1.11.1.19: dye decolorizing peroxidase
This is an abbreviated version!
For detailed information about dye decolorizing peroxidase, go to the full flat file.
Word Map on EC 1.11.1.19
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1.11.1.19
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peroxidases
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heme
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lignin
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auricula-judae
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thanatephorus
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cucumeris
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veratryl
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auricularia
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irpex
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ligninolytic
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lacteus
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lignin-degrading
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kraft
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adusta
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bjerkandera
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chlorite
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nonphenolic
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2,6-dimethoxyphenol
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sapidus
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lignin-derived
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paper production
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degradation
- 1.11.1.19
- peroxidases
- heme
- lignin
- auricula-judae
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thanatephorus
- cucumeris
-
veratryl
-
auricularia
- irpex
-
ligninolytic
- lacteus
-
lignin-degrading
-
kraft
- adusta
- bjerkandera
- chlorite
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nonphenolic
- 2,6-dimethoxyphenol
- sapidus
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lignin-derived
- paper production
- degradation
Reaction
Synonyms
AnaPX, AncDyPD-b1, DtpA, dye decolorizing peroxidases type B, dye-decolorizing peroxidase, DyP, DyP I, DyP II, DyP-I, DyP-type peroxidase, DyP-V, DyP1, DyP1B, DyP2, DyP3, DyP4, DyPA, EfeB, LiP BA45, LiP-SN, manganese-independent peroxidase I, manganese-independent peroxidase II, MnP BA30, POX, reactiveblue-5: hydrogen-peroxide oxidoreductase, TT1485, tyrA, YcdB, YfeX, YRW2 Mb, YwbN
ECTree
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Crystallization
Crystallization on EC 1.11.1.19 - dye decolorizing peroxidase
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hanging drop vapor diffusion method, using 32.5% (w/v) PEG 4000 as precipitant
to 2.1 A resolution. At the distal side of the heme molecule, flexible aspartate residue Asp168 plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterward, its side chain changes its conformation, now pointing toward the protein backbone. A transient radical on the surface-exposed residue Tyr337 is the oxidation site for bulky substrates
HEPES-bound enzyme, sitting drop vapor diffusion method, using 25% (v/v) 2-methyl-2,4-pentanediol, 50 mM HEPES, pH 7.0
resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the six-coordinated low-spin state being the most populated. The poor catalytic activity of BsDyP is ascribed to the presence of a catalytically incompetent six-coordinated low-spin population. 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 -40 mV at pH 7.6, which is substantially more positive than those reported for the majority of other peroxidases
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sitting drop vapor diffusion method, using 1.6-1.95 M ammonium sulfate and 0.1 M MES or 0.1 M citrate buffer pH 6.5
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structures of native enzyme, the D171N mutant, the native enzyme complexed with cyanide, and the D171N mutant associated with cyanide, to 1.4 A, 1.42 A, 1.45 and 1.4 A resolution, respectively. Structures contain four amino acids forming the binding pocket for hydrogen peroxide, and they are remarkably conserved in this family. The structures show that OD2 of Asp171 accepts a proton from hydrogen peroxide in compound I formation, and that OD2 can swing to the appropriate position in response to the ligand for heme iron
sitting drop vapor diffusion method, using 20% (w/v) PEG300, 0.1 M Tris buffer pH 8.5, 5% PEG8000 and 10% (v/v) glycerol
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enzyme in the absence of substrate as well as in the presence of potassium cyanide and veratryl alcohol, hanging drop vapor diffusion method, using 2.4 M sodium malonate pH 7.0
in complex with heme, hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 20% (w/v) PEG3350 and 0.1 M Bis-Tris pH 5.5
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sitting drop vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate and 34% (w/v) PEG 4000
TyrA in complex with iron protoporphyrin (IX), hanging drop vapor diffusion method, using 0.1 M Tris pH 8.0, 5% (v/v) 2-propanol, 20% (w/v) polyethylene glycol 4000, and 1 mM hemin
batch method, using 0.89 M ammonium sulfate, 0.92 M sodium chloride, at 10°C
deglycosylated DyP is crystallized by the batch method, using 0.92 M NaCl and 0.89 M ammonium sulfate as precipitant
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deglycosylated DyP is crystallized by the sitting drop vapor diffusion method, using 25.3% (w/v) PEG 8000 at 5.5 K (pH 6.2)
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sitting drop vapor diffusion method, using 0.2 M potassium thiocyanate and 20% (w/v) PEG 3000