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evolution
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DNA sequence comparisons and phylogenetic analysis and tree
evolution
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DNA sequence comparisons and phylogenetic analysis and tree
evolution
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DNA sequence comparisons and phylogenetic analysis and tree
evolution
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DNA sequence comparisons and phylogenetic analysis and tree
evolution
maganese peroxidases (MnPs) can be divided into groups of short, long, and extra-long MnPs. The length of long MnPs is 348-361 amino acids, extra-long MnPs are longer than 362 amino acids, and short MnPs are no longer than 348 amino acids. The long and extralong MnPs are characterized by a C-terminal tail that surrounds the main heme access channel, preventing oxidation of low-redox-potential substrates (e.g. ABTS, 2,6-DMP). MrMnP1 is 343 amino acids long and can be categorized as a short MnP
evolution
MGMnPs may have evolved to adapt to chloride-rich environments, e.g. mangrove forests
evolution
MnP124076 is the only short MnP found in Ceriporiopsis subvermispora, MnP157986 is an extralong MnP and has the longest amino acid sequence. MnP50297 and MnP117436 are an extralong MnP and a long MnP, respectively, and they are the most abundantly produced MnPs in each subfamily by Ceriporiopsis subvermispora grown in aspen wood-containing medium
evolution
the enzyme belongs to the class II fungal peroxidases (PODs)
evolution
the enzyme belongs to the ligninolytic peroxidase gene family, 13 MnP genes and five dye-decolorizing peroxidase (DyP) genes are present in the Irpex lacteus strain F17 genome, they represent two different families of heme peroxidases and are unrelated to the fungal class II peroxidases
evolution
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the enzyme belongs to the ligninolytic peroxidase gene family, 13 MnP genes and five dye-decolorizing peroxidase (DyP) genes are present in the Irpex lacteus strain F17 genome, they represent two different families of heme peroxidases and are unrelated to the fungal class II peroxidases
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evolution
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the enzyme belongs to the class II fungal peroxidases (PODs)
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evolution
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maganese peroxidases (MnPs) can be divided into groups of short, long, and extra-long MnPs. The length of long MnPs is 348-361 amino acids, extra-long MnPs are longer than 362 amino acids, and short MnPs are no longer than 348 amino acids. The long and extralong MnPs are characterized by a C-terminal tail that surrounds the main heme access channel, preventing oxidation of low-redox-potential substrates (e.g. ABTS, 2,6-DMP). MrMnP1 is 343 amino acids long and can be categorized as a short MnP
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evolution
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MnP124076 is the only short MnP found in Ceriporiopsis subvermispora, MnP157986 is an extralong MnP and has the longest amino acid sequence. MnP50297 and MnP117436 are an extralong MnP and a long MnP, respectively, and they are the most abundantly produced MnPs in each subfamily by Ceriporiopsis subvermispora grown in aspen wood-containing medium
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evolution
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the enzyme belongs to the class II fungal peroxidases (PODs)
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physiological function
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lignin-degrading enzyme
physiological function
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a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
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a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
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a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
physiological function
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enzyme MnP generates Mn3+ (act as a diffusible charge transfer mediators) which can oxidize a large amount of phenolic substrates such as simple phenols, amines, dyes as well as phenolic lignin model compounds. In contrast to laccase, MnP is not capable of oxidizing the more recalcitrant nonphenolic compounds
physiological function
manganese peroxidase (MnP) is an extracellular glycosylated heme protein produced by various basidiomycetous fungi. It requires hydrogen peroxide as an oxidant to function. In the catalytic cycle of MnP, Mn2+ is oxidized into Mn3+. A complex of Mn3+ and organic acid with low molecular weight is subsequently formed and acts as a diffusible redox-mediator to attack phenolic lignin structures and break the aromatic rings of lignin polymers. The recombinant isozyme MnP3 from Cerrena unicolor strain BBP6 has strong decolorizing activity on a variety of dyes and it is efficient in denim bleaching. It is also able to degrade fluorene and phenanthrene effectively. Due to its broad substrate specificity, MnP is capable of transforming many structurally different pollutants such as synthetic dyes, PAHs and pesticides
physiological function
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manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
physiological function
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manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
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manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
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the crude manganese peroxidase from Bacillus velezensis strain Al-Dhabi 140 shows an optimum degradation process and maximum removal efficacy of 87 mg/l at tetracycline concentration 143.75 mg/l, pH 6.9, and 8.04% inoculum
physiological function
the manganese peroxidase of Irpex lacteus strain 17 is able to degrade recalcitrant aromatic pollutants
physiological function
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manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
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physiological function
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lignin-degrading enzyme
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physiological function
Bacillus velezensis Al-Dhabi 140
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the crude manganese peroxidase from Bacillus velezensis strain Al-Dhabi 140 shows an optimum degradation process and maximum removal efficacy of 87 mg/l at tetracycline concentration 143.75 mg/l, pH 6.9, and 8.04% inoculum
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physiological function
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the manganese peroxidase of Irpex lacteus strain 17 is able to degrade recalcitrant aromatic pollutants
-
physiological function
-
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
-
physiological function
-
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
-
physiological function
-
manganese peroxidase (MnP) is an extracellular glycosylated heme protein produced by various basidiomycetous fungi. It requires hydrogen peroxide as an oxidant to function. In the catalytic cycle of MnP, Mn2+ is oxidized into Mn3+. A complex of Mn3+ and organic acid with low molecular weight is subsequently formed and acts as a diffusible redox-mediator to attack phenolic lignin structures and break the aromatic rings of lignin polymers. The recombinant isozyme MnP3 from Cerrena unicolor strain BBP6 has strong decolorizing activity on a variety of dyes and it is efficient in denim bleaching. It is also able to degrade fluorene and phenanthrene effectively. Due to its broad substrate specificity, MnP is capable of transforming many structurally different pollutants such as synthetic dyes, PAHs and pesticides
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
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additional information
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GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
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GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
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GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
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GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
role of Glu166 in the Mn2+-independent activity
additional information
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role of Glu166 in the Mn2+-independent activity
additional information
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screening and tetracycline degrading efficiency of the five bacteria isolated from the municipal soil sludge, overview. The strain termed Al-Dhabi 140 from Bacillus velezensis shows the highest activity
additional information
the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
additional information
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the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
additional information
Bacillus velezensis Al-Dhabi 140
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screening and tetracycline degrading efficiency of the five bacteria isolated from the municipal soil sludge, overview. The strain termed Al-Dhabi 140 from Bacillus velezensis shows the highest activity
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additional information
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role of Glu166 in the Mn2+-independent activity
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additional information
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the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
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additional information
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role of Glu166 in the Mn2+-independent activity
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