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S168W
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
S168W
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mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
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T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G
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mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
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E166D
site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
E166G
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
E166Q
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
E166D
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site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
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E166G
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site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
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E166Q
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site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
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E166D
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site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
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E166G
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site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
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E166Q
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site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
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A172W
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/A269R
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant does not show altered kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/A273T
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/F259M
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/I171V
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/K168V
site-directed mutagenesis, the mutant shows increased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W
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site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
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A172W/F259M
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site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
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A172W/I171V
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site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
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A172W/K168V
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site-directed mutagenesis, the mutant shows increased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
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A48C/A63C
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A48C and A63C double mutant with an engineered disulfide bond near the distal calcium binding site to restrict the movement of helix B upon loss of calcium and to stabilize against this loss, thermal and pH-stability is improved compared with that of native and recombinant MnP, thermally treated enzyme contains one calcium and retains a percentage of its activity
F190A
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mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
F190I
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mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190L
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rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190Y
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engineered mutant
M273L
mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
N131D
mutant displays a similar catalysis pattern to that of wild-type enzyme, Asn131 is the only potential glycosylation site
N81S
mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
R177A
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mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177D
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mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177E
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mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177K
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mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177N
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mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177Q
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mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R42A
mutant displays a similar catalysis pattern to that of wild-type enzyme, Arg42 is forming the peroxide binding pocket
S168W
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mutant can oxidize both Mn2+ and typical lignin peroxidase substrates such as veratryl alcohol
M237L
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engineered mutant
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M273L
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mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
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M67L
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engineered mutant
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N81S
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mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
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F190A
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mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
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F190I
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mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
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F190L
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rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
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F190Y
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engineered mutant
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R177A
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mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
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R177D
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mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
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R177E
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mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
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R177K
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mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
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R177N
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mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
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additional information
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usage of a fibrous bed reactor to culture of Bacilllus velezensis strain Al-Dhabi 140 on fibrous matrix to transform tetracycline in synthetic wastewater. The transformed product of tetracycline from the fibrous bed reactor is evident by the activity of ligninolytic enzymes produced by Bacillus velezensis strain Al-Dhabi 140 in reactor. Decrease in antibacterial potency by tetracycline degradation is obtained after 10 days. The zone of inhibition is 24 mm at day 1 and 9 mm at day 10
additional information
Bacillus velezensis Al-Dhabi 140
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usage of a fibrous bed reactor to culture of Bacilllus velezensis strain Al-Dhabi 140 on fibrous matrix to transform tetracycline in synthetic wastewater. The transformed product of tetracycline from the fibrous bed reactor is evident by the activity of ligninolytic enzymes produced by Bacillus velezensis strain Al-Dhabi 140 in reactor. Decrease in antibacterial potency by tetracycline degradation is obtained after 10 days. The zone of inhibition is 24 mm at day 1 and 9 mm at day 10
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additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
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four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
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additional information
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
additional information
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both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
additional information
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both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
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additional information
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both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
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additional information
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MnP production from NITW715076_2, NITW715076_1, and NITW715076 isolates
additional information
to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
additional information
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to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
additional information
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to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
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