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1.11.1.6: catalase

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

Word Map on EC 1.11.1.6

Reaction

2 H2O2 =

O2
+ 2 H2O

Synonyms

Ab-catalase, BNC, caperase, CAT, CAT-1, CAT-A, CAT-P, Cat1.4, CatA, catalase, catalase A, catalase C, catalase form III, catalase P, catalase-1, catalase-A, catalase-peroxidase, catalase-phenol oxidase, CatB, CATC, CatF, CatG, CatP, CATPO, CcmC, CP, equilase, H2O2:H2O2 oxidoreductase, haem catalase, HPI-A, HPI-B, HPII, HTHP, hydrogen peroxide oxidoreductase, KAT, Kat E catalase, KatA, KatB, KatC, KatP, KpA, manganese catalase, More, optidase, PktA, polyethylene glycol-catalase, tyrosine-coordinated heme protein, VktA

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.6 catalase

Crystallization

Crystallization on EC 1.11.1.6 - catalase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffraction to 1.96 A. Comparison with catalase from Proteus mirabilis. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. The reduced thermal stability of cold-adapted Aliivibrio salmonicida catalase may be explained by a reduced number of ion-pair networks and displacement of the four C-terminal alpha-helices
fee enzyme and enzyme complexed with ammonia or NO, hanging drop vapor diffusion method, mixing of 0.004 ml of 12-13 mg/ml protein, containing NH4OH, with an equal volume of the reservoir solution consisting of 45-60 mM magnesium formate, pH 6.7, 2-3 weeks, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.88-1.99 A resolution
purified catalase form III, sitting drop vapour diffusion method, mixing of 40 mg/ml protein in 0.05 M sodium phosphate, pH 6.8, with reservoir solution containing 12% PEG 4000 and 0.05 M sodium phosphate, pH 6.8, X-ray diffraction structure determination and analysis at 2.69 A resolution
-
metal-bound [FeII/FeII]-ADEec and [FeII/MnII]-ADEec enzyme, sitting drop vapor diffusion, room temperature, X-ray diffraction struccture determination and analysis at 2.63-2.8 A resolution
-
homology modeling using crystal structures of human and bovine catalases
mutant M244A, diffraction to 2.0 A, monoclinic space group C2, presence of a dimer in the asymmetric unit
-
ammonium sulfate precipitation
Kloeckera sp.
-
hanging drop vapour diffusion method, using 24% (w/v) PEG 2000, 10 mM NaCl, 10 mM CaCl2, and 3% (w/v) 6-aminocaproic acid in 100 mM bis-Tris buffer pH 6.5 at 18°C
-
hanging-drop vapor diffusion method. Crystal structure of the complex of the catalase with the classical catalase inhibitor 3-amino-1,2,4-triazole is determined at 1.95 A resolution
native and recombinant wild-type enzyme and enzyme mutants H82N and V123F, sitting drop vapour diffusion method, mixing of 9.4 mg/ml protein with reservoir solution containing 18% w/v PEG 2000, 0.1 M barium chloride, 0.1 M bis-tris pH 6.8 for the wild-type enzyme, and 6-16% w/v PEG 400, 0.2 M potassium chloride, 0.01 M calcium chloride, 0.05 M sodium cacodylate, pH 5.0-5.6 for the mutant H82N or PEG 4000 instead of PEG 400 for the mutant V123F, X-ray diffraction structure determination and analysis at 2.7 A, 1.4 A, 1.5 A, and 1.9 A resolution, respectively
-
comparison with catalase from Aliivibrio salmonicida LFI1238. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. Compared with Proteus mirabilis, the four C-terminal alpha-helices of Aliivibrio salmonicida LFI1238 catalase are displaced in the structures, explaining the reduced thermal stability