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EC Tree
IUBMB Comments Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
The taxonomic range for the selected organisms is: Synechocystis sp. The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
catalase-peroxidase, catalase peroxidase, catalase/peroxidase, hydroperoxidase i, katg2, katx2, katg1, fvcp02, fvcp01, fesod a,
more
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catalase-peroxidase
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catalase-peroxidase
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bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7
KatG
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KatG
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bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7
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2 H2O2 = O2 + 2 H2O
distal site Asp152 is essential for the catalase activity of catalase-peroxidase, mechanism for hydrogen peroxide oxidation in volving residues Trp122 and Asp152
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donor:hydrogen-peroxide oxidoreductase
Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
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2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
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-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
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-
-
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?
guajacol + H2O2
? + H2O
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peroxidase activity
-
-
?
o-dianisidine + H2O2
? + H2O
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peroxidase activity
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
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-
-
-
?
pyrogallol + H2O2
? + H2O
additional information
?
-
H2O2
O2 + H2O
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-
-
-
?
H2O2
O2 + H2O
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catalase activity
-
-
?
pyrogallol + H2O2
? + H2O
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-
-
-
?
pyrogallol + H2O2
? + H2O
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peroxidase activity
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-
?
additional information
?
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bifunctional enzyme providing catalase and peroxidase activities, intermediate structure
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?
additional information
?
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the recombinant protein contains high catalase activity and an appreciable peroxidase activity with o-dianisidine, guaiacol and pyrogallol, but not with NAD(P)H, ferrocytochrome c, ascorbate or glutathione as electron donors
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?
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Fe
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dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant
Fe2+
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heme
Fe2+
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dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant
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additional information
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the enzyme is not inhibited by 3-amino-1,2,4-triazole
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azide
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cyanide
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cyanide
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highly sensitive
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2.8
H2O2
wild type enzyme, in 25 mM HEPES-NaOH buffer (pH 7.0) at 25°C
0.007
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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peroxidase reaction, at pH 4.3 and 25°C
additional information
additional information
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steady- and transient-state kinetics
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1
H2O2
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peroxidase reaction, at pH 4.3 and 25°C
1.7
H2O2
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catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
2.3
H2O2
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catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
2.4
H2O2
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mutant D152S, pH 7.0, 30°C
2.5
H2O2
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mutants D152N and P151A, pH 7.0, 30°C
3.1
H2O2
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catalase reaction, at pH 7.0 and 37°C
3.2
H2O2
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mutant D152W, pH 7.0, 30°C
4.1
H2O2
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wild-type enzyme, pH 7.0, 30°C
4.1
H2O2
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catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
4.9
H2O2
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catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
20
H2O2
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catalase reaction, at pH 5.5-6.0 and 37°C
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13
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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peroxidase reaction, at pH 4.3 and 25°C
2
H2O2
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catalase activity, mutant enzyme H123E, in 100 mM phosphate buffer, pH 7.0, at 23°C
6
H2O2
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catalase activity, mutant enzyme Y249F, in 100 mM phosphate buffer, pH 7.0, at 23°C
20
H2O2
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mutant D152W, pH 7.0, 30°C
95
H2O2
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mutant D152N, pH 7.0, 30°C
170
H2O2
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catalase activity, mutant enzyme R439A, in 100 mM phosphate buffer, pH 7.0, at 23°C
200
H2O2
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mutant D152S, pH 7.0, 30°C
200
H2O2
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catalase activity, mutant enzyme D152S, in 100 mM phosphate buffer, pH 7.0, at 23°C
200
H2O2
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catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
200
H2O2
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mutant enzyme D152S, catalase activity, pH and temperature not specified in the publication
580
H2O2
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catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
890
H2O2
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mutant enzyme E243Q, catalase activity, pH and temperature not specified in the publication
2500
H2O2
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mutant P151A, pH 7.0, 30°C
3500
H2O2
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wild-type enzyme, pH 7.0, 30°C
3500
H2O2
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catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
3500
H2O2
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catalase activity, wild type enzyme, in 100 mM phosphate buffer, pH 7.0, at 23°C
3500
H2O2
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catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
3500
H2O2
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wild type enzyme, catalase activity, pH and temperature not specified in the publication
7630
H2O2
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catalase reaction, at pH 7.0 and 37°C
8000
H2O2
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catalase reaction, at pH 5.5-6.0 and 37°C
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120
H2O2
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catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
250
H2O2
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catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
710
H2O2
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catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
850
H2O2
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catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
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0.051
azide
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in 67 mM phosphate buffer, pH 7.0, at 30°C
0.037
cyanide
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in 67 mM phosphate buffer, pH 7.0, at 30°C
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0.013
azide
Synechocystis sp.
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at pH 7.0 and 37°C
0.17
cyanide
Synechocystis sp.
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at pH 7.0 and 37°C
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0.5
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substrate guajacol, mutant P151A
0.55
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peroxidase activity, using guaiacol as substrate, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
0.61
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crude enzyme, peroxidase activity, in 67 mM phosphate buffer, pH 7.0, at 25°C
1.7
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after 2.79fold purification, peroxidase activity, in 67 mM phosphate buffer, pH 7.0, at 25°C
1.9
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peroxidase activity, using o-dianisidine as substrate, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
12.5
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substrate pyrogallol, mutant D152N
13.6
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substrate pyrogallol, mutant D152S
2.4
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substrate o-dianisidine, mutant P151A
2.5
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substrate guajacol, mutants D152N and D152S
21.5
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substrate o-dianisidine, mutant D152W
3.2
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substrate o-dianisidine, wild-type enzyme
3.8
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peroxidase activity, using o-dianisidine as substrate, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
368
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crude enzyme, catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
4.3
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peroxidase activity, using o-dianisidine as substrate, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
5.5
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peroxidase specific activity, using o-dianisidine as substrate, at pH 4.3 and 25°C
5420
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catalase specific activity, at pH 7.0 and 37°C
6.4
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peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.3 and 25°C
6.6
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substrate pyrogallol, wild-type enzyme
7.3
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substrate pyrogallol, mutant D152W
7.5
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substrate o-dianisidine, mutant D152N
7.6
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substrate o-dianisidine, mutant D152S
983
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after 2.67fold purification, catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
0.6
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substrate guajacol, wild-type enzyme
0.6
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peroxidase activity, using guaiacol as substrate, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
0.6
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peroxidase activity, using guaiacol as substrate, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
4.1
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substrate guajacol, mutant D152W
4.1
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substrate pyrogallol, mutant P151A
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5.4
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isoelectric focusing
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UniProt
brenda
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malfunction
although the rate of H2O2 decomposition is about 30times lower in the katG deletion mutant than in the wild type, the strain has a normal phenotype and its doubling time as well as its resistance to H2O2 and methyl viologen are indistinguishable from those of the wild type
physiological function
catalase-peroxidase has a protective role against environmental H2O2
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80000
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about 80000, SDS-PAGE
85000
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2 * 85000, SDS-PAGE
85122
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2 * 85122, MALDI-TOF mass spectrometry
85137
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2 * 85137, calculated from amino acid sequence
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homodimer
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2 * 85000, SDS-PAGE
homodimer
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2 * 85122, MALDI-TOF mass spectrometry
homodimer
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2 * 85137, calculated from amino acid sequence
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D152N
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site-directed mutagenesis, 2.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
D152W
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site-directed mutagenesis, 0.6% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
E253Q
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the mutant shows strongly reduced catalase activity
H123E
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mutant with very low catalase activity
N153A
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the mutant shows 6% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG
N153D
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the mutant shows 16.5% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG
P151A
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site-directed mutagenesis, slightly increased catalase activity compared to the wild-type enzyme
R439A
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mutant with very low catalase activity
D152S
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site-directed mutagenesis, 5.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
D152S
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mutant with very low catalase activity
D152S
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the mutant shows strongly reduced catalase activity
W122F
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inactive
W122F
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mutant without catalase activity
Y249F
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the bimolecular rate constants of dioxygen binding to ferrous Y249F is 1.3fold higher than the wild-type value. The dissociation constants of the ferrous-dioxygen is 1.5fold higher than wild-type value
Y249F
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mutant with very low catalase activity
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65
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the enzyme is completely inactive after less than 1 min at 65°C
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ammonium sulfate precipitation and DEAE-cellulose column chromatography
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Zn2+-chelate affinity chromatography and phenyl-Sepharose column chromatography
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) pLysS cells
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expression of wild-type and mutant enzymes in Escherichia coli
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Jakopitsch, C.; Auer, M.; Regelsberger, G.; Jantschko, W.; Furtmuller, P.G.; Ruker, F.; Obinger, C.
Distal site aspartate is essential in the catalase activity of catalase-peroxidases
Biochemistry
42
5292-5300
2003
Synechocystis sp.
brenda
Jakopitsch, C.; Wanasinghe, A.; Jantschko, W.; Furtmueller, P.G.; Obinger, C.
Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism
J. Biol. Chem.
280
9037-9042
2005
Synechocystis sp.
brenda
Singh, R.; Wiseman, B.; Deemagarn, T.; Jha, V.; Switala, J.; Loewen, P.
Comparative study of catalase-peroxidases (KatGs)
Arch. Biochem. Biophys.
471
207-214
2008
Archaeoglobus fulgidus, Burkholderia pseudomallei, Escherichia coli, Geobacillus stearothermophilus, Mycobacterium tuberculosis, Rhodobacter capsulatus, Synechocystis sp.
brenda
Vlasits, J.; Furtmueller, P.G.; Jakopitsch, C.; Zamocky, M.; Obinger, C.
Probing hydrogen peroxide oxidation kinetics of wild-type Synechocystis catalase-peroxidase (KatG) and selected variants
Biochim. Biophys. Acta
1804
799-805
2010
Synechocystis sp.
brenda
Jakopitsch, C.; Rueker, F.; Regelsberger, G.; Dockal, M.; Peschek, G.A.; Obinger, C.
Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization
Biol. Chem.
380
1087-1096
1999
Synechocystis sp.
brenda
Jakopitsch, C.; Auer, M.; Regelsberger, G.; Jantschko, W.; Furtmller, P.; Rker, F.; Obinger, C.
The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases
Eur. J. Biochem.
270
1006-1013
2003
Synechocystis sp.
brenda
Vlasits, J.; Jakopitsch, C.; Schwanninger, M.; Holubar, P.; Obinger, C.
Hydrogen peroxide oxidation by catalase-peroxidase follows a non-scrambling mechanism
FEBS Lett.
581
320-324
2007
Synechocystis sp., Mycobacterium tuberculosis
brenda
Tichy, M.; Vermaas, W.
In vivo role of catalase-peroxidase in Synechocystis sp. strain PCC 6803
J. Bacteriol.
181
1875-1882
1999
Synechocystis sp. (P73911), Synechocystis sp.
brenda