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1.11.1.18: bromide peroxidase

This is an abbreviated version!
For detailed information about bromide peroxidase, go to the full flat file.

Word Map on EC 1.11.1.18

Reaction

RH
+
HBr
 +
H2O2
=
RBr
 + 2 H2O

Synonyms

apobromoperoxidase I, BPO, BPO 1, BPO 2, BPO I, BPO-A1, BPO-A2, BPO1, bpoA1, bromooperoxidase, bromoperoxidase, bromoperoxidase A2, bromoperoxidase I, bromoperoxidase II, bromoperoxidase-catalase, BrPO, CoVBPO, CVBPO, EC 1.11.1.10, haeme-thiolate peroxidase, HAP phytase, metal-free bromoperoxidase, More, non-haem bromoperoxidase, non-haem bromoperoxidase BPO 1, non-haem bromoperoxidase BPO 2, non-haem bromoperoxidase BPO-A2, non-heme haloperoxidases, non-heme-type bromoperoxidase, nonhaem-type bromoperoxidase BPO 1a, nonhaem-type bromoperoxidase BPO 1b, nonhaem-type bromoperoxidase BPO 3, nonheme bromoperoxidase, nVBPO, perhydrolase, rVBPO, St-Phy, sVBPO, V-BPO, V-BrPO, V-containing-haloperoxidase, vanadate haloperoxidase, vanadate-dependent bromoperoxidase I, vanadium bromoperoxidase, vanadium containing bromoperoxidase, vanadium-bromoperoxidase, vanadium-containing bromoperoxidase, vanadium-dependent bromoperoxidase, vanadium-dependent bromoperoxidase 2, vanadium-dependent haloperoxidase, vanadium-dependent peroxidase, vBPO, VBPO1, VBPO2, VBrPO, VBrPO(AnI), VBrPO(AnII)

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.18 bromide peroxidase

Crystallization

Crystallization on EC 1.11.1.18 - bromide peroxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized from ammonium sulfate solutions in a form suitable for X-ray diffraction analysis. Crystals are grown by the vapour-diffusion technique using the sitting-drop method. X-ray diffraction studies show that the crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 with a = b = 114.3 and c = 276.0 A. The crystals diffract to at least 2.4 A resolution
purified native enzyme, hanging drop vapor diffusion method, mixing of 0.001-0.002 ml of 8 mg/ml protein solution with 0.0005-0.001 ml of reservoir solution containing 0.1 M sodium chloride, 0.01 M Tris-HCl, pH 5.5, and 25% PEG 3350 leading to monoclinic crystals, or 0.15 M potassium rhodanide, 0.01 M Tris, pH 7.5, and 19% PEG 3350 leading to hexagonal crystals, both at a temperature of 18°C, X-ray diffraction structure determination and analysis at 2.26 A resolution, molecular replacement and modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template
structure of the enzyme is solved by single isomorphous replacement anomalous scattering X-ray crystallography at 2.0 A resolution. Crystals of the holoenzyme and the apoenzyme are obtained from 2.1 M ammonium sulfate solutions buffered at pH 8.3 and diffract to 2.4 A resolution. The crystals are stable in the X-ray beam for more than one week. They belong to the tetragonal system, space group P4(3)2(1)2, with lattice constants a ?= 114.3 A,? c = 276.0 A
the crystals exhibit a teardrop morphology and are grown from 2 M ammonium dihydrogen phosphate pH and diffract to beyond 1.7 A resolution. They are in tetragonal space group P4222 with unit-cell dimensions of a = b = 201.9 A, c = 178.19 A, alpha = beta = gamma = 90°
-
sitting drop vapour diffusion method, two crystal forms are obtained, one hexagonal form using ammonium phosphate as precipitant (form 1) and a second cubic vanadium bound form (form 2). The best crystals of the cubic form 2 containing vanadate are only obtained with the wild type enzyme. The optimised conditions use an initial protein concentration of 18 mg/ml in 50 mM Tris-H2SO4, 0.4 M KBr, 1 mM Na3VO4, 20% (w/v) polyethylene glycol 6000. For the wild type enzyme crystals grown in form 2, a mother liquor substituting the precipitant with 25% polyethylene glycol 400 and 25% polyethylene glycol 6000 is used
-
the hanging-drop vapor diffusion method
-