1.11.1.16 1,4-benzohydroquinone + H2O2 - Pleurotus eryngii ? + H2O - ? 380834 1.11.1.16 1,4-dimethoxybenzene + H2O2 Mn2+-independent activity Bjerkandera sp. 1,4-benzoquinone + formaldehyde + H2O - ? 380835 1.11.1.16 1-methylanthracene + H2O2 at 43% of the rate with 9-methylanthracene Bjerkandera adusta 1-methylanthraquinone + H2O - ? 380850 1.11.1.16 1-naphthol + H2O2 - Bjerkandera adusta ? + H2O - ? 375543 1.11.1.16 1-phenyl-1,2-ethandiol + H2O2 substrate of N246A mutant enzyme Rhodococcus jostii ? + 2 H2O - ? 461859 1.11.1.16 1-phenyl-1-propanol + H2O2 substrate of N246A mutant enzyme Rhodococcus jostii ? + 2 H2O - ? 461861 1.11.1.16 1-phenyl-2-propanol + H2O2 substrate of N246A mutant enzyme Rhodococcus jostii ? + 2 H2O - ? 461862 1.11.1.16 1-phenylethanol + H2O2 substrate of N246A mutant enzyme Rhodococcus jostii ? + 2 H2O - ? 461866 1.11.1.16 2 2,6-dimethoxyphenol + 2 H2O2 - Pleurotus eryngii coerulignone + 2 H2O - ? 260326 1.11.1.16 2 2,6-dimethoxyphenol + 2 H2O2 - Bjerkandera fumosa coerulignone + 2 H2O - ? 260326 1.11.1.16 2 2,6-dimethoxyphenol + 2 H2O2 Mn2+-dependent and independent activity Pleurotus eryngii coerulignone + 2 H2O - ? 260326 1.11.1.16 2 2,6-dimethoxyphenol + 2 H2O2 Mn2+-independent activity Bjerkandera sp. coerulignone + 2 H2O - ? 260326 1.11.1.16 2 2,6-dimethoxyphenol + 2 H2O2 Mn2+-independent activity Bjerkandera sp. BOS55 coerulignone + 2 H2O - ? 260326 1.11.1.16 2 2,6-dimethoxyphenol + H2O2 - Bjerkandera sp. coerulignone + 2 H2O - ? 425319 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Lentinus tigrinus 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Physisporinus vitreus 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Pleurotus eryngii 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Bjerkandera adusta 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Lentinus squarrosulus 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 activity of EC 1.11.1.13 Rhodococcus jostii 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 oxidation of Mn2+ to Mn3+ (manganese peroxidase activity) is measured as the H2O2-dependent formation of the complex malonate-Mn3+ Bjerkandera adusta 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Lentinus squarrosulus TAMI004 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Bjerkandera adusta UAMH8258 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Physisporinus vitreus PF18 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Lentinus squarrosulus 12292 ITS 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn(II) + 2 H+ + H2O2 - Lentinus tigrinus VKM F-160 2 Mn(III) + 2 H2O - ? 425344 1.11.1.16 2 Mn2+ + 2 H+ - Bjerkandera fumosa 2 Mn3+ + H2 - ? 425346 1.11.1.16 2 Mn2+ + 2 H+ + H2O2 - Bjerkandera sp. 2 Mn3+ + 2 H2O - ? 425345 1.11.1.16 2 Mn2+ + 2 H+ + H2O2 - Pleurotus eryngii 2 Mn3+ + 2 H2O - ? 425345 1.11.1.16 2 Mn2+ + H2O2 + 2 H+ - Pseudomonas putida 2 Mn3+ + 2 H2O - ? 425347 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2 - Physisporinus vitreus oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O - ? 461911 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2 - Pleurotus eryngii oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O - ? 461911 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2 - Rhodococcus jostii oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O - ? 461911 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2 - Equus caballus oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O - ? 461911 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2 - Mus musculus oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O - ? 461911 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2 - Pleurotus ostreatus ? - ? 440556 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2 - Bjerkandera adusta ? - ? 440556 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2 - Pleurotus eryngii ? - ? 440556 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2 - Bjerkandera fumosa ? - ? 440556 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2 - Pleurotus sapidus ? - ? 440556 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 - Pseudomonas putida ? + H2O - ? 380887 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 - Pleurotus eryngii ? + H2O - ? 380887 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 - Bjerkandera fumosa ? + H2O - ? 380887 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 Mn2+-independent activity Bjerkandera sp. ? + H2O - ? 380887 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 - Pseudomonas putida MET94 ? + H2O - ? 380887 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+ - Pleurotus eryngii ? - ? 413882 1.11.1.16 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+ - Rhodococcus jostii ? + H2O - ? 425353 1.11.1.16 2,6-dimethoxybenzohydroquinone + H2O2 - Pleurotus eryngii ? + H2O - ? 380902 1.11.1.16 2,6-dimethoxyphenol + 2 H+ + H2O2 - Physisporinus vitreus oxidized 2,6-dimethoxyphenol + 2 H2O - ? 461464 1.11.1.16 2,6-dimethoxyphenol + 2 H+ + H2O2 - Rhodococcus jostii oxidized 2,6-dimethoxyphenol + 2 H2O - ? 461464 1.11.1.16 2,6-dimethoxyphenol + 2 H+ + H2O2 - Lentinus squarrosulus oxidized 2,6-dimethoxyphenol + 2 H2O - ? 461464 1.11.1.16 2,6-dimethoxyphenol + 2 H+ + H2O2 substrate 2,6-dimethoxyphenol (DMP) is transformed at the distal site of heme prosthetic group (lignin peroxidase activity) Bjerkandera adusta oxidized 2,6-dimethoxyphenol + 2 H2O - ? 461464 1.11.1.16 2,6-dimethoxyphenol + 2 H+ + H2O2 - Lentinus squarrosulus TAMI004 oxidized 2,6-dimethoxyphenol + 2 H2O - ? 461464 1.11.1.16 2,6-dimethoxyphenol + 2 H+ + H2O2 - Physisporinus vitreus PF18 oxidized 2,6-dimethoxyphenol + 2 H2O - ? 461464 1.11.1.16 2,6-dimethoxyphenol + H+ + H2O2 - Pleurotus ostreatus ? - ? 440612 1.11.1.16 2,6-dimethoxyphenol + H+ + H2O2 - Bjerkandera adusta ? - ? 440612 1.11.1.16 2,6-dimethoxyphenol + H+ + H2O2 - Pleurotus eryngii ? - ? 440612 1.11.1.16 2,6-dimethoxyphenol + H+ + H2O2 - Bjerkandera fumosa ? - ? 440612 1.11.1.16 2,6-dimethoxyphenol + H2O2 - Pleurotus ostreatus ? - ? 375648 1.11.1.16 2,7-diaminofluorene + H2O2 during oxidation of 2,7-diaminofluorene, both with and without Mn2+, biphasic kinetics with apparent saturation in both micromolar and millimolar ranges are obtained Bjerkandera fumosa ? + H2O - ? 425386 1.11.1.16 2-chloro-1,4-dimethoxybenzene + H2O2 Mn2+-independent activity Bjerkandera sp. 2-chloro-1,4-benzoquinone + H2O - ? 380982 1.11.1.16 2-methoxy-1,4-benzohydroquinone + H2O2 - Pleurotus eryngii ? + H2O - ? 381008 1.11.1.16 2-methylanthracene + H2O2 at 24% of the rate with 9-methylanthracene Bjerkandera adusta 2-methylanthraquinone + H2O - ? 381009 1.11.1.16 3,3',5,5'-tetramethylbenzidine + 2 H+ + H2O2 - Equus caballus ? + 2 H2O - ? 462007 1.11.1.16 3,3',5,5'-tetramethylbenzidine + 2 H+ + H2O2 - Mus musculus ? + 2 H2O - ? 462007 1.11.1.16 3-hydroxyanthranilic acid + H2O2 Mn2+-independent activity Bjerkandera sp. ? + H2O - ? 381094 1.11.1.16 3-methyl-2-benzothiazolinone hydrazone + H2O2 enzyme has several substrate binding sites for 3-methyl-2-benzothiazolinone hydrazone, in addition to low and high affinity binding sites for Mn2+ Bjerkandera adusta ? + H2O - ? 425576 1.11.1.16 4-aminobenzoic acid + H2O2 - Bjerkandera fumosa ? + H2O - ? 425617 1.11.1.16 4-hydroquinone + H2O2 - Pleurotus eryngii 4-benzoquinone + H2O - ? 425643 1.11.1.16 9-methylanthracene + H2O2 - Bjerkandera adusta 10-methylanthracene-9-one + H2O - ? 381282 1.11.1.16 acetosyringone + H2O2 + H+ - Pseudomonas putida oxidized acetosyringone + H2O - ? 425871 1.11.1.16 Acid Blue 62 + H2O2 + H+ - Pseudomonas putida oxidized Acid Blue 62 + H2O - ? 425887 1.11.1.16 amaranth + H2O2 - Pleurotus ostreatus ? + H2O - ? 425920 1.11.1.16 anthracene + H2O2 at 4.8% of the rate with 9-methylanthracene Bjerkandera adusta anthraquinone + H2O - ? 381424 1.11.1.16 anthracene + H2O2 - Bjerkandera fumosa 9,10-anthraquinone + H2O - ? 425930 1.11.1.16 Azure B + 2 H+ + H2O2 dye decolorization, substrate of N246A mutant enzyme Rhodococcus jostii oxidized Azure B + 2 H2O - ? 462284 1.11.1.16 beta-carotene + H+ + H2O2 - Pleurotus sapidus ? - ? 441129 1.11.1.16 bovine pancreatic RNase no redox mediators involved Pleurotus ostreatus oxidized bovine pancreatic RNase - ? 381599 1.11.1.16 carbazole + H2O2 at 4.8% of the rate with 9-methylanthracene Bjerkandera adusta ? + H2O - ? 381614 1.11.1.16 catechol + H2O2 - Pleurotus eryngii 2-benzoquinone + H2O - ? 426071 1.11.1.16 chrysene + H2O2 - Bjerkandera fumosa ? + H2O - ? 426104 1.11.1.16 fluoranthene + H2O2 - Bjerkandera fumosa ? + H2O - ? 426403 1.11.1.16 fluorene + H2O2 - Bjerkandera fumosa 9-fluorenone + H2O - ? 426404 1.11.1.16 fulvic acid + H2O2 - Bjerkandera adusta ? + H2O - ? 441404 1.11.1.16 guaiacol + H2O2 - Pleurotus eryngii ? + H2O - ? 373352 1.11.1.16 guaiacol + H2O2 Mn2+-independent activity Bjerkandera sp. ? + H2O - ? 373352 1.11.1.16 guaiacol + H2O2 - Pleurotus eryngii 3,3'-dimethoxy-4,4'-biphenylquinone + H2O - ? 426468 1.11.1.16 guaiacol + H2O2 - Pleurotus eryngii oxidized guaiacol + 2 H2O - ? 462554 1.11.1.16 guaiacol + H2O2 + H+ - Pseudomonas putida oxidized guaiacol + H2O - ? 414675 1.11.1.16 guaiacol + H2O2 + H+ - Pseudomonas putida MET94 oxidized guaiacol + H2O - ? 414675 1.11.1.16 guaiacylglycerol-beta-guaiacyl ether + H2O2 GGE, substrate of mutant enzyme N246A Rhodococcus jostii glycerol + guaiacol + 2 H2O - ? 462558 1.11.1.16 humic acid + H2O2 - Bjerkandera adusta ? + H2O - ? 426488 1.11.1.16 indigo carmine + 2 H+ + H2O2 dye decolorization Physisporinus vitreus oxidized indigo carmine + 2 H2O - ? 462602 1.11.1.16 lignin + H2O2 lignin fraction from straw pulpin, versatile peroxidase reacts with soluble lignin fragments in the absence of added mediators, most probably causing extensive polymerisation of high and intermediate fractions of lignin, and an increase of the small-molecular-mass lignin fraction Bjerkandera sp. ? + H2O - ? 397695 1.11.1.16 lignin + H2O2 substrate Kraft lignin. The highest production of radicals with minimal loss of activity, is obtained by using an enzyme dose of 15 U/g, with a continuous addition of H2O2 during 1 h. Enzymatically generated Mn(III)-malonate is able to activate lignin Bjerkandera sp. ? + H2O - ? 397695 1.11.1.16 lignin + H2O2 substrate Kraft lignin. The highest production of radicals with minimal loss of activity, is obtained by using an enzyme dose of 15 U/g, with a continuous addition of H2O2 during 1 h. Enzymatically generated Mn(III)-malonate is able to activate lignin Bjerkandera sp. R1 ? + H2O - ? 397695 1.11.1.16 manganese(II)-substituted polyoxometalate + H2O2 - Pleurotus eryngii manganese(III)-substituted polyoxometalate + H2O2 - ? 414831 1.11.1.16 methoxyhydroquinone + H2O2 - Pleurotus eryngii ? + H2O - ? 382296 1.11.1.16 methyl green + 2 H+ + H2O2 dye decolorization Physisporinus vitreus oxidized methyl green + 2 H2O - ? 462704 1.11.1.16 methylene blue + H2O2 - Bjerkandera adusta ? + H2O - ? 426674 1.11.1.16 Mn2+ + H+ + H2O2 - Pleurotus ostreatus Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H+ + H2O2 - Bjerkandera adusta Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H+ + H2O2 - Pleurotus eryngii Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H+ + H2O2 - Bjerkandera sp. Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H+ + H2O2 - Bjerkandera fumosa Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H+ + H2O2 - Cerrena consors Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H+ + H2O2 - Bjerkandera adusta ATCC 90940 Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H+ + H2O2 - Pleurotus ostreatus PC9 Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H+ + H2O2 - Bjerkandera sp. R1 Mn3+ + H2O - ? 289095 1.11.1.16 Mn2+ + H2O2 - Pleurotus ostreatus Mn3+ + H2O - ? 377173 1.11.1.16 Mn2+ + H2O2 - Pleurotus eryngii Mn3+ + H2O - ? 377173 1.11.1.16 Mn2+ + H2O2 - Bjerkandera sp. Mn3+ + H2O - ? 377173 1.11.1.16 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 - ? 377173 1.11.1.16 Mn2+ + H2O2 - Pleurotus eryngii ? - ? 389178 1.11.1.16 Mn2+ + H2O2 + 2,6-dimethoxyphenol - Stereum ostrea ? - ? 426681 1.11.1.16 Mn2+ + H2O2 + guaiacol - Stereum ostrea ? - ? 426682 1.11.1.16 Mn2+ + H2O2 + phenol red - Stereum ostrea ? - ? 426683 1.11.1.16 Mn2+ + H2O2 + Reactive Black 5 - Pleurotus eryngii ? - ? 441643 1.11.1.16 Mn2+ + H2O2 + remazol black-5 incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l Stereum ostrea ? - ? 426684 1.11.1.16 Mn2+ + H2O2 + remazol blue-19 incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l Stereum ostrea ? - ? 426685 1.11.1.16 Mn2+ + H2O2 + remazol brilliant violet incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l Stereum ostrea ? - ? 426686 1.11.1.16 Mn2+ + H2O2 + remazol orange-16 incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l Stereum ostrea ? - ? 426687 1.11.1.16 Mn2+ + H2O2 + rose bengal incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l Stereum ostrea ? - ? 426688 1.11.1.16 Mn2+ + H2O2 + veratryl alcohol - Stereum ostrea ? - ? 426689 1.11.1.16 Mordant Black 9 + H2O2 + H+ - Pseudomonas putida oxidized Mordant Black 9 + H2O - ? 426693 1.11.1.16 additional information substrate specificity analysis, overview Equus caballus ? - - 89 1.11.1.16 additional information substrate specificity analysis, overview Mus musculus ? - - 89 1.11.1.16 additional information in the absence of Mn2+, efficient hydroquinone oxidation is dependent on exogenous H2O2. In the presence of Mn2+, exogenous H2O2 is not required for complete oxidation of hydroquinones Pleurotus eryngii ? - ? 89 1.11.1.16 additional information enzyme is able to decolorize 27 out of 41 industrial dyes tested Bjerkandera adusta ? - ? 89 1.11.1.16 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 ? - ? 89 1.11.1.16 additional information enzyme is able to oxidize efficiently Mn2+ and phenolic and nonphenolic compounds in absence of this ion Bjerkandera sp. ? - ? 89 1.11.1.16 additional information in presence of H2O2 and Mn2+, a cell-free supernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2 Phanerodontia chrysosporium ? - ? 89 1.11.1.16 additional information manganese peroxidase activity is more efficient than lignin peroxidase activity, with activity increasing with increasing concentrations of Mn2+ due to a second metal binding site involved in homotropic substrate Mn2+ activation. The activation of maganese peroxidase is also accompanied by a decrease in both activation energy and substrate Mn2+ affinity Bjerkandera adusta ? - ? 89 1.11.1.16 additional information no substrates: Fe2+, veratryl alcohol Pseudomonas putida ? - ? 89 1.11.1.16 additional information oxidation of substrates may occur in two ways, either directly by the enzyme or by diffusible chelated Mn3+ as an oxidizing agent Bjerkandera fumosa ? - ? 89 1.11.1.16 additional information presence of two independent catalytic sites for different phenols and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in native enzyme, characterizedby high and low specificity constants, i.e. Km in the micromolar range and Km in the millimolar range, respcetively Pleurotus eryngii ? - ? 89 1.11.1.16 additional information no activity with Phenol Red and Remazol Brilliant Blue Pleurotus sapidus ? - ? 89 1.11.1.16 additional information ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds Bjerkandera adusta ? - - 89 1.11.1.16 additional information highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase Physisporinus vitreus ? - - 89 1.11.1.16 additional information humic acid degradation by versatile peroxidase and laccase using sod-podzolic soil, representative of the southern taiga region, decolorization of humic acids, overview. The soil sample is taken from the birch forest plot of forest experimental dacha of Russian state Agrarian University-Moscow Timiryazev agricultural academy (Moscow, Russia, N55°49008.4', E37°32042') Lentinus tigrinus ? - - 89 1.11.1.16 additional information versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase Lentinus squarrosulus ? - - 89 1.11.1.16 additional information enzyme DypB degrades solvent-obtained fractions of a Kraft lignin. The recombinant mutant enzyme Rh_DypB shows a classical peroxidase activity which is significantly increased by adding Mn2+ ions, kinetic parameters for H2O2, Mn2+, ABTS, and 2,6-DMP are determined. The enzyme shows broad dye-decolorization activity, especially in the presence of Mn2+, oxidizes various aromatic monomers from lignin, and cleaves the guaiacylglycerol-beta-guaiacyl ether (GGE), i.e., the Calpha-Cbeta bond of the dimeric lignin model molecule of beta-O-4 linkages. Under optimized conditions, 2 mM GGE is fully cleaved by recombinant Rh_DypB, generating guaiacol in only 10 min, at a rate of 12.5 micromol/min/mg enzyme. Screening of oxidation activity on monomeric lignin model compounds, overview Rhodococcus jostii ? - - 89 1.11.1.16 additional information Fourier transform infrared (FTIR) analysis to assess the decolorization of Reactive Black 5 and kraft lignin by immobilized Lentinus squarrosulus in optimized production medium containing 0.01% RB5 and 0.02% kraft lignin Lentinus squarrosulus ? - - 89 1.11.1.16 additional information the enzyme performs decolorization of azo dyes. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. Pyrolysis-GC/MS analysis of lignin modified products, detailed overview Physisporinus vitreus ? - - 89 1.11.1.16 additional information the enzyme shows a broad substrate spectrum Pleurotus eryngii ? - - 89 1.11.1.16 additional information the oxidation of 2,6-dimethylphenol, Mn2+ and remazol brilliant blue R (RBBR) of the three different substrates occurs at different active sites of the enzyme molecule. Versatile peroxidase (VP) from Bjerkandera adusta is an enzyme able to oxidize bulky and high-redox substrates trough a long-range electron t (LRET) pathway. The catalytic rate of the LRET mediated transformation shows a good correlation with the ionization energy of the additional amino acid on the protein surface Bjerkandera adusta ? - - 89 1.11.1.16 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 ? - - 89 1.11.1.16 additional information no substrates: Fe2+, veratryl alcohol Pseudomonas putida MET94 ? - ? 89 1.11.1.16 additional information versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase Lentinus squarrosulus TAMI004 ? - - 89 1.11.1.16 additional information ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds Bjerkandera adusta UAMH8258 ? - - 89 1.11.1.16 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 ? - - 89 1.11.1.16 additional information highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase Physisporinus vitreus PF18 ? - - 89 1.11.1.16 additional information the enzyme performs decolorization of azo dyes. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. Pyrolysis-GC/MS analysis of lignin modified products, detailed overview Physisporinus vitreus PF18 ? - - 89 1.11.1.16 additional information Fourier transform infrared (FTIR) analysis to assess the decolorization of Reactive Black 5 and kraft lignin by immobilized Lentinus squarrosulus in optimized production medium containing 0.01% RB5 and 0.02% kraft lignin Lentinus squarrosulus 12292 ITS ? - - 89 1.11.1.16 additional information in presence of H2O2 and Mn2+, a cell-free supernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2 Phanerodontia chrysosporium BKM-F-1767 ? - ? 89 1.11.1.16 additional information humic acid degradation by versatile peroxidase and laccase using sod-podzolic soil, representative of the southern taiga region, decolorization of humic acids, overview. The soil sample is taken from the birch forest plot of forest experimental dacha of Russian state Agrarian University-Moscow Timiryazev agricultural academy (Moscow, Russia, N55°49008.4', E37°32042') Lentinus tigrinus VKM F-160 ? - - 89 1.11.1.16 NADH + H2O2 - Pleurotus eryngii NAD+ + H2O - ? 260333 1.11.1.16 o-anisidine + H2O2 Mn2+-independent activity Bjerkandera sp. ? + H2O - ? 382433 1.11.1.16 Orange II + H+ + H2O2 - Pleurotus ostreatus ? - ? 441810 1.11.1.16 Orange II + H+ + H2O2 - Pleurotus ostreatus PC9 ? - ? 441810 1.11.1.16 Orange II + H2O2 - Pleurotus ostreatus ? + H2O - ? 426880 1.11.1.16 p-anisidine + H2O2 Mn2+-independent activity Bjerkandera sp. ? + H2O - ? 382451 1.11.1.16 p-dimethoxybenzene + H2O2 catalyzed by isoforms PS3, PS1 Pleurotus eryngii benzoquinone + H2O - ? 382454 1.11.1.16 phenanthrene + H2O2 - Bjerkandera fumosa 9,10-phenanthrenequinone + H2O - ? 426914 1.11.1.16 Phenol Red + H+ + H2O2 - Pleurotus ostreatus ? - ? 441864 1.11.1.16 Phenol Red + H+ + H2O2 - Pleurotus ostreatus PC9 ? - ? 441864 1.11.1.16 phenol red + H2O2 Mn2+-dependent activity Pleurotus eryngii oxidized phenol red + H2O - ? 382544 1.11.1.16 Poly R-478 no redox mediators involved Pleurotus ostreatus oxidized Poly R-478 - ? 382588 1.11.1.16 Poly R-478 + H2O2 decolorization of the dye Pleurotus ostreatus ? - ? 398133 1.11.1.16 pyrene + H2O2 - Bjerkandera fumosa ? + H2O - ? 426968 1.11.1.16 Reactive Black 5 + 2 H+ + H2O2 - Pleurotus eryngii oxidized Reactive Black 5 + 2 H2O - ? 461676 1.11.1.16 Reactive Black 5 + 2 H+ + H2O2 - Lentinus squarrosulus oxidized Reactive Black 5 + 2 H2O - ? 461676 1.11.1.16 Reactive Black 5 + 2 H+ + H2O2 dye decolorization Physisporinus vitreus oxidized Reactive Black 5 + 2 H2O - ? 461676 1.11.1.16 Reactive Black 5 + 2 H+ + H2O2 dye decolorization, substrate of N246A mutant enzyme Rhodococcus jostii oxidized Reactive Black 5 + 2 H2O - ? 461676 1.11.1.16 Reactive Black 5 + 2 H+ + H2O2 - Lentinus squarrosulus TAMI004 oxidized Reactive Black 5 + 2 H2O - ? 461676 1.11.1.16 Reactive Black 5 + 2 H+ + H2O2 dye decolorization Physisporinus vitreus PF18 oxidized Reactive Black 5 + 2 H2O - ? 461676 1.11.1.16 Reactive Black 5 + 2 H+ + H2O2 - Lentinus squarrosulus 12292 ITS oxidized Reactive Black 5 + 2 H2O - ? 461676 1.11.1.16 Reactive Black 5 + H+ + H2O2 - Pleurotus ostreatus ? - ? 441915 1.11.1.16 Reactive Black 5 + H+ + H2O2 - Bjerkandera adusta ? - ? 441915 1.11.1.16 Reactive Black 5 + H+ + H2O2 - Pleurotus eryngii ? - ? 441915 1.11.1.16 Reactive Black 5 + H+ + H2O2 - Bjerkandera fumosa ? - ? 441915 1.11.1.16 Reactive Black 5 + H+ + H2O2 - Pleurotus ostreatus PC9 ? - ? 441915 1.11.1.16 Reactive Black 5 + H2O2 - Pleurotus eryngii oxidized Reactive Black 5 + H2O - ? 382712 1.11.1.16 Reactive Black 5 + H2O2 catalyzed by isoform PS1 Pleurotus eryngii oxidized Reactive Black 5 + H2O - ? 382712 1.11.1.16 Reactive Black 5 + H2O2 - Pleurotus eryngii ? - ? 389644 1.11.1.16 Reactive Black 5 + H2O2 versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation Pleurotus eryngii ? - ? 389644 1.11.1.16 Reactive Black 5 + H2O2 - Bjerkandera adusta ? + H2O - ? 398245 1.11.1.16 Reactive Black 5 + H2O2 - Pleurotus ostreatus ? + H2O - ? 398245 1.11.1.16 Reactive Blue 38 + H2O2 - Bjerkandera adusta ? + H2O - ? 398246 1.11.1.16 Reactive Blue 5 + H2O2 + H+ - Pseudomonas putida oxidized Reactive Blue 5 + H2O - ? 415189 1.11.1.16 Reactive Blue 5 + H2O2 + H+ - Pseudomonas putida MET94 oxidized Reactive Blue 5 + H2O - ? 415189 1.11.1.16 Reactive Blue 72 + H2O2 - Bjerkandera adusta ? + H2O - ? 398247 1.11.1.16 Reactive Violet 5 + H2O2 - Bjerkandera adusta ? + H2O - ? 398248 1.11.1.16 Remazol brilliant blue R + 2 H+ + H2O2 dye decolorization Physisporinus vitreus oxidized Remazol brilliant blue R + 2 H2O - ? 462995 1.11.1.16 remazol brilliant blue R + H2O2 transformation of the bulky substrate remazol brilliant blue R (RBBR), is monitored at its maximum visible absorbance wavelength of 590 nm Bjerkandera adusta ? + 2 H2O - ? 462996 1.11.1.16 remazol brilliant blue R + H2O2 substrate of N246A mutant enzyme Rhodococcus jostii oxidized remazol brilliant blue R + 2 H2O - ? 462997 1.11.1.16 RNase A + H2O2 - Pleurotus ostreatus ? - ? 389658 1.11.1.16 sinapic acid + H2O2 - Pleurotus eryngii ? + 2 H2O - ? 463029 1.11.1.16 syringaldazine + H2O2 - Bjerkandera fumosa ? - ? 427097 1.11.1.16 syringaldehyde + H2O2 + H+ - Pseudomonas putida oxidized syringaldehyde + H2O - ? 415349 1.11.1.16 syringaldehyde + H2O2 + H+ - Pseudomonas putida MET94 oxidized syringaldehyde + H2O - ? 415349 1.11.1.16 syringol + H+ + H2O2 - Pleurotus sapidus ? - ? 442012 1.11.1.16 syringol + H2O2 - Pleurotus eryngii ? + H2O - ? 382861 1.11.1.16 vanillylidenacetone + H2O2 Mn2+-dependent activity Pleurotus eryngii ? + H2O - ? 382952 1.11.1.16 veratryl alcohol + H+ + H2O2 - Pleurotus sapidus veratraldehyde + H2O - ? 442067 1.11.1.16 veratryl alcohol + H2O2 - Pleurotus eryngii verytryl aldehyde + 2 H2O - ? 461717 1.11.1.16 veratryl alcohol + H2O2 - Lentinus squarrosulus verytryl aldehyde + 2 H2O - ? 461717 1.11.1.16 veratryl alcohol + H2O2 - Lentinus squarrosulus TAMI004 verytryl aldehyde + 2 H2O - ? 461717 1.11.1.16 veratryl alcohol + H2O2 - Pleurotus eryngii 3,4-dimethoxybenzoic acid + 2 H2O - ? 463090 1.11.1.16 veratryl alcohol + H2O2 substrate of N246A mutant enzyme Rhodococcus jostii 3,4-dimethoxybenzoic acid + 2 H2O - ? 463090 1.11.1.16 veratryl alcohol + H2O2 + H+ - Pleurotus ostreatus veratraldehyde + H2O - ? 382957 1.11.1.16 veratryl alcohol + H2O2 + H+ - Pleurotus eryngii veratraldehyde + H2O - ? 382957 1.11.1.16 veratryl alcohol + H2O2 + H+ - Bjerkandera sp. veratraldehyde + H2O - ? 382957 1.11.1.16 veratryl alcohol + H2O2 + H+ - Bjerkandera adusta veratraldehyde + H2O - ? 382957 1.11.1.16 veratryl alcohol + H2O2 + H+ - Bjerkandera fumosa veratraldehyde + H2O - ? 382957 1.11.1.16 veratryl alcohol + H2O2 + H+ catalyzed by isoforms PS2, PS1 Pleurotus eryngii veratraldehyde + H2O - ? 382957 1.11.1.16 veratryl alcohol + H2O2 + H+ Mn2+-independent activity Pleurotus eryngii veratraldehyde + H2O - ? 382957 1.11.1.16 veratryl alcohol + H2O2 + H+ Mn2+-independent activity Bjerkandera sp. veratraldehyde + H2O - ? 382957 1.11.1.16 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 - ? 382957