1.11.1.16: versatile peroxidase
This is an abbreviated version!
For detailed information about versatile peroxidase, go to the full flat file.
Word Map on EC 1.11.1.16
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1.11.1.16
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lignin
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pleurotus
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peroxidases
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ligninolytic
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eryngii
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laccase
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white-rot
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bjerkandera
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ostreatus
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veratryl
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adusta
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chrysosporium
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phanerochaete
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lignin-degrading
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non-phenolic
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2,6-dimethoxyphenol
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delignification
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aryl-alcohols
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degradation
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synthesis
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industry
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analysis
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paper production
- 1.11.1.16
- lignin
- pleurotus
- peroxidases
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ligninolytic
- eryngii
- laccase
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white-rot
- bjerkandera
- ostreatus
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veratryl
- adusta
- chrysosporium
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phanerochaete
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lignin-degrading
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non-phenolic
- 2,6-dimethoxyphenol
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delignification
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aryl-alcohols
- degradation
- synthesis
- industry
- analysis
- paper production
Reaction
Synonyms
B-type dye-decolorizing peroxidase, bacterial lignin peroxidase, DypB, manganese peroxidase 4, Mb peroxidase, metMb peroxidase, Mnp4, More, myoglobin, R1B4, versatile peroxidase, versatile peroxidase MnP2, versatile peroxidase VPL2 precursor, VP1, Vpl2, VPS1
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General Information
General Information on EC 1.11.1.16 - versatile peroxidase
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evolution
malfunction
metabolism
physiological function
additional information
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
evolution
versatile peroxidase (VP) is a lignin-degrading heme-containing oxidoreductase classified as a class II peroxidase, which is secreted by several species of basidiomycetes, mostly from the genera Pleurotus and Bjerkandera
evolution
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versatile peroxidase is regarded as a hybrid of lignin peroxidase and manganese peroxidase. This enzyme possesses the catalytic features of oxidation of aromatic compounds through long-range electron transfer (LRET) and Mn (II) to Mn (III), analogous to the latter peroxidase
evolution
Bjerkandera adusta UAMH8258
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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
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evolution
Lentinus squarrosulus 12292 ITS
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versatile peroxidase is regarded as a hybrid of lignin peroxidase and manganese peroxidase. This enzyme possesses the catalytic features of oxidation of aromatic compounds through long-range electron transfer (LRET) and Mn (II) to Mn (III), analogous to the latter peroxidase
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acetylation of tyrosine residues would inhibit peroxidase activity
malfunction
Tyr103 acetylation significantly reduces the rate of ferrylMb auto-reduction, indicating the role of tyrosine residues as intramolecular substrates
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ligninases, including laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase, are crucial components of the ligninolytic machinery. The white-rot fungi engage collective action of these enzymes in mineralization of the complex macromolecule
metabolism
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versatile peroxidase of the white-rot fungus Lentinus tigrinus is involved in biotransformation of soil humic matter. Alkali-extractable and acid-insoluble constituents of SOM (HA) contain true macromolecular components, stable in the presence of 0.1% sodium dodecyl sulfate but degradable/resynthesizable by oxidative enzymes acting on covalent linkages. The humic acid degradation in the presence of laccase occurs at slower initial rate than in the presence of the enzyme. Each of the enzymes causes about 60% color loss and almost complete degradation of HA into smaller molecules within 2 weeks of cultivation. Depolymerization of HA in the culture liquid in the presence of laccase is accompanied by polymerization of degradation products on mycelium. Humus macromolecules are not stable to oxidative enzymes once desorbed from the mineral phase. Laccase of Lentinus tigrinus is comparable by its degradation potential to VP, and interfacial secondary synthesis reactions occur during humus decay in the presence of laccase. Comparison of versatile peroxidase and laccase activities, detailed overview
metabolism
Lentinus squarrosulus 12292 ITS
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ligninases, including laccase, lignin peroxidase, manganese peroxidase, and versatile peroxidase, are crucial components of the ligninolytic machinery. The white-rot fungi engage collective action of these enzymes in mineralization of the complex macromolecule
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metabolism
Lentinus tigrinus VKM F-160
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versatile peroxidase of the white-rot fungus Lentinus tigrinus is involved in biotransformation of soil humic matter. Alkali-extractable and acid-insoluble constituents of SOM (HA) contain true macromolecular components, stable in the presence of 0.1% sodium dodecyl sulfate but degradable/resynthesizable by oxidative enzymes acting on covalent linkages. The humic acid degradation in the presence of laccase occurs at slower initial rate than in the presence of the enzyme. Each of the enzymes causes about 60% color loss and almost complete degradation of HA into smaller molecules within 2 weeks of cultivation. Depolymerization of HA in the culture liquid in the presence of laccase is accompanied by polymerization of degradation products on mycelium. Humus macromolecules are not stable to oxidative enzymes once desorbed from the mineral phase. Laccase of Lentinus tigrinus is comparable by its degradation potential to VP, and interfacial secondary synthesis reactions occur during humus decay in the presence of laccase. Comparison of versatile peroxidase and laccase activities, detailed overview
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despite the presence of Mn2+ in the medium, a transformant overexpressing the enzyme produces mnp4 transcripts as well as versatile peroxidase activity as early as 4 days after inoculation. The level of expression is constant throughout 10 days of incubation and the activity is comparable to the typical activity in Mn2+-deficient media
physiological function
although their function is most commonly associated with facilitating oxygen storage and diffusion, myoglobin (Mb) has also been implicated in cellular antioxidant defense. The oxidized (Fe3+) form of Mb (metMB) can react with hydrogen peroxide (H2O2) to produce ferrylmyoglobin (ferrylMb). FerrylMb can be reduced back to metMb for another round of reaction with H2O2. Horse skeletal muscle Mb displays peroxidase activity using 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and 3,3',5,5'-tetramethylbenzidine (TMB) as reducing substrates, as well as the biologically-relevant substrates NADH/NADPH, ascorbate, caffeic acid, and resveratrol. FerrylMb can be reduced by both ethanol and acetaldehyde. MetMb reacts with hypochlorite in a heme-dependent fashion, indicating that Mb could play a role in hypochlorite detoxification. Mb peroxidase activity might be an important antioxidant mechanism in vertebrate cardiac and skeletal muscle under a variety of physiological conditions, such as those that might occur in contracting skeletal muscle or during hypoxia
physiological function
although their function is most commonly associated with facilitating oxygen storage and diffusion, myoglobin (Mb) has also been implicated in cellular antioxidant defense. The oxidized (Fe3+) form of Mb (metMB) can react with hydrogen peroxide (H2O2) to produce ferrylmyoglobin (ferrylMb). FerrylMb can be reduced back to metMb for another round of reaction with H2O2. Horse skeletal muscle Mb displays peroxidase activity using 2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) and 3,3',5,5'-tetramethylbenzidine (TMB) as reducing substrates, as well as the biologically-relevant substrates NADH/NADPH, ascorbate, caffeic acid, and resveratrol. FerrylMb can be reduced by both ethanol and acetaldehyde. MetMb reacts with hypochlorite in a heme-dependent fashion, indicating that Mb could play a role in hypochlorite detoxification. Mb peroxidase activity might be an important antioxidant mechanism in vertebrate cardiac and skeletal muscle under a variety of physiological conditions, such as those that might occur in contracting skeletal muscle or during hypoxia
physiological function
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Lentinus squarrosulus is a saprophytic white-rot producing novel versatile peroxidase that is capable of selectively degrading lignin of the crop residues. Treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification
physiological function
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treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification. Screening of wild isolates for a versatile peroxidase having exceptional efficiency for aromatics and manganese oxidation
physiological function
versatile peroxidase (VP) from Pleurotus eryngii is a heme-containing peroxidase with a broad substrate spectrum that can break down many structurally distinct pollutants, including azo dyes. Versatile peroxidase is a hybrid enzyme that combines the catalytic characteristics of MnP (i.e., the ability to oxidase Mn2+ to Mn3+, which when complexed by organic acids can oxidize aromatic compounds, EC 1.11.1.13) with the LiP-like ability (EC 1.11.1.14) to use the long-range electron transfer (LRET) pathway based on surface-exposed catalytic tryptophan for the oxidation of compounds with a higher redox potential. Versatile peroxidase can directly oxidize many high-redox-potential dyes, whereas LiP requires various redox mediators to complete the same reaction. Verstaile peroxidase can also oxidize veratryl alcohol but has a much lower affinity for it as compared to lignin peroxidase (LiP)
physiological function
versatile peroxidase (VP) secreted by white-rot fungi is involved in the degradation of lignin within land ecosystems, with a broad substrate scope and minor requirements
physiological function
versatile peroxidases can directly attack lignin, cellulose, and hemicellulose in the plant cell wall to decompose it
physiological function
Lentinus squarrosulus TAMI004
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treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification. Screening of wild isolates for a versatile peroxidase having exceptional efficiency for aromatics and manganese oxidation
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physiological function
Bjerkandera adusta UAMH8258
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versatile peroxidases can directly attack lignin, cellulose, and hemicellulose in the plant cell wall to decompose it
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physiological function
Lentinus squarrosulus 12292 ITS
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Lentinus squarrosulus is a saprophytic white-rot producing novel versatile peroxidase that is capable of selectively degrading lignin of the crop residues. Treatment of crops with Lentinus squarrosulus rich in versatile peroxidase show a decrease in neutral detergent fiber, and acid detergent lignin contents, promptig delignification
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enzyme VP1 contains a Mn-binding site, a heme binding site and a substrate binding site according to the conserved domain database (CDD). VP1 demonstrates both MnP and LiP structural characterization, including Mn-binding site and an exposed tryptophan residue. The conserved Mn-binding site allows VP to obtain electrons from Mn(II) and oxidize Mn(II) to Mn(III). Three conserved amino acid residues, Glu63, Glu67, and Asp202, comprise the Mn-binding site of both VP and MnP. The chelated Mn(III) ions released from the Mn binding site act as diffusible charge transfer mediators attacking low redox potential phenolic substrates like 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol. According to multiple sequence alignment, the tryptophan residue is conserved in VP1 and other VPs and LiPs, but not in MnPs. Trp191 in VP1 is likely to have a direct oxidation capacity on high redox potential substrates, such as verytryl alcohol and Reactive Black 5 via long-range electron transfer (LRET) to heme. In addition, two conserved residues, His102 and His259, located on the proximal and the distal of heme binding region and conserved in VP and LiP, may also involve in LRET for high redox potential substrates oxidation
additional information
role of tyrosine residues in Mb peroxidase activity
additional information
role of tyrosine residues in Mb peroxidase activity, overview. Residue Y103 is important in orienting certain substrates in the heme pocket
additional information
versatile peroxidase (VP) from Bjerkandera adusta is able to oxidize bulky and high-redox substrates through a long-range electron transfer (LRET) pathway
additional information
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versatile peroxidase (VP) from Bjerkandera adusta is able to oxidize bulky and high-redox substrates through a long-range electron transfer (LRET) pathway
additional information
versatile peroxidase (VP) has an access channel that is open to the solvent and where low-redox potential substrates are oxidized. In addition, VP has a superficial catalytic tryptophan that, in its active state, oxidizes both low-redox and more significantly, high redox potential substrates through a long-range electron transfer pathway to the heme, like lignin peroxidase. In the sagittal plane of the protein structure there is a small heme access channel where Mn2+ is oxidized to Mn3+, the latter acting as a diffusible oxidizer as also occurs in MnP (EC 1.11.1.13)
additional information
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versatile peroxidase is endowed with polyvalent catalytic sites that render this protein with high redox potential
additional information
versatile peroxidase three-dimensional structure modeling, overview. The active site residues are Arg70, His74, and Asn111
additional information
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versatile peroxidase three-dimensional structure modeling, overview. The active site residues are Arg70, His74, and Asn111
additional information
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versatile peroxidase, an extracellular heme protein of the ligninolytic system, is endowed with polyvalent catalytic sites that render this protein with high redox potential
additional information
Lentinus squarrosulus TAMI004
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versatile peroxidase, an extracellular heme protein of the ligninolytic system, is endowed with polyvalent catalytic sites that render this protein with high redox potential
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additional information
Bjerkandera adusta UAMH8258
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versatile peroxidase three-dimensional structure modeling, overview. The active site residues are Arg70, His74, and Asn111
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additional information
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enzyme VP1 contains a Mn-binding site, a heme binding site and a substrate binding site according to the conserved domain database (CDD). VP1 demonstrates both MnP and LiP structural characterization, including Mn-binding site and an exposed tryptophan residue. The conserved Mn-binding site allows VP to obtain electrons from Mn(II) and oxidize Mn(II) to Mn(III). Three conserved amino acid residues, Glu63, Glu67, and Asp202, comprise the Mn-binding site of both VP and MnP. The chelated Mn(III) ions released from the Mn binding site act as diffusible charge transfer mediators attacking low redox potential phenolic substrates like 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol. According to multiple sequence alignment, the tryptophan residue is conserved in VP1 and other VPs and LiPs, but not in MnPs. Trp191 in VP1 is likely to have a direct oxidation capacity on high redox potential substrates, such as verytryl alcohol and Reactive Black 5 via long-range electron transfer (LRET) to heme. In addition, two conserved residues, His102 and His259, located on the proximal and the distal of heme binding region and conserved in VP and LiP, may also involve in LRET for high redox potential substrates oxidation
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additional information
Lentinus squarrosulus 12292 ITS
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versatile peroxidase is endowed with polyvalent catalytic sites that render this protein with high redox potential
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