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Information on EC 1.11.1.21 - catalase-peroxidase and Organism(s) Escherichia coli and UniProt Accession B1IVD5
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1.11.1.21 catalase-peroxidaseIUBMB 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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Word Map
- 1.11.1.21
-
1.11.1.7
-
katgs
- mycobacterium
- tuberculosis
- isoniazid
- dismutase
- ascorbate
- heme
- horseradish
- peroxidases
- guaiacol
-
ferric
- myeloperoxidase
- catalases
-
1.6.4.2
-
lignification
-
monofunctional
- lactoperoxidase
-
peroxidatic
-
isonicotinic
-
high-spin
-
inh-resistant
-
isoniazid-resistant
- o-dianisidine
- pseudomallei
-
antituberculosis
-
soret
-
catalatic
-
pro-drug
-
antitubercular
- medicine
-
mycolic
-
isoperoxidase
- monodehydroascorbate
-
1.8.5.1
-
low-spin
-
1.10.3.1
- pyrogallol
- 3-amino-1,2,4-triazole
-
coniferyl
-
1.14.18.1
-
4.3.1.5
- synthesis
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, afkatg, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
KatG
KatG
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-methoxyphenol + H2O2
? + H2O
about 90% conversion
products are oligomers of different weight, i.g. of 27 monomer units and of 23 monomer units
-
?
catechol + H2O2
? + H2O
about 90% conversion
products are oligomers of 7 monomer units
-
?
phenol + H2O2
? + H2O
about 90% conversion
products are oligomers of different weight, i.g. of 27 monomer units and of 23 monomer units
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
tert-butyl hydroperoxide + H2O2
oxidized tert-butyl hydroperoxide + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
KatP has stronger catalase than peroxidase activity
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
ferric KatP possesses a mixture of pentacoordinate and hexacoordinate high-spin heme iron
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
-
the bacterial manganese-dependent SOD A when bound to iron has peroxidase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
acts as an inhibitor of peroxidase activity at lower pH (pH 3.8-4.5)
H2O2
-
enzyme inhibition is observed at hydrogen peroxide concentrations greater than 1.0 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme KatGDELTAFG, in 50 mM acetate buffer pH 5.0, at 23°C
0.024
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.3 and 25°C
0.043
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y22F, pH 5.0, 23°C
0.048
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102L, at pH 6.0 and 25°C
0.055
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, wild type enzyme, at pH 6.0 and 25°C
0.061
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.08
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme H106C, at pH 6.0 and 25°C
0.086
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA200-214, pH 5.0, 23°C
0.087
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.1
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102C, at pH 6.0 and 25°C
0.23
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
0.24
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme W105L, at pH 6.0 and 25°C
0.31
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 5.0, 23°C
0.33
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme H106Y, at pH 6.0 and 25°C
0.4
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102K, at pH 6.0 and 25°C
0.48
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme W105F, at pH 6.0 and 25°C
1.06
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTAL193-N228, pH 5.0, 23°C
1.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA209-228, pH 5.0, 23°C
3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 50 mM acetate buffer, pH 5.0, at 23°C
0.07
H2O2
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.18
H2O2
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.83
H2O2
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
1.5
H2O2
-
peroxidase activity, mutant enzyme KatGDELTAFG, in 50 mM acetate buffer pH 5.0, at 23°C
3.5
H2O2
-
wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
4
H2O2
-
catalase activity, wild type enzyme, 100 mM phosphate buffer pH 7.0, at 23°C
4.5
H2O2
-
catalase activity, mutant enzyme KatGDELTAFG, 100 mM phosphate buffer pH 7.0, at 23°C
5.2
H2O2
-
mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme H106Y, at pH 6.0 and 25°C
1.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme H106C, at pH 6.0 and 25°C
25
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.3 and 25°C
26
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme KatGDELTAFG, in 50 mM acetate buffer pH 5.0, at 23°C
33.3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
50.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA200-214, pH 5.0, 23°C
52
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
55.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
77
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 50 mM acetate buffer, pH 5.0, at 23°C
83
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 5.0, 23°C
97
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y22F, pH 5.0, 23°C
660
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102L, at pH 6.0 and 25°C
710
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102C, at pH 6.0 and 25°C
740
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTAL193-N228, pH 5.0, 23°C
1100
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA209-228, pH 5.0, 23°C
3700
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102K, at pH 6.0 and 25°C
17000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, wild type enzyme, at pH 6.0 and 25°C
140000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme W105L, at pH 6.0 and 25°C
210000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme W105F, at pH 6.0 and 25°C
22.4
H2O2
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
26
H2O2
-
catalase activity, mutant enzyme KatGDELTAFG, 100 mM phosphate buffer pH 7.0, at 23°C
26
H2O2
-
peroxidase activity, mutant enzyme KatGDELTAFG, in 50 mM acetate buffer pH 5.0, at 23°C
58
H2O2
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
65
H2O2
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
2140
H2O2
-
mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
11000
H2O2
-
wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
12000
H2O2
-
catalase activity, wild type enzyme, 100 mM phosphate buffer pH 7.0, at 23°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
26
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 50 mM acetate buffer, pH 5.0, at 23°C
270
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 5.0, 23°C
546
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
580
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA200-214, pH 5.0, 23°C
634
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
750
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTAL193-N228, pH 5.0, 23°C
960
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA209-228, pH 5.0, 23°C
2300
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y22F, pH 5.0, 23°C
5.7
H2O2
-
catalase activity, mutant enzyme KatGDELTAFG, 100 mM phosphate buffer pH 7.0, at 23°C
320
H2O2
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
360
H2O2
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
410
H2O2
-
mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
3100
H2O2
-
catalase activity, wild type enzyme, 100 mM phosphate buffer pH 7.0, at 23°C
3200
H2O2
-
wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
azide
Escherichia coli
-
mutant enzyme W105L, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.008
azide
Escherichia coli
-
wild type enzyme, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.01
azide
Escherichia coli
-
mutant enzyme R102K, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.095
azide
Escherichia coli
-
mutant enzyme R102L, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.18
azide
Escherichia coli
-
mutant enzyme R102C, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.19
azide
Escherichia coli
-
mutant enzyme H106C, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.23
azide
Escherichia coli
-
mutant enzyme H106Y, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.25
azide
Escherichia coli
-
mutant enzyme W105F, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.012
cyanide
Escherichia coli
-
mutant enzyme W105F, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.04
cyanide
Escherichia coli
-
mutant enzyme H106C, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.055
cyanide
Escherichia coli
-
mutant enzyme R102L, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.065
cyanide
Escherichia coli
-
mutant enzyme W105L, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.075
cyanide
Escherichia coli
-
mutant enzyme R102C, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.09
cyanide
Escherichia coli
-
wild type enzyme, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.21
cyanide
Escherichia coli
-
mutant enzyme H106Y, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
0.39
cyanide
Escherichia coli
-
mutant enzyme R102K, at pH 7.0 and 37°C for catalase activity and at pH 6.0 and 25°C for peroxidase activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
1900
8.3
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.3 and 25°C
85
11
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.3 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
periplasmic catalase-peroxidases contributes to bacterial virulence
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA200-214
-
mutation eliminates catalase activity, but variant is substantially more active as peroxidase
DELTAL193-N228
-
mutant lacking Large Loop1, mutation eliminates catalase activity, but variant is substantially more active as peroxidase
H106C
H106Y
H257Y
-
the mutant shows 0.05% of wild type catalase activity and 1.8% of wild type peroxidase activity
H267Y
-
the peroxidatic-to-catalatic ratio of the mutant is increased 36fold, the heme content of the mutant is reduced relative to the wild type enzyme
R102C
R102K
R102L
W105F
W105L
Y111A
-
the mutation leads to a 5fold reduction in the apparent kcat for catalase activity and an 8fold decrease in the apparent second-order rate constant. For peroxidase activity, the H2O2- and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)-dependent peroxidatic apparent kcat are reduced by 66% and 40%, respectively. Preparations of this variant yield a mixture of high- and low-spin heme states, thus creating the appearance of a transition between wild type (high-spin) and C-terminal lacking (low-spin) KatG
Y226F
-
mutation eliminates catalase activity, but variant is substantially more active as peroxidase
additional information
-
the heme environment of mutant KatGDELTAFG (lacking its FG insertion) is highly similar to wild type KatG, but the variant retains only 0.2% catalase activity. In contrast, the deletion reduces peroxidase activity by only 50%
H106C
-
the mutant shows 0.01% of wild type catalase activity and 1.7% of wild type peroxidase activity
H106C
-
the peroxidatic-to-catalatic ratio of the mutant is increased 125fold, the heme content of the mutant is reduced relative to the wild type enzyme
H106Y
-
the mutant shows 0.008% of wild type catalase activity and 2.7% of wild type peroxidase activity
H106Y
-
the peroxidatic-to-catalatic ratio of the mutant is increased 321fold, the heme content of the mutant is reduced relative to the wild type enzyme
R102C
-
the mutant shows 0.5% of wild type catalase activity and 10% of wild type peroxidase activity
R102C
-
the peroxidatic-to-catalatic ratio of the mutant is increased 18fold, the heme content of the mutant is reduced relative to the wild type enzyme
R102K
-
the mutant shows 1.8% of wild type catalase activity and 13% of wild type peroxidase activity
R102K
-
the peroxidatic-to-catalatic ratio of the mutant is increased 7fold, the heme content of the mutant is reduced relative to the wild type enzyme
R102L
-
the mutant shows 1% of wild type catalase activity and 13% of wild type peroxidase activity
R102L
-
the peroxidatic-to-catalatic ratio of the mutant is increased 13fold, the heme content of the mutant is reduced relative to the wild type enzyme
W105F
-
the mutant shows 0.1% of wild type catalase activity and 288% of wild type peroxidase activity
W105F
-
the peroxidatic-to-catalatic ratio of the mutant is increased 2800fold, the heme content of the mutant is reduced relative to the wild type enzyme
W105L
-
the mutant shows 0.3% of wild type catalase activity and 197% of wild type peroxidase activity
W105L
-
the peroxidatic-to-catalatic ratio of the mutant is increased 612fold, the heme content of the mutant is reduced relative to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant KatGDELTAFG is expressed in Escherichia coli BL-21 (DE3) pLysS cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of 0.5 mM Fe(II)-citrate to culture liquid results in 36% increase in enzyme, substrate o-dianisidine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Varnado, C.L.; Hertwig, K.M.; Thomas, R.; Roberts, J.K.; Goodwin, D.C.
Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7
Arch. Biochem. Biophys.
421
166-174
2004
Escherichia coli
Moore, R.L.; Powell, L.J.; Goodwin, D.C.
The kinetic properties producing the perfunctory pH profiles of catalase-peroxidases
Biochim. Biophys. Acta
1784
900-907
2008
Escherichia coli
Moore, R.L.; Cook, C.O.; Williams, R.; Goodwin, D.C.
Substitution of strictly conserved Y111 in catalase-peroxidases: Impact of remote interdomain contacts on active site structure and catalytic performance
J. Inorg. Biochem.
102
1819-1824
2008
Escherichia coli
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.
Li, Y.; Goodwin, D.C.
Vital roles of an interhelical insertion in catalase-peroxidase bifunctionality
Biochem. Biophys. Res. Commun.
318
970-976
2004
Escherichia coli
Hillar, A.; Peters, B.; Pauls, R.; Loboda, A.; Zhang, H.; Mauk, A.G.; Loewen, P.C.
Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis
Biochemistry
39
5868-5875
2000
Escherichia coli, Escherichia coli UM262
Loewen, P.C.; Triggs, B.L.; George, C.S.; Hrabarchuk, B.E.
Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli
J. Bacteriol.
162
661-667
1985
Escherichia coli
Smulevich, G.; Jakopitsch, C.; Droghetti, E.; Obinger, C.
Probing the structure and bifunctionality of catalase-peroxidase (KatG)
J. Inorg. Biochem.
100
568-585
2006
Escherichia coli, Mycobacterium tuberculosis (P9WIE5), Synechococcus sp. (Q31MN3), Burkholderia pseudomallei (Q939D2), Synechococcus sp. PCC 7942 (Q31MN3), Mycobacterium tuberculosis H37Rv (P9WIE5)
Di Gennaro, P.; Bargna, A.; Bruno, F.; Sello, G.
Purification of recombinant catalase-peroxidase HPI from E. coli and its application in enzymatic polymerization reactions
Appl. Microbiol. Biotechnol.
98
1119-1126
2014
Escherichia coli (B1IVD5), Escherichia coli, Escherichia coli DSM 1576 (B1IVD5)
Kudalkar, S.N.; Campbell, R.A.; Li, Y.; Varnado, C.L.; Prescott, C.; Goodwin, D.C.
Enhancing the peroxidatic activity of KatG by deletion mutagenesis
J. Inorg. Biochem.
116
106-115
2012
Escherichia coli
Ganini, D.; Petrovich, R.M.; Edwards, L.L.; Mason, R.P.
Iron incorporation into MnSOD A (bacterial Mn-dependent superoxide dismutase) leads to the formation of a peroxidase/catalase implicated in oxidative damage to bacteria
Biochim. Biophys. Acta
1850
1795-1805
2015
Escherichia coli
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