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Information on EC 1.11.1.21 - catalase-peroxidase and Organism(s) Synechocystis sp. and UniProt Accession P73911

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.21 catalase-peroxidase
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.
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Synechocystis sp.
UNIPROT: P73911
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Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
2
=
+
2
2
=
+
2
Synonyms
catalase-peroxidase, catalase peroxidase, catalase/peroxidase, hydroperoxidase i, katg2, katx2, katg1, fvcp02, fvcp01, fesod a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
catalase-peroxidase
EC 1.11.1.7
-
formerly
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 H2O2 = O2 + 2 H2O
show the reaction diagram
distal site Asp152 is essential for the catalase activity of catalase-peroxidase, mechanism for hydrogen peroxide oxidation in volving residues Trp122 and Asp152
-
SYSTEMATIC NAME
IUBMB Comments
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
show the reaction diagram
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
show the reaction diagram
-
-
-
-
?
guajacol + H2O2
? + H2O
show the reaction diagram
-
peroxidase activity
-
-
?
H2O2
O2 + H2O
show the reaction diagram
o-dianisidine + H2O2
? + H2O
show the reaction diagram
-
peroxidase activity
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
show the reaction diagram
-
-
-
-
?
pyrogallol + H2O2
? + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
azide
cyanide
additional information
-
the enzyme is not inhibited by 3-amino-1,2,4-triazole
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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)
-
peroxidase reaction, at pH 4.3 and 25°C
1 - 20
H2O2
additional information
additional information
-
steady- and transient-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.3 and 25°C
2 - 8000
H2O2
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
120 - 850
H2O2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.051
azide
-
in 67 mM phosphate buffer, pH 7.0, at 30°C
0.037
cyanide
-
in 67 mM phosphate buffer, pH 7.0, at 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
azide
Synechocystis sp.
-
at pH 7.0 and 37°C
0.17
cyanide
Synechocystis sp.
-
at pH 7.0 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.5
-
substrate guajacol, mutant P151A
0.55
-
peroxidase activity, using guaiacol as substrate, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
0.61
-
crude enzyme, peroxidase activity, in 67 mM phosphate buffer, pH 7.0, at 25°C
1.7
-
after 2.79fold purification, peroxidase activity, in 67 mM phosphate buffer, pH 7.0, at 25°C
1.9
-
peroxidase activity, using o-dianisidine as substrate, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
12.5
-
substrate pyrogallol, mutant D152N
13.6
-
substrate pyrogallol, mutant D152S
2.4
-
substrate o-dianisidine, mutant P151A
2.5
-
substrate guajacol, mutants D152N and D152S
21.5
-
substrate o-dianisidine, mutant D152W
3.2
-
substrate o-dianisidine, wild-type enzyme
3.8
-
peroxidase activity, using o-dianisidine as substrate, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
368
-
crude enzyme, catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
4.3
-
peroxidase activity, using o-dianisidine as substrate, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
5.5
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.3 and 25°C
5420
-
catalase specific activity, at pH 7.0 and 37°C
6.4
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.3 and 25°C
6.6
-
substrate pyrogallol, wild-type enzyme
7.3
-
substrate pyrogallol, mutant D152W
7.5
-
substrate o-dianisidine, mutant D152N
7.6
-
substrate o-dianisidine, mutant D152S
983
-
after 2.67fold purification, catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
-
gel filtration
80000
-
about 80000, SDS-PAGE
85000
-
2 * 85000, SDS-PAGE
85122
-
2 * 85122, MALDI-TOF mass spectrometry
85137
-
2 * 85137, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D152N
-
site-directed mutagenesis, 2.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
D152S
D152W
-
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
-
the mutant shows strongly reduced catalase activity
H123E
-
mutant with very low catalase activity
N153A
-
the mutant shows 6% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG
N153D
-
the mutant shows 16.5% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG
P151A
-
site-directed mutagenesis, slightly increased catalase activity compared to the wild-type enzyme
R439A
-
mutant with very low catalase activity
W122F
Y249F
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
the enzyme is completely inactive after less than 1 min at 65°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE-cellulose column chromatography
-
Zn2+-chelate affinity chromatography and phenyl-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expression of wild-type and mutant enzymes in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team