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

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 I, DyP II, DyP-I, DyP-type peroxidase, DyP1, DyP2, DyP3, EfeB, LiP BA45, LiP-SN, manganese-independent peroxidase I, manganese-independent peroxidase II, TT1485, tyrA, YcdB, YfeX, 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
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
-
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
-
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
-
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
-
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
-
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)
-
sitting drop vapor diffusion method, using 0.2 M potassium thiocyanate and 20% (w/v) PEG 3000