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
-
ligninolytic
- eryngii
- laccase
-
white-rot
- bjerkandera
- ostreatus
-
veratryl
- adusta
- chrysosporium
-
phanerochaete
-
lignin-degrading
-
non-phenolic
- 2,6-dimethoxyphenol
-
delignification
-
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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Metals Ions
Metals Ions on EC 1.11.1.16 - versatile peroxidase
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Ca2+
Cu2+
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though copper is not directly involved in the activity of versatile peroxidase, copper is an activator for multiple catabolic enzymes such as lytic polysaccharide monooxygenases (LPMO) and glyoxal oxidases that are indirectly involved with versatile peroxidase activity
Fe2+
Manganese
Mn2+
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required, Ca2+-depleted enzyme is able to form the active intermediate compound I but its long range electron transfer has been disrupted
Ca2+
required, binding structure, three-dimensional modeling, overview
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oxidation of Mn(II) to Mn(III), presence of manganese in the reaction mixture with industrial dyes does not enhance the decoloration rate
Manganese
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Km value 0.022 for wild-type, 0.021 for mutant W170A, 0.022 for mutant R263N, 0.026 for mutant Q266F, 0.027 for mutant V166/168L
Mn2+
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activity of manganese peroxidase progressively increases with concentration of Mn2+ to a maximum at about 1.8 mM, with a corresponding decrease in lignin peroxidase activity to less than 10%
Mn2+
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Mn(II) can promote the oxidation of low redox potential substrates and increase decolorization efficiency up to 70% for the recombinant enzyme VP1 (rVP1), binding site structure analysis
Mn2+
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isoenzyme Pl, putative Mn-interaction site near E35, E39, D175. Isoenzyme Ps1, putative Mn-interaction site near E36, E40, D181