which efficiently degrade lignin and a wide range of aromatic xenobiotics, including polychlorinated phenols, nitro- and amino-substituted phenols, synthetic dyes, and polycyclic aromatic hydrocarbons, are phenol oxidase laccase (EC 1.10.3.2) and three heme peroxidases: lignin peroxidase (LiP, EC 1.11.1.14), which catalyze the oxidative cleavage of carbon-carbon bonds and ether bonds (C-O-C) in non-phenolic aromatic substrates of high redox potential, and the manganese peroxidase (MnP, EC 1.11.1.13), which requires Mn2+ to complete its catalytic cycle and forms Mn3+ -chelates, acting as diffusing oxidizers, and also versatile peroxidase (VP, EC 1.11.1.16) that has both previous activities and is present in Pleurotus and Bjerkandera fungal species, and in some other fungi such as Lepista irina and Panus tigrinus. Evolutionary and phylogenetic analysis Bjerkandera adusta
additional information versatile peroxidase three-dimensional structure modeling, overview. The active site residues are Arg70, His74, and Asn111 Bjerkandera adusta
physiological function versatile peroxidases can directly attack lignin, cellulose, and hemicellulose in the plant cell wall to decompose it Bjerkandera adusta