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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Crystallization
Crystallization on EC 1.11.1.16 - versatile peroxidase
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construction of enzyme model and identification of active sites for oxidation of Mn2+ and of aromatic substrates
hanging drop vapor diffusion method, crystal structures of untreated versatile peroxidase (immediately after expression in Escherichia coli and in vitro reconstitution), native versatile peroxidase (treated with Mn2+), D175A variant, and wild-type verstile peroxidase (from Pleurotus eryngii culture)
mutant enzyme W164Y, sitting-drop vapor diffusion method, resolution 1.94 A
mutants E140G, P141G, K176G, and E140G/K176G, to 1.6, 2.0, 1.5, 1.7 and 2.35 A resolution, respectively
sitting drop vapor diffusion method, using 0.1 M sodium MES buffer at pH 6.5, 25% (w/v) PEG 4000 and 0.2 M MgCl2
resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the five-coordinated quantum mechanically mixed-spin state being the most populated in the latter. The spin population is sensitively dependent on the pH, temperature, and physical, i.e., solution versus crystal versus immobilized, state of the enzymes. The redox potential for the Fe2+/Fe3+ couple is -260 mV
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structural changes in the mutants D153H, D153A, R244L, N246H, N246A, D153A/N246A are confined to the distal heme environment