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.

Reaction

Reactive Blue 5
+ 2 H2O2 =
Phthalate
+
2,2'-disulfonyl azobenzene
+
3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate
+ 2 H2O

Synonyms

AnaPX, dye-decolorizing peroxidase, DyP, DyP-type peroxidase, DyP1, DyP2, DyP3, manganese-independent peroxidase I, manganese-independent peroxidase II, TT1485, tyrA, YcdB, YwbN

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.19 dye decolorizing peroxidase

Crystallization

Crystallization on EC 1.11.1.19 - dye decolorizing peroxidase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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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
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
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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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