EC Number   |
General Information |
Reference |
|---|
   1.11.1.16 | 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 |
-, 765635 |
| 1.11.1.16 | 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 |
764602 |
| 1.11.1.16 | evolution |
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 |
-, 764315 |
| 1.11.1.16 | malfunction |
acetylation of tyrosine residues would inhibit peroxidase activity |
764524 |
| 1.11.1.16 | malfunction |
Tyr103 acetylation significantly reduces the rate of ferrylMb auto-reduction, indicating the role of tyrosine residues as intramolecular substrates |
764524 |
| 1.11.1.16 | metabolism |
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 |
-, 764315 |
| 1.11.1.16 | metabolism |
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 |
-, 765179 |
| 1.11.1.16 | more |
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 |
-, 764848 |
| 1.11.1.16 | more |
role of tyrosine residues in Mb peroxidase activity |
764524 |
| 1.11.1.16 | more |
role of tyrosine residues in Mb peroxidase activity, overview. Residue Y103 is important in orienting certain substrates in the heme pocket |
764524 |
