Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.11.1.21: catalase-peroxidase

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

Word Map on EC 1.11.1.21

Reaction

2 H2O2 =

O2
+ 2 H2O

Synonyms

AfKatG, BW16_04845, CAT, CAT-2, catalase -peroxidase KatG, catalase peroxidase, catalase-peroxidase, catalase/peroxidase, CP 2, CP01, CP02, CPX, CthediskatG, EC 1.11.1.7, FeSOD A, FvCP01, FvCP02, FVEG_10866, FVEG_12888, HCP, hemoprotein b-590, HPI, hydroperoxidase I, KatG, KatG1, KatG2, KatP, katX2, KpCP, PCP, Rv1908c

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.21 catalase-peroxidase

Crystallization

Crystallization on EC 1.11.1.21 - catalase-peroxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure reveals highly conserved catalytic residues His57 and Asn130 in the heme cavity and Asp110 in the main channel
to 1.65-1.95 A resolution. One binding site in the main access channel and one site on the protein surface accommodate pyrogallol, catechol, resorcinol, guaiacol, hydroquinone, and 2-chlorophenol. A third site, in the heme distal side, accommodates only pyrogallol and catechol and interacts with the heme iron and the catalytic His and Arg residues
-
crystal structure of the D141E variant determined at 1.8 A resolution
-
hanging drop vapor diffusion method, using 16-20% (w/v) PEG 4K, 20% (v/v) 2-methyl-2,4-pentanediol and 0.1 M sodium citrate pH 5.6, at 20°C
mutant enzyme D141A in complex with isoniazid, hanging drop vapor diffusion method, using 16-20% (w/v) PEG 4000, 20% (w/v) 2-methyl-2,4-pentanediol, and 0.1 M sodium citrate pH 5.6
purified recombinant enzyme, hanging drop vapour diffusion method, 0.001 ml of 22 mg/ml protein in potassium phosphate, pH 7.0, mixed with equal volume of reservoir solution containing 16-20% PEG 4000, 20% 2-methyl-2,4-pentanediol, and 0.1 M sodium citrate, pH 5.6, 3-5 days, 20°C, X-ray diffraction strcuture determination and analysis at 1.8 A resolution, molecular replacement
hanging-drop vapour-diffusion method, the rhombic plate-shaped crystals are grown from purified protein solution using (NH4)2SO4 as precipitant at 20°C. The crystal belongs to the monoclinic system, space group C2, and diffract beyond 2.0 A resolution
the 2.0 A crystal structure of the enzyme reveals that it is a dimer of two identical subunits. Each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase. The active site is in the N-terminal domain. Although the arrangement of the catalytic residues and the cofactor heme b in the active site is virtually identical to that of class I peroxidases, the heme moiety is buried inside the domain, similar to that in a typical catalase. In the vicinity of the active site, novel covalent bonds are formed among the side chains of three residues, including that of a tryptophan on the distal side of the heme. Together with the C-terminal domain, these covalent bonds fix two long loops on the surface of the enzyme that cover the substrate access channel to the active site. These features provide an explanation for the dual activities of this enzyme
hanging drop vapor diffusion method, using 4% (w/v) polyethylene glycol 3350 and 0.1 M sodium acetate (pH 4.6), at 20°C
purified wild-type and mutant enzymes with bound isoniazid, X-ray diffraction structure determination and analysis at 2.7-3.7 A resolution, dimeric cryo-electronmicroscopic structure of KatGINH. The two protomers are nearly identical, with a root-meansquare deviation (RMSD) value of 0.4 A for Ca atoms when superposing protomer A onto protomer B. There is one notable difference, with protomer B displaying density for residues 206-221. These residues form part of a large loop insertion (LL1), which extends from Glu195 to Asn231 and includes Tyr229 of the MYW catalytic triad. Density for these residues is not observed in protomer A
purified recombinant His6-tagged enzyme CAT-2, (1) microbatch method, mixing 800 nl of 20 mg/ml protein in 50 mM phosphate Na/K, pH 7.0, 150 mM NaCl, and 0.5% noctyl-beta-D-glycoside with 800 nl of crystallization solution containing 0.2 M calcium acetate and 20% PEG 3350, the drops are covered with 0.01 ml of paraffin oil for 7 days at 18°C, (2) sitting drop vapor diffusion technique, mixing of 200 nl of 42 mg/ml protein in 50 mM arginine/glutamate, pH 7.5, with 200 nl of crystallization solution containing 9% PEG 8000, 225 mM magnesium chloride, and 100 mM Tris/HCl, pH 7.0, at 18°C, 3-4 weeks. X-ray diffraction structure determination and analysis at 2.9 A and 2.6 A resolution, respectively, structure modeling
sitting drop vapor diffusion method, using 15% (w/v) PEG 4000 and 0.1 M sodium acetate (pH 4.6)
to 1.55 A resolution. Structure reveals a wrapping at the dimer interface of the N-terminal elongations from the two subunits and cysteine residues that cross-link the two subunits
in complex with isoniazid, sitting drop vapor diffusion method, using 4.3 M sodium formate and 100 mM sodium citrate, pH 6.4
vapor diffusion method, using 4.0-4.3 M sodium formate with 100 mM sodium citrate pH 6.0-6.5 as a precipitant