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1-H-pyrrol-2-carbohydrazide
?
-
analysis of association and dissociation rate constants
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
2,6-dimethoxyphenol + H2O2
? + H2O
3,3'-diaminobenzidine + H2O2
? + H2O
3,3'-dimethoxybenzidine + H2O2
? + H2O
4-aminoantipyrine + H2O2
? + H2O
-
-
-
?
benzoic hydrazide
?
-
analysis of association and dissociation rate constants
-
-
?
beta-(3,4-dihydroxyphenyl)-L-alanine + H2O2
? + H2O
catechol + H2O2
? + H2O
-
-
-
?
ethanol + H2O2
acetaldehyde + ?
ethyl hydrogen peroxide + ethanol
acetaldehyde + ?
ethyl hydrogen peroxide + methanol
acetaldehyde + ?
ethyl hydrogen peroxide + nitrite
acetaldehyde + ?
formic acid + H2O2
?
-
-
-
?
furoic hydrazide
?
-
analysis of association and dissociation rate constants
-
-
?
H2O2 + 4-nitrophenol
?
-
-
-
-
?
H2O2 + dimethylaniline
?
-
low activity
-
-
?
H2O2 + methanol
formaldehyde + H2O
H2O2 + o-dianisidine
? + H2O
H2O2 + phenol
?
-
-
-
-
?
H2O2 + propyl gallate
?
-
best peroxidase substrate
-
-
?
H2O2 + pyrocatechol
?
-
-
-
-
?
isonicotinic hydrazide
?
-
antituberculosis drug, bactericidal function neeeds activation by bifunctional catalase-peroxidase KatG to produce an acyl-NAD adduct. Substrate binds with high affinity to a small portion of ferric enzyme in a six-coordinate heme iron form
-
-
?
methanol + H2O2
formaldehyde + ?
methyl hydrogen peroxide
formaldehyde + ?
-
-
-
?
NADH + H2O2
NAD+ + H2O
-
-
-
?
NADPH + H2O2
NADP+ + H2O
-
-
-
?
nicotinic hydrazide
?
-
analysis of association and dissociation rate constants
-
-
?
o-dianisidine + H2O2
? + H2O
o-methoxyphenol + H2O2
? + H2O
picolinic hydrazide
?
-
analysis of association and dissociation rate constants
-
-
?
pyrogallol + H2O2
? + H2O
reduced cytochrome c + H2O2
oxidized cytochrome c + H2O
-
-
-
?
additional information
?
-
2 H2O2
2 H2O + O2
-
-
-
?
2 H2O2
2 H2O + O2
-
-
-
-
?
2 H2O2
2 H2O + O2
-
-
-
-
?
2 H2O2
H2O + O2
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
via intermediate Compound I
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
via Compound I and Compound II intermediates
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
via Compound I and Compound II intermediates
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
r
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
KTL38510
-
-
-
?
2 H2O2
O2 + 2 H2O
KTL38510
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
only isoenzyme I has peroxidase activity
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
only isoenzyme I has peroxidase activity
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
2,6-dimethoxyphenol + H2O2
? + H2O
-
-
-
?
2,6-dimethoxyphenol + H2O2
? + H2O
-
-
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
-
-
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
isoform Cat-2
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
-
-
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
-
-
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
-
-
-
?
3,3'-dimethoxybenzidine + H2O2
? + H2O
-
-
-
?
3,3'-dimethoxybenzidine + H2O2
? + H2O
-
-
-
?
ascorbate + H2O2
? + H2O
-
-
-
?
ascorbate + H2O2
? + H2O
-
-
-
?
ascorbate + H2O2
? + H2O
-
-
-
?
ascorbate + H2O2
? + H2O
isoform Cat-2
-
?
ascorbate + H2O2
? + H2O
-
-
-
?
ascorbate + H2O2
? + H2O
-
-
-
?
beta-(3,4-dihydroxyphenyl)-L-alanine + H2O2
? + H2O
-
-
-
?
beta-(3,4-dihydroxyphenyl)-L-alanine + H2O2
? + H2O
Kloeckera sp.
-
low activity
-
?
beta-(3,4-dihydroxyphenyl)-L-alanine + H2O2
? + H2O
Kloeckera sp. 2201
-
low activity
-
?
ethanol + H2O2
acetaldehyde + ?
-
no peroxidase activity
-
?
ethanol + H2O2
acetaldehyde + ?
-
-
-
?
ethanol + H2O2
acetaldehyde + ?
-
-
-
?
ethyl hydrogen peroxide + ethanol
acetaldehyde + ?
-
-
-
?
ethyl hydrogen peroxide + ethanol
acetaldehyde + ?
-
-
-
?
ethyl hydrogen peroxide + methanol
acetaldehyde + ?
-
-
-
?
ethyl hydrogen peroxide + methanol
acetaldehyde + ?
-
-
-
?
ethyl hydrogen peroxide + nitrite
acetaldehyde + ?
-
-
-
?
ethyl hydrogen peroxide + nitrite
acetaldehyde + ?
-
-
-
?
H2O2
O2 + H2O
-
-
-
-
?
H2O2
O2 + H2O
Beta vulgaris var. cicla
-
-
-
?
H2O2
O2 + H2O
-
no peroxidase activity
-
?
H2O2
O2 + H2O
-
involved in acatalasemia
-
?
H2O2
O2 + H2O
Capra capra
-
-
-
?
H2O2
O2 + H2O
Capra capra
-
-
-
?
H2O2
O2 + H2O
-
no peroxidase-activity
-
?
H2O2
O2 + H2O
-
monofunctional catalase
-
?
H2O2
O2 + H2O
Cucurbita sp.
-
-
-
?
H2O2
O2 + H2O
-
two monofunctional, one bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
two monofunctional, one bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
detoxification enzyme, enzyme protects the cell against high concentrations of peroxide
-
-
?
H2O2
O2 + H2O
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
one monofunctional, two bifunctional catalases
-
?
H2O2
O2 + H2O
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
monofunctional catalase
-
?
H2O2
O2 + H2O
-
enzyme is responsible for prevention of dehydration-related oxidative damage during seed desiccation, H2O2 may play a role for enzyme expression regulation and in the transduction pathway
-
-
?
H2O2
O2 + H2O
-
detoxification and protection enzyme
-
-
?
H2O2
O2 + H2O
-
enzyme is responsible for the protection of the Helicobacter pylori cells against phagocyte attack in the gastric mucosa by disumtation of H2O2
-
-
?
H2O2
O2 + H2O
-
detoxification and protection enzyme
-
-
?
H2O2
O2 + H2O
-
abnormal reaction kinetics
-
?
H2O2
O2 + H2O
-
abnormal reaction kinetics
-
?
H2O2
O2 + H2O
-
involved in acatalasemia
-
?
H2O2
O2 + H2O
-
regulator of H2O2-levels or protective function for hemoglobin or other SH-proteins
-
?
H2O2
O2 + H2O
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
Kloeckera sp.
-
-
-
?
H2O2
O2 + H2O
Kloeckera sp. 2201
-
-
-
?
H2O2
O2 + H2O
monofunctional catalase
-
?
H2O2
O2 + H2O
-
catalase activity
-
-
?
H2O2
O2 + H2O
-
catalase activity
-
-
?
H2O2
O2 + H2O
-
catalase activity
-
-
?
H2O2
O2 + H2O
-
no peroxidase activity
-
?
H2O2
O2 + H2O
two monofunctional catalases, Cat-1 and Cat-3, one catalase-peroxidase enzyme, Cat-2
-
?
H2O2
O2 + H2O
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
H2O2
O2 + H2O
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
H2O2
O2 + H2O
-
detoxification enzyme, enzyme is naturally adapted to the cold climate of the arctic tundra
-
-
?
H2O2
O2 + H2O
-
detoxification enzyme, enzyme is naturally adapted to the cold climate of the arctic tundra
-
-
?
H2O2
O2 + H2O
-
one catalase-peroxidase, one catalase enzyme
-
?
H2O2
O2 + H2O
-
KatA catalase important for resistance of planctonic and biofilm cells to H2O2
-
?
H2O2
O2 + H2O
-
essential for optimal resistance to H2O2. KatB was not produced during the normal growth cycle. Catalase activity is greater in nonmucoid than in mucoid, alginate-producing organisms. When exposed to hydrogen peroxide and, to a greater extent, paraquat, total catalase activity was elevated 7fold to 16fold, respectively
-
-
?
H2O2
O2 + H2O
detoxification enzyme
-
-
?
H2O2
O2 + H2O
with pyrogallol as electron donor
-
-
?
H2O2
O2 + H2O
detoxification enzyme
-
-
?
H2O2
O2 + H2O
with pyrogallol as electron donor
-
-
?
H2O2
O2 + H2O
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
H2O2 decomposition is accompanied by enzyme inactivation which can be minimized in vitro by immobilization of the enzyme
-
-
?
H2O2
O2 + H2O
-
H2O2 decomposition is accompanied by enzyme inactivation which can be minimized in vitro by immobilization of the enzyme
-
-
?
H2O2
O2 + H2O
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
protective role of the enzyme
-
-
?
H2O2
O2 + H2O
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
three isoenzymes, Cat-1, Cat-2 and Cat-3
-
?
H2O2 + 2-aminophenol
?
-
-
-
-
?
H2O2 + 2-aminophenol
?
-
-
-
-
?
H2O2 + 3-chlorophenol
?
-
-
-
-
?
H2O2 + 3-chlorophenol
?
-
-
-
-
?
H2O2 + 4-chlorophenol
?
-
-
-
-
?
H2O2 + 4-chlorophenol
?
-
-
-
-
?
H2O2 + methanol
formaldehyde + H2O
-
peroxidase activity
-
-
?
H2O2 + methanol
formaldehyde + H2O
-
peroxidase activity
-
-
?
H2O2 + methanol
formaldehyde + H2O
-
peroxidase activity
-
-
?
H2O2 + o-dianisidine
? + H2O
-
peroxidase activity
-
-
?
H2O2 + o-dianisidine
? + H2O
-
peroxidase activity
-
-
?
H2O2 + o-dianisidine
? + H2O
-
peroxidase activity
-
-
?
methanol + H2O2
formaldehyde + ?
-
-
-
?
methanol + H2O2
formaldehyde + ?
-
-
-
?
methanol + H2O2
formaldehyde + ?
Kloeckera sp.
-
only in the presence of glucose and glucose oxidase
-
?
methanol + H2O2
formaldehyde + ?
Kloeckera sp. 2201
-
only in the presence of glucose and glucose oxidase
-
?
o-dianisidine + H2O2
? + H2O
-
peroxidatic activity
-
?
o-dianisidine + H2O2
? + H2O
-
-
-
?
o-dianisidine + H2O2
? + H2O
isoform Cat-2
-
?
o-dianisidine + H2O2
? + H2O
-
-
-
?
o-methoxyphenol + H2O2
? + H2O
-
only isoenzyme I has peroxidase activity
-
?
o-methoxyphenol + H2O2
? + H2O
-
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
-
only isoenzyme I has peroxidase activity
-
?
o-methoxyphenol + H2O2
? + H2O
-
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
isoform Cat-2
-
?
o-methoxyphenol + H2O2
? + H2O
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
-
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
-
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
-
i.e. guaiacol
-
?
pyrogallol + H2O2
? + H2O
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
?
additional information
?
-
no substrate: o-phenylenediamine. The purified catalase is not reduced by sodium dithionite
-
-
?
additional information
?
-
-
enzyme also shows alkaline peroxidase activity, which is much lower than the catalase activity, no peroxidase activity with 3-aminophenol, 2,4,6-trichlorophenol, and 3-nitrophenol
-
-
?
additional information
?
-
-
BNC does not show any peroxidatic activity with 4-aminoantipyrine or pyrogallol as substrate
-
-
?
additional information
?
-
-
enzyme also shows alkaline peroxidase activity, which is much lower than the catalase activity, no peroxidase activity with 3-aminophenol, 2,4,6-trichlorophenol, and 3-nitrophenol
-
-
?
additional information
?
-
-
BNC does not show any peroxidatic activity with 4-aminoantipyrine or pyrogallol as substrate
-
-
?
additional information
?
-
-
the enzyme does not interact with Brij 35 micelles, enzyme exhibits superactivity in the reverse micells formed by 0.1 M Brij 30 in heptane, isooctane, and dodecane, but not in decaline
-
-
?
additional information
?
-
-
adenine deaminase, EC 3.5.4.2, from the amidohydrolase superfamily of enzymes catalyzes the conversion of adenine to hypoxanthine and ammonia. But it also catalyzes the catalase reaction converting H2O2 to H2O and O2. [MnII/MnII]-ADEec is active as a deaminase but not as a catalase. In contrast, [FeII/FeII]-ADEec catalyzes both reactions
-
-
?
additional information
?
-
-
regulation of enzyme expression and activity by drying occurs on transcriptional level, increase in enzyme activity during drying is associated with an decrease of H2O2 level and lipid peroxidation
-
-
?
additional information
?
-
-
the enzyme contains a unique tetra-lysine motif at the C-terminus which probably is required for interaction with protein KapA
-
-
?
additional information
?
-
-
the enzyme has negligible inhibitory effects on endothelium-dependent relaxations in mouse isolated aorta and small mesenteric artery which are not caused by H2O2, endothelium-independent relaxations are caused by H2O2 and are abolished by the enzyme, overview
-
-
?
additional information
?
-
-
the bifunctional catalase with phenol oxidase activity catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds
-
-
?
additional information
?
-
-
the bifunctional catalase with phenol oxidase activity catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds
-
-
?
additional information
?
-
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
?
additional information
?
-
-
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
?
additional information
?
-
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
?
additional information
?
-
-
peroxidase and catalase activities are involved in direct adventitious shoot formation induced by thidiazuron in zygotic embryos
-
-
?
additional information
?
-
-
CcmC is a key determinant for cytochrome c biogenesis, pyoverdine maturation, and expression of some quorum sensing-regulated traits
-
-
?
additional information
?
-
-
the enzyme is involved in protection against peroxides and oxidative DNA damage, it is downregulated in biofilm cultures of Pseudomonas aeruginosa, that display up to a 105fold increase in mutability compared with planktonic cultures
-
-
?
additional information
?
-
-
no detectable peroxidase activity
-
-
?
additional information
?
-
-
no detectable peroxidase activity
-
-
?
additional information
?
-
-
enzyme is easiliy reduced by dithionite, no peroxidase activity with o-dianisidine and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
additional information
?
-
-
2 enzymes TvC-I and TvC-II do not show peroxidase ctivity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
?
-
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
via intermediate Compound I
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
H2O2
O2 + H2O
-
-
-
?
H2O2
O2 + H2O
Beta vulgaris var. cicla
-
-
-
?
H2O2
O2 + H2O
-
no peroxidase activity
-
?
H2O2
O2 + H2O
-
involved in acatalasemia
-
?
H2O2
O2 + H2O
Capra capra
-
-
-
?
H2O2
O2 + H2O
Capra capra
-
-
-
?
H2O2
O2 + H2O
-
no peroxidase-activity
-
?
H2O2
O2 + H2O
-
monofunctional catalase
-
?
H2O2
O2 + H2O
Cucurbita sp.
-
-
-
?
H2O2
O2 + H2O
-
two monofunctional, one bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
two monofunctional, one bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
detoxification enzyme, enzyme protects the cell against high concentrations of peroxide
-
-
?
H2O2
O2 + H2O
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
one monofunctional, two bifunctional catalases
-
?
H2O2
O2 + H2O
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
monofunctional catalase
-
?
H2O2
O2 + H2O
-
enzyme is responsible for prevention of dehydration-related oxidative damage during seed desiccation, H2O2 may play a role for enzyme expression regulation and in the transduction pathway
-
-
?
H2O2
O2 + H2O
-
detoxification and protection enzyme
-
-
?
H2O2
O2 + H2O
-
enzyme is responsible for the protection of the Helicobacter pylori cells against phagocyte attack in the gastric mucosa by disumtation of H2O2
-
-
?
H2O2
O2 + H2O
-
detoxification and protection enzyme
-
-
?
H2O2
O2 + H2O
-
abnormal reaction kinetics
-
?
H2O2
O2 + H2O
-
abnormal reaction kinetics
-
?
H2O2
O2 + H2O
-
involved in acatalasemia
-
?
H2O2
O2 + H2O
-
regulator of H2O2-levels or protective function for hemoglobin or other SH-proteins
-
?
H2O2
O2 + H2O
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
Kloeckera sp.
-
-
-
?
H2O2
O2 + H2O
Kloeckera sp. 2201
-
-
-
?
H2O2
O2 + H2O
monofunctional catalase
-
?
H2O2
O2 + H2O
-
no peroxidase activity
-
?
H2O2
O2 + H2O
two monofunctional catalases, Cat-1 and Cat-3, one catalase-peroxidase enzyme, Cat-2
-
?
H2O2
O2 + H2O
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
H2O2
O2 + H2O
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
H2O2
O2 + H2O
-
detoxification enzyme, enzyme is naturally adapted to the cold climate of the arctic tundra
-
-
?
H2O2
O2 + H2O
-
detoxification enzyme, enzyme is naturally adapted to the cold climate of the arctic tundra
-
-
?
H2O2
O2 + H2O
-
one catalase-peroxidase, one catalase enzyme
-
?
H2O2
O2 + H2O
-
KatA catalase important for resistance of planctonic and biofilm cells to H2O2
-
?
H2O2
O2 + H2O
-
essential for optimal resistance to H2O2. KatB was not produced during the normal growth cycle. Catalase activity is greater in nonmucoid than in mucoid, alginate-producing organisms. When exposed to hydrogen peroxide and, to a greater extent, paraquat, total catalase activity was elevated 7fold to 16fold, respectively
-
-
?
H2O2
O2 + H2O
detoxification enzyme
-
-
?
H2O2
O2 + H2O
detoxification enzyme
-
-
?
H2O2
O2 + H2O
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
H2O2 decomposition is accompanied by enzyme inactivation which can be minimized in vitro by immobilization of the enzyme
-
-
?
H2O2
O2 + H2O
-
H2O2 decomposition is accompanied by enzyme inactivation which can be minimized in vitro by immobilization of the enzyme
-
-
?
H2O2
O2 + H2O
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
protective role of the enzyme
-
-
?
H2O2
O2 + H2O
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
-
three isoenzymes, Cat-1, Cat-2 and Cat-3
-
?
additional information
?
-
-
adenine deaminase, EC 3.5.4.2, from the amidohydrolase superfamily of enzymes catalyzes the conversion of adenine to hypoxanthine and ammonia. But it also catalyzes the catalase reaction converting H2O2 to H2O and O2. [MnII/MnII]-ADEec is active as a deaminase but not as a catalase. In contrast, [FeII/FeII]-ADEec catalyzes both reactions
-
-
?
additional information
?
-
-
regulation of enzyme expression and activity by drying occurs on transcriptional level, increase in enzyme activity during drying is associated with an decrease of H2O2 level and lipid peroxidation
-
-
?
additional information
?
-
-
the enzyme has negligible inhibitory effects on endothelium-dependent relaxations in mouse isolated aorta and small mesenteric artery which are not caused by H2O2, endothelium-independent relaxations are caused by H2O2 and are abolished by the enzyme, overview
-
-
?
additional information
?
-
-
the bifunctional catalase with phenol oxidase activity catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds
-
-
?
additional information
?
-
-
the bifunctional catalase with phenol oxidase activity catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds
-
-
?
additional information
?
-
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
?
additional information
?
-
-
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
?
additional information
?
-
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
?
additional information
?
-
-
peroxidase and catalase activities are involved in direct adventitious shoot formation induced by thidiazuron in zygotic embryos
-
-
?
additional information
?
-
-
CcmC is a key determinant for cytochrome c biogenesis, pyoverdine maturation, and expression of some quorum sensing-regulated traits
-
-
?
additional information
?
-
-
the enzyme is involved in protection against peroxides and oxidative DNA damage, it is downregulated in biofilm cultures of Pseudomonas aeruginosa, that display up to a 105fold increase in mutability compared with planktonic cultures
-
-
?
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1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one
-
-
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
inhibition is pH-dependent. Lowest concentration where inhibition is observed is 1.2 mM at pH 4.5, 0.6 mM at pH 4.3, 0.3 mM at pH 4.0
3-amino-1H-1,2,4-triazole
4-aminoantipyrine
-
inhibition of catalase activity
5,5-dithiobis(2-nitrobenzoic acid)
Capra capra
-
complete inhibition at 0.4 mM
acetic acid
-
in vitro inhibitor
ascorbate
-
in vitro inhibitor
Ba2+
-
partial inhibition at 2 mM
BO3-
Capra capra
-
weak inhibition at 1 mM
CaCl2
-
irreversible loss of activity at 2 M
Co2+
-
partial inhibition at 2 mM
Cr2+
1 mM, 3% of initial activity
dinitrosyl iron complex
-
decrease in enzyme activity without changing the mechanism. The inhibition efficiency is elevated by two orders of magnitude and also increases with decrease in pH in the presence of 150 mM chloride or 150 mM bromide or 0.050 mM thiocyanate. In presence of oxyhemoglobin plus o-phenanthroline, the inhibitory effect is sharply attenuated
eicosapentaenoic acid
-
the incubation of Jurkat cells with 0.1 mM eicosapentaenoic acid causes a significant decrease of catalase activity but not of protein or mRNA content
Endogenous inhibitor
-
purified on catalase-Sepharose from bovine, different inhibition sensitivities for three isoforms
-
epigallocatechin gallate
-
-
ethane-1,2-diol
-
activity at 30-60°C in presence of ethanol-1,2-diol, overview
ethanol
-
in vitro inhibitor
ethanol/chloroform
25%/15%, 71% residual activity
formaldehyde
Capra capra
-
non-competitive inhibition
formic acid
-
in vitro inhibitor
gamma-linolenic acid
-
the incubation of Jurkat cells with 0.05 mM gamma-linolenic acid causes a significant decrease of catalase activity but not of protein or mRNA content
Hg2+
10 mM, 14% residual activity
histidine
-
10 mM histidine reduces activity by 19%
hydroxyl radicals
inactivation of isoform Cat-1
Hydroxylamine hydrochloride
indole acetic acid
Capra capra
-
non-competitive inhibition
inositol phosphoglycan-like compound from Bos taurus thyroid gland
-
produced by the hydrolysis of the membrane-bound glycosyl phosphoinositides, noncompetitive inhibition. 50% residual activity, the site of action is not the prosthetic group
-
inositol phosphoglycan-like compound from Escherichia coli
-
produced by the hydrolysis of the membrane-bound glycosyl phosphoinositides, noncompetitive inhibition. 50% residual activity, the site of action is not the prosthetic group
-
KNO2
-
37% inhibition at 1 mM
KNO3
-
14% inhibition at 1 mM
L-cysteine
Capra capra
-
35% inhibition at 3.3 mM
L-Glutamic acid
Beta vulgaris var. cicla
-
84% inhibition at 30 mM
L-lactic acid
Capra capra
-
63% inhibition at 25 mM
L-Malic acid
Capra capra
-
50% inhibition at 6 mM
L-tryptophan
Capra capra
-
80% inhibition at 1.6 mM
L-tyrosine
Capra capra
-
80% inhibition at 5 mM
linoleic acid
-
the incubation of Jurkat cells with 0.1 mM linoleic acid causes a significant decrease of catalase activity but not of protein or mRNA content
Maleic acid
Capra capra
-
51% inhibition at 0.8 mM
methanol
-
in vitro inhibitor
MgCl2
-
irreversible loss of activity at 2 M
N-bromosuccinimide
Capra capra
-
complete inhibition at 3.34 mM
N-ethylmaleimide
Capra capra
-
complete inhibition at 18.3 mM
NO
generated from 1-(N,N-diethylamino)diazen-1-ium-1,2-diolate, competitive inhibitor, nitrosylated catalase is kinetically labile, NO tends to dissociate rapidly from the active site, binding structure, overview. Kinetic analysis of dissociation of NO from the enzyme-inhibitor complex
oleic acid
-
the incubation of Jurkat cells with 0.2 mM oleic acid causes a significant decrease of catalase activity but not of protein or mRNA content
oxalic acid
Capra capra
-
51% inhibition at 4 mM
p-chloromercuribenzoate
Capra capra
-
complete inhibition at 0.33 mM, summation effect with 2-mercaptoethanol
palmitic acid
-
the incubation of Jurkat cells with 0.2 mM palmitic acid causes a significant decrease of catalase activity but not of protein or mRNA content
pentaerythritol tetranitrate
-
-
phenol
-
inhibition of catalase activity
pyocyanin
-
may decrease cellular catalase activity via both transcriptional regulation and direct inactivation of the enzyme
Pyruvic acid
Capra capra
-
16% inhibition at 5 mM
SDS
Beta vulgaris var. cicla
-
55% inhibition at 0.01%
SO3-
Capra capra
-
weak inhibition at 4 mM
Sodium dithionite
-
inhibitory
stearic acid
-
the incubation of Jurkat cells with 0.2 mM stearic acid causes a significant decrease of catalase activity but not of protein or mRNA content
Urea
Beta vulgaris var. cicla
-
50% inhibition at 4 M in 3.5 min
2-mercaptoethanol
-
-
2-mercaptoethanol
Beta vulgaris var. cicla
-
50% inhibition at 3 mM
2-mercaptoethanol
Capra capra
-
complete inhibition at 23 mM, summation effect with p-chloromercuribenzoate
2-mercaptoethanol
Capra capra
-
complete inactivation
2-mercaptoethanol
-
36% inhibition at 1 mM
2-mercaptoethanol
-
rapid inactivation
2-mercaptoethanol
30 mM, 14% residual activity
2-mercaptoethanol
-
slight inhibition for all three isoforms at 10 mM
3-Amino-1,2,4-triazole
1 mM, 86% inhibition
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
inhibitory. Inhibition of extracellular catalase activity leads to a striking inactivation of secreted cysteine cathepsins
3-Amino-1,2,4-triazole
-
potent catalase inhibitor, maximum inhibition at 10 mM
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
very weak inhibitor of erythrocytic CAT activity
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
3-amino-1,2,4-triazole at concentrations of 10 mM has no inhibition on the activity
3-Amino-1,2,4-triazole
specific irreversible inhibitor, complete inhibition at 20 mM
3-Amino-1,2,4-triazole
-
10 mM, 81% inhibition
3-Amino-1,2,4-triazole
-
10 mM, 26% residual activity
3-Amino-1,2,4-triazole
500 microM reduces the reactivity of catalase to 50%
3-Amino-1,2,4-triazole
4 mM, 38% residual activity
3-Amino-1,2,4-triazole
-
strong inhibition
3-Amino-1,2,4-triazole
-
TvC-I and TvC-II, inactivation
3-Amino-1,2,4-triazole
strong inhibition
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
retains 38% of its initial activity in the presence of 40 mM
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
reaction occurs only in vivo, irreversible inhibition
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
not inhibitory
3-amino-1H-1,2,4-triazole
-
isoenzyme HPI: 25% inhibition at 10 mM, isoenzyme HPII: 70-80% inhibition at 10 mM
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
33% inactivation at 20 mM in 2.5 h
3-amino-1H-1,2,4-triazole
-
not inhibitory
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
exclusive in vivo inhibitor
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
IC50: 80 mM
3-amino-1H-1,2,4-triazole
-
59% inhibition at 20 mM
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
50% inactivation in 1 h
3-amino-1H-1,2,4-triazole
-
no effect on catalase-peroxidase enzyme
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
98% inhibition at 10 mM
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
not inhibitory
3-amino-1H-1,2,4-triazole
-
90% inhibition at 20 mM
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
56% inactivation at 20 mM
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
-
strong inhibition for isoforms Cat-1, Cat-2, 32% inhibition for isoform Cat-3 at 10 mM
azide
-
-
azide
-
catalase activity at pH 4.5, in comparison to the other two pH optima at 6.5 and 10.0, has highest sensitivity to azide
azide
-
very strong inhibitor of erythrocytic CAT but a relatively weak CAT inhibitor in human hemolysates
azide
irreversible inhibitor, effective at concentrations less than1 mM
azide
10 mM, no residual activity
BrCN
-
selective modification of the active site, only in vitro
Cd2+
-
after 48 h of exposure to 0.1 mM Cd2+, germination is unaltered, but root length and catalase activity are significantly reduced. 24 h post exposure, catalase activity is restored or even enhanced. The mechanism of catalse inactivation by Cd2+ involves oxidation of the protein structure. Cd2+ induces overexpression of catalase isoforms CatA1 and CatA2 in cotyledon and root
Cd2+
-
Cd2+ has a small role in the reduction of CAT activity
CN-
-
strong inhibition
CN-
-
TvC-I and TvC-II, at micromolar range
Cu2+
Beta vulgaris var. cicla
-
47% inhibition at 0.2 mM
Cu2+
Capra capra
-
55% inhibition at 0.2 mM
Cu2+
1 mM, 7% of initial activity
Cu2+
10 mM, 52% residual activity
cyanide
-
catalase activity at pH 4.5, in comparison to the other two pH optima at 6.5 and 10.0, has lowest sensitivity to cyanide
cyanide
-
most potent inhibitor of root nodule catalase
cyanide
-
most potent inhibitor of root nodule catalase
cyanide
10 mM, no residual activity
Dithionite
-
-
dithiothreitol
Beta vulgaris var. cicla
-
50% inhibition at 10 mM
dithiothreitol
Capra capra
-
complete inhibition at 33 mM
dithiothreitol
Capra capra
-
complete inactivation
dithiothreitol
-
the activity can be inhibited by 75% by addition of 5 mM dithiothreitol
dithiothreitol
-
slight inactivation
dithiothreitol
-
slight inhibition at 10 mM for all three isoforms
EDTA
-
10 mM EDTA reduces activity by 27%
F-
-
-
Fe2+
Beta vulgaris var. cicla
-
14% inhibition at 1.5 mM
Glutaraldehyde
Beta vulgaris var. cicla
-
24% inactivation at 8%
Glutaraldehyde
-
the presence of trace amount of glutaraldehyde in immobilization medium causes the catalase activity to decline
H2O2
Beta vulgaris var. cicla
-
55% inactivation at 10 mM in 60 min
H2O2
-
inactivation at temperatures above 40°C, overview
H2O2
-
catalase activity at pH 4.5 is inhibited by 5 mM H2O2 and above
H2O2
-
inactivation half-life: 20-30 min at 2 mM
H2O2
-
excess H2O2 inhibits the enzyme. In the presence of excess H2O2, [FeII/FeII]-ADEec rapidly loses its ability to deaminate adenine
H2O2
-
50% inhibition for catalase at 4.5 mM, for peroxidase at 0.4 mM
H2O2
-
rapid inactivation above 0.1 M
H2O2
Kloeckera sp.
-
inhibition above 50 mM
H2O2
-
H2O2 causes 17% inhibition at 80 mM
H2O2
substrate inhibition, no detectable activity above 60 mM H2O2
H2O2
-
inactivation half-life: 20-30 min at 2 mM
H2O2
-
inhibitory above 60 mM
hydroxylamine
-
-
hydroxylamine
-
85.1% inactivation at 0.005 mM
hydroxylamine
-
in vitro inhibitor
hydroxylamine
-
99% inhibition of catalase activity and 17% inhibition of peroxidase activity at 0.1 mM, complete inhibition of catalase activity and 56% inhibition of peroxidase activity at 1 mM
hydroxylamine
-
50% inhibition for catalase at 0.002 mM, for peroxidase at 0.078 mM
hydroxylamine
-
0.00011 mM, 50% inhibition
Hydroxylamine hydrochloride
0.05 mM, 78% inhibition
Hydroxylamine hydrochloride
-
strong inhibition
iodoacetamide
Beta vulgaris var. cicla
-
50% inhibition at 2 mM
iodoacetamide
Capra capra
-
complete inhibition at 11.7 mM
KCN
-
-
KCN
Beta vulgaris var. cicla
-
50% inhibition at 0.65 mM
KCN
-
72.5% inactivation at 0.005 mM
KCN
-
effective inhibition
KCN
-
inhibitory. Inhibition of extracellular catalase activity leads to a striking inactivation of secreted cysteine cathepsins
KCN
50% inhibition at 0.08 mM
KCN
-
74% inhibition of catalase activity and 86% inhibition of peroxidase activity at 0.1 mM, 96% inhibition of catalase and peroxidase activity at 1 mM
KCN
isoform Cat-2, IC50: 0.146 mM, catalase activity, IC50: 0.168 mM, peroxidase activity
KCN
-
97% inhibition at 1 mM
KCN
-
50% inhibition of both catalase and peroxidase activities at 0.02 mM
KCN
-
73% inactivation at 0.01 mM
KCN
-
strong inhibition for all three isoforms at 1 mM
L-aspartic acid
Beta vulgaris var. cicla
-
92% inhibition at 30 mM
L-aspartic acid
Capra capra
-
25% inhibition at 16 mM
Mn2+
Beta vulgaris var. cicla
-
56% inhibition at 1 mM
Mn2+
Capra capra
-
30% inhibition at 1 mM
Mn2+
1 mM, 50% of initial activity
NaCl
-
50 mM, 17% residual activity in leaf, 54% residual activity in nodule
NaCl
-
50 mM, 30% residual activity in leaf, 24% residual activity in nodule
NaCN
-
50% inhibition at 300 mM
NaCN
-
50% inhibition at 60 mM
NaCN
-
50% inhibition at 35 mM
NaCN
-
50% inhibition at 30 mM
NaCN
-
50% inhibition at 15 mM
NaCN
-
50% inhibition at 9 mM
NaCN
-
50% inhibition at 150 mM
NaCN
-
50% inhibition at 20 mM
NaCN
-
50% inhibition at 25 mM
NaCN
-
50% inhibition at 60 mM
NaCN
-
50% inhibition at 80 mM
NaCN
-
50% inhibition at 12 mM
NaCN
-
50% inhibition at 12 mM
NaCN
-
50% inhibition at 35 mM
NaCN
-
50% inhibition at 80 mM
NaCN
-
50% inhibition at 15 mM
NaN3
-
-
NaN3
Beta vulgaris var. cicla
-
50% inhibition at 0.0018 mM
NaN3
Capra capra
-
non-competitive inhibition
NaN3
-
76.4% inactivation at 0.005 mM
NaN3
-
effective inhibition
NaN3
50% inhibition at 0.001 mM
NaN3
-
68% inhibition of catalase activity and 90% inhibition of peroxidase activity at 0.1 mM, 92% inhibition of catalase activity and 99% inhibition of peroxidase activity at 1 mM
NaN3
-
98% inhibition at 1 mM
NaN3
-
complete inhibition at 0.01 mM
NaN3
-
50% inhibition for catalase at 0.15 mM, for peroxidase at 0.73 mM
NaN3
-
TvC-I and TvC-II, at micromolar range
NaN3
-
97% inactivation at 0.1 mM
NaN3
-
strong inhibition for all three isoforms at 0.001 mM
nitrite
-
efficiency of inhibition sharply increases in presence of chloride, bromide, thiocyanate. Inhibition involves NO+ ions rather than NO molecules due to nitrosation of enzyme, and the enhancement of inhibition in presence of halide ions may be caused by nitrosyl halide formation
nitrite
nitrite effectively reduces inactive catalase compound II to the ferric enzyme. Presence of chloride significantly enhances nitrite-induced catalase inhibition
nitrite
-
in vitro inhibitor
nitrite
-
uncompetitive inhibitor
S-nitrosoglutathione
-
-
Sodium azide
0.05 mM, 69% inhibition
Sodium azide
-
strong inhibition
Sodium azide
only 10% inhibition at 1 mM
Sodium azide
-
0.00052 mM, 50% inhibition
Sodium cyanide
-
maximum inhibition in the catalase activity is noted in liver on day 4 (about 82.6%) and minimum inhibition is observed in brain on day 1 (about 18.9%), while all exposure periods witnessed continuously decreases catalase activity in all the tissues as compared to control
Sodium cyanide
-
0.0115 mM, 50% inhibition
additional information
-
detailed comparison of inhibitors
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
enzyme inhibition by flavonoids, structure-function relationship, overview
-
additional information
-
detailed comparison of inhibitors
-
additional information
not inhibited by exposure of cells to 3-amino-1,2,4-triazole
-
additional information
-
not inhibited by exposure of cells to 3-amino-1,2,4-triazole
-
additional information
-
incubation in the light clearly inhibits the activity of catalase, about 40% of the activity is lost within 2 h and only 25% remain after 5 h of incubation in the light
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
oxygenation of active site residues, inhibiting catalase activity, occurs via release of hydroxyl radicals
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
tissue necrosis factor-alpha treatment causes downregulation of catalase expression in MCF-7, Caco-2 and Hct-116 cancer cell lines
-
additional information
-
acetazolamide and nitrate at concentrations up to 0.1 mM do not inhibit erythrocytic CAT activity
-
additional information
-
detailed comparison of inhibitors
-
additional information
enzyme is not inhibited by presence of 5 mM sodium azide
-
additional information
-
enzyme is not inhibited by presence of 5 mM sodium azide
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
telomerase deficiency reduces catalase activity
-
additional information
exposure to white light of nearly 0.800 mE per square meter and second for 120 min at 25°C inactivates the wild-type enzyme activity by about 50%
-
additional information
-
exposure to white light of nearly 0.800 mE per square meter and second for 120 min at 25°C inactivates the wild-type enzyme activity by about 50%
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
detailed comparison of inhibitors
-
additional information
no effect by 0.01 mM hydrogen peroxide or 100 nM paraquat
-
additional information
-
no effect by 0.01 mM hydrogen peroxide or 100 nM paraquat
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
detailed comparison of inhibitors
-
additional information
-
no inhibition by H2O2 up to 450 mM
-
additional information
-
no reduction of TvC-II by dithionite
-
additional information
-
Ni2+, Ca2+, Mg2+ and Mn2+ have both enhancing and inhibitory effects
-
additional information
-
detailed comparison of inhibitors
-
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3-Amino-1,2,4-triazole
-
18% activation of catalase activity and unaltered peroxidase activity at 0.1 mM, 56% activation of catalase activity and 21% activation of peroxidase activity at 10 mM
all-trans-retinol
-
treatment of cultured Sertoli cells leads to activation of catalase by increasing its protein content, but without alteration of its mRNA expression. Retinol treatment also increases cell lipoperoxidation and intracellular reactive species production. All effects induced by retinol are inhibited by the antioxidant Trolox
AnkB
-
the periplasmic ankyrin-like protein is required for optimal catalase B (KatB) activity and resistance to hydrogen peroxide
-
chloramphenicol
-
24% activation at 0.1 mM in 1 min
Fe2+
-
the catalase activity shows a strong positive dependence on the intracellular iron concentration in Fe-replete medium and low activity under Fe-limited growth conditions
hemin
-
0.002-0.01 mM required for half-maximal to maximal enzyme production
Ibuprofen
-
induces a variety of enzymes associated with the oxidative stress response, including catalase, glucose-6-phosphate-dehydrogenase, and aldehyde reductase in a dose-related manner
Leucine-enkephalin
-
the intracellular and extracellular CAT activity is increased with increasing concentration (0.001-0.05 mg/ml) of leucine-enkephalin
NaCl
-
highest activity for catalase at 2 M, for peroxidase at 1 M
NADPH
addition of NADPH stimulates the activity of CatP in a dose-dependent manner most likely by preventing the inactivation from oxidative damage through its substrate H2O2
peracetic acid
-
low doses induce enzyme promoter activity and increase total enzymic activity in cell extracts
progesterone receptor isoform B
-
-
-
retinal
-
retinal (0.007 and 0.014 mM) increases CAT activity after 24 h of treatment
retinoic acid
-
retinoic acid (100 nM and 0.001 mM) increases CAT activity after 24 h of treatment
Tris
-
stimulation at 10 mM
bensulfuron methyl
-
-
bensulfuron methyl
-
the catalase activity is higher with bensulfuron-methyl than with quinclorac
imidazole
-
2fold activation at 10 mM
imidazole
-
up to 20 mM: enhancement of Vmax
quinclorac
-
-
Sodium arsenate
-
CAT activity is activated by 200 mM arsenate up to 120% compared to the control
Sodium arsenate
-
CAT activity is activated by 200 mM arsenate up to 133% compared to the control
Sodium arsenate
-
CAT activity is activated by 200 mM arsenate up to 300% compared to the control
additional information
-
strong induction of both catalase and bifunctional catalase-peroxidase by raising the intracelllar H2O2 level with paraquat, but not by exogenous H2O2
-
additional information
-
stimulation of the enzyme by natural and artificial drying
-
additional information
-
the periplasmic enzyme is dependent on the twin-arginine target protein KapA for activity
-
additional information
-
increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
-
additional information
-
addition of non-toxic concentrations of H2O2 to cultured THP-1 cells neither influences catalase activity nor mRNA expression levels and activity of cathepsins
-
additional information
-
3alpha-hydroxy tibolone has no activating effect
-
additional information
-
increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
-
additional information
H2O2 induces enzyme expression
-
additional information
-
H2O2 induces enzyme expression
-
additional information
the activity of CatA increases when the fungus is grown under endogenous oxidative stress, i.e. in oleic acid. CatP and PbCatC demonstrat no alteration in activity under these conditions
-
additional information
-
the activity of CatA increases when the fungus is grown under endogenous oxidative stress, i.e. in oleic acid. CatP and PbCatC demonstrat no alteration in activity under these conditions
-
additional information
in planta, activity increases dramatically about 8 h after infection of host tobacco plants
-
additional information
in planta, activity increases dramatically about 8 h after infection of host tobacco plants
-
additional information
in planta, activity increases dramatically about 8 h after infection of host tobacco plants
-
additional information
-
in planta, activity increases dramatically about 8 h after infection of host tobacco plants
-
additional information
no effect by 0.01 mM hydrogen peroxide or 100 nM paraquat, 3.4fold increase in intracellular activity by elimination of thiosulfate from the aerobic growth medium
-
additional information
-
no effect by 0.01 mM hydrogen peroxide or 100 nM paraquat, 3.4fold increase in intracellular activity by elimination of thiosulfate from the aerobic growth medium
-
additional information
daidzein shows a significant induction of catalase promoter activity at 0.1 mM in a reporter gene assay and at 0.2 mM in Northern blot experiments
-
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83
methanol
Kloeckera sp.
-
peroxidase activity
0.048
o-Dianisidine
-
peroxidase activity, pH 4.5, 30°C
additional information
additional information
-
0.025
H2O2
-
-
0.0847
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0)
0.0867
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0)
0.14
H2O2
-
peroxidase activity
0.64
H2O2
-
second isoform, 25°C, pH 6.5
0.64
H2O2
-
isoenzyme with optimum at pH 6.5
0.67
H2O2
-
catalase activity, pH 8.5, 30°C
1
H2O2
-
first isoform, 25°C, pH 4.5
1
H2O2
-
isoenzyme with optimum at pH 4.5
1.47
H2O2
-
peroxidase activity, pH 4.5, 30°C
3
H2O2
-
peroxidase activity, pH 7.0, 25°C
3.5
H2O2
-
wild-type, pH 7.0, 23°C
3.7
H2O2
-
catalase activity
4
H2O2
mutant L189W/H225T
5.2
H2O2
-
mutant Y111A, pH 7.0, 23°C
6.3
H2O2
-
catalase activity, pH 7.0, 30°C
10
H2O2
-
isoenzyme HPII, pH 10.5
10
H2O2
pH 7.0, 60°C, mutant enzyme I313F
10
H2O2
pH 7.0, 60°C, wild-type enzyme
10.5
H2O2
KTL38510
wild-type, pH 7.5, 35°C
11
H2O2
pH 7.0, 60°C, mutant enzyme L321A
13.4
H2O2
-
third isoform, 25°C, pH 10.0
13.4
H2O2
-
isoenzyme with optimum at pH 10.0
13.74
H2O2
-
recombinant wild-type enzyme, pH 7.0, 25°C
18.2
H2O2
-
isoenzyme HPII, pH 6.8
20
H2O2
pH 7.0, 60°C, mutant enzyme E316F
24
H2O2
-
in 20 mM Tris-HCl buffer (pH 9.0), at 30°C
25
H2O2
Kloeckera sp.
-
catalase activity
27
H2O2
-
catalase activity, pH 7.0, 25°C
27.73
H2O2
-
pH 7.0, 25°C, free enzyme
28.6
H2O2
-
free catalase, in 50 mM phosphate buffer pH 7.0, at 25°C
31.42
H2O2
-
pH 7.0, 25°C, immobilized enzyme
33
H2O2
pH 7.0, 60°C, mutant enzyme E316H
40
H2O2
pH 7.0, 60°C, mutant enzyme H246W
41.5
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0), at 4°C
43.6
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0), at 25°C
50
H2O2
Beta vulgaris var. cicla
-
-
50
H2O2
pH 7.0, 60°C, mutant enzyme I314F
61
H2O2
-
pH and temperature not specified in the publication
67
H2O2
pH 7.0, 60°C, mutant enzyme V536A
78
H2O2
in 50 mM NaH2PO4-Na2HPO4 buffer (pH 7.0) at 20°C
95.9
H2O2
-
catalase covalently immobilized onto Eupergit C, in 50 mM phosphate buffer pH 7.0, at 25°C
101
H2O2
-
pH 7.0, temperature not specified in the publication
158.8
H2O2
-
catalase from Penicillium piceum strain F-648
600
H2O2
pH 7.0, 60°C, mutant enzyme V536W
1722
H2O2
-
enzyme immobilized on florisil
additional information
additional information
-
stopped-flow kinetics, 25°C, pH 7.0
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetic modeling, overview
-
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0.00122
(+)-catechin
Bos taurus
-
pH 7.0, 23°C
0.049
(-)-epigallocatechin
Bos taurus
-
pH 7.0, 23°C
20
3-Amino-1,2,4-triazole
Homo sapiens
-
erythrocytic CAT, at 25°C, pH not specified in the publication
80
3-amino-1H-1,2,4-triazole
Methanosarcina barkeri
IC50: 80 mM
0.0166
apigenin
Bos taurus
-
pH 7.0, 23°C
0.033
Astragalin
Bos taurus
-
pH 7.0, 23°C
2
beta-mercaptoethanol
Bacillus sp. (in: Bacteria)
-
-
0.056
catechol
Bos taurus
-
pH 7.0, 23°C
0.000029
epicatechin gallate
Bos taurus
-
pH 7.0, 23°C
0.00033
epigallocatechin gallate
Bos taurus
-
pH 7.0, 23°C
0.02
galangin
Bos taurus
-
pH 7.0, 23°C
0.046
gallic acid
Bos taurus
-
pH 7.0, 23°C
0.0003 - 0.0044
hydroxylamine
0.0744
kaempferol
Bos taurus
-
pH 7.0, 23°C
0.0116
luteolin
Bos taurus
-
pH 7.0, 23°C
0.000014
myricetin
Bos taurus
-
pH 7.0, 23°C
0.001
NaN3
Methanosarcina barkeri
IC50: 0.001 mM
0.0018
pyrogallol
Bos taurus
-
pH 7.0, 23°C
0.045
quercetin
Bos taurus
-
pH 7.0, 23°C
0.036
rutin
Bos taurus
-
pH 7.0, 23°C
0.345
Sodium azide
Bos taurus
-
pH 7.0, 23°C
0.0000002
azide
Homo sapiens
-
erytrocyctic CAT, at 25°C, pH not specified in the publication
0.0004
azide
Rhodospirillum rubrum
-
pH 7.0, 25°C
0.0015
azide
Paracoccidioides brasiliensis
in 50 mM sodium phosphate buffer, pH 7.8, at 37°C
0.0017
azide
Bacillus sp. (in: Bacteria)
-
-
0.009
azide
Homo sapiens
-
hemolysate CAT, at 25°C, pH not specified in the publication
0.01
azide
Brassica oleracea var. gongylodes
-
first isoform, 25°C, pH 4.5
0.01
azide
Brassica oleracea
-
isoenzyme with optimum at pH 4.5
0.075
azide
Brassica oleracea var. gongylodes
-
second isoform, 25°C, pH 6.5
0.075
azide
Brassica oleracea
-
isoenzyme with optimum at pH 6.5
1
azide
Brassica oleracea var. gongylodes
-
third isoform, 25°C, pH 10.0
1
azide
Brassica oleracea
-
isoenzyme with optimum at pH 10.0
0.0088
cyanide
Rhodospirillum rubrum
-
pH 7.0, 25°C
0.2
cyanide
Brassica oleracea var. gongylodes
-
second isoform, 25°C, pH 6.5
0.2
cyanide
Brassica oleracea
-
isoenzyme with optimum at pH 6.5
2
cyanide
Brassica oleracea var. gongylodes
-
third isoform, 25°C, pH 10.0
2
cyanide
Brassica oleracea
-
isoenzyme with optimum at pH 10.0
12
cyanide
Brassica oleracea var. gongylodes
-
first isoform, 25°C, pH 4.5
12
cyanide
Brassica oleracea
-
isoenzyme with optimum at pH 4.5
0.0003
hydroxylamine
Bacillus sp. (in: Bacteria)
-
-
0.002
hydroxylamine
Paracoccidioides brasiliensis
in 50 mM sodium phosphate buffer, pH 7.8, at 37°C
0.0044
hydroxylamine
Rhodospirillum rubrum
-
pH 7.0, 25°C
0.005
KCN
Methanosarcina barkeri
IC50: 0.005 mM
0.168
KCN
Neurospora crassa
isoform Cat-2, IC50: 0.146 mM, catalase activity, IC50: 0.168 mM, peroxidase activity
0.00095
nitrite
Bos taurus
pH 5.0, temperature not specified in the publication
0.007
nitrite
Bos taurus
pH 6.0, temperature not specified in the publication
0.009
nitrite
Homo sapiens
-
erythrocytic CAT, at 25°C, pH not specified in the publication
0.063
nitrite
Bos taurus
pH 7.0, temperature not specified in the publication
0.162
nitrite
Bos taurus
pH 7.4, temperature not specified in the publication
0.75
nitrite
Homo sapiens
-
hemolysate CAT, at 25°C, pH not specified in the publication
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0.004
-
peroxidase activity after 5 days of cell culture
0.016
-
peroxidase activity after 10 days of cell culture
0.033
pH 7.0, 60°C, mutant enzyme H246W
0.085
pH 7.0, 60°C, mutant enzyme V536W
0.086
-
peroxidase activity after 5 days of cell culture in presence of 0.1 mM paraquat
0.092
pH 7.0, 60°C, mutant enzyme I314F
0.107
pH 7.0, 60°C, mutant enzyme L321A
0.163
pH 7.0, 60°C, mutant enzyme E316H
0.164
-
peroxidase activity after 10 days of cell culture in presence of 0.1 mM paraquat
0.173
pH 7.0, 60°C, mutant enzyme E316F
0.213
pH 7.0, 60°C, wild-type enzyme
0.232
pH 7.0, 60°C, mutant enzyme I313F
0.236
pH 7.0, 60°C, mutant enzyme V536A
0.94
-
purified enzyme, peroxidase activity, mixed-type
1.5
-
about, cell lysates of wild-type Caco-2 cells
104.3
-
peroxidase activity
1134
after 3.1fold purification, in 50 mM sodium phosphate buffer, pH 7.8, at 37°C
1145
-
purified enzyme, catalase activity
117
-
partially purified TvC-I
120000
half-maximal activity at 30 mM H2O2
130
isoform Cat-2, peroxidase activity with 3,3-diaminobenzidine
1300
isoform Cat-2, peroxidase activity with guaiacol
139
-
catalase activity after 5 days of cell culture in presence of 0.1 mM paraquat
14490
crude extract, pH 7.0, at 20°C
1486
-
catalatic activity
15.2
-
peroxidatic activity
1600
isoform Cat-2, peroxidase activity with o-dianisidine
18710
-
recombinant wild-type enzyme, pH 7.0, 60°C
19700
native enzyme, cell extract, pH 7.0, 25°C
199600
after 13.8fold purification, pH 7.0, at 20°C
222000
purified native enzyme, pH 7.0, 25°C
234.8
-
catalase activity after 10 days of cell culture in presence of 0.1 mM paraquat
23500
91fold purified enzyme, at 70°C
25700
-
purified native enzyme, pH 7.0, 40°C
3.5 - 4.5
-
about, cell lysates of wild-type Y-1 cells
316
-
crude extract, at 30°C
35000
-
after 110.7fold purification, at 30°C
366.6
crude extract, in 50 mM sodium phosphate buffer, pH 7.8, at 37°C
4
-
mutant H82N, pH 7.0, 60°C
470
isoform Cat-2, peroxidase activity with ascorbate
56950
Beta vulgaris var. cicla
-
-
6
-
about, cell lysates of Caco-2 cells recombinantly overexpressing IGFBP-2
6400
purified enzyme, pH 6,5, 37°C
65
-
mutant V123F, pH 7.0, 60°C
74.14
-
catalase activity after 10 days of cell culture
77.5
-
about, cell lysates of wild-type and recombinantly IGFBP-2-overexpressing 293 cells
8
-
about, cell lysates of Y-1 cells recombinantly overexpressing IGFBP-2
8.76
-
catalase activity after 5 days of cell culture
82
-
purified recombinant His-tagged enzyme expressed in Bacillus subtilis
8870
-
native wild-type enzyme, pH 7.0, 60°C
55000
-
purified enzyme, catalase activity, mixed-type
additional information
-
enzyme activity at pH 7.0, 23°C, in nonionic micellar and reverse micellar systems, formed by mixing of Brij 30, Brij 35, cyclohexane, decaline, dodecane, n-heptane or isooctane, and water, overview
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
activity in vivo, intracellularly
additional information
-
-
additional information
-
activity in vivo, intracellularly and extracellularly
additional information
-
activity in vivo, intracellularly and extracellularly
additional information
-
activity in vivo with different growth temperatures, intracellularly and extracellularly
additional information
-
activity in vivo, intracellularly and extracellularly
additional information
-
activity in vivo, intracellularly and extracellularly
additional information
-
activity in vivo
additional information
-
activity in vivo, intracellularly and extracellularly
additional information
-
specific activity of 219,360 U/ml, pH 7.0, temperature not specified in the publication
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-
epithelial cell
brenda
-
-
brenda
-
-
brenda
-
-
brenda
constitutive expression for the first 3 h post injection of H2O2
brenda
-
Y-1 cell, increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
brenda
-
-
brenda
catalase activity is significantly higher in patients with renal cell carcinoma than in controls
brenda
-
-
brenda
-
Caco-2 cell, increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
brenda
-
the catalase activity in striatum is significantly decreased in the lesioned group as compared to sham group and pretreatment with Withania somnifera reverses its activity significantly and dose dependently in the lesioned goup pretretaed with 100 mg/kg 200 mg/ml or 300 mg/kg body weight extracts of Withania somnifera orally as compared to lesioned group
brenda
-
heme in the growth medium is absolutely required for enzyme expression
brenda
expression is highest 46 h after cyst germination
brenda
-
zygotic
brenda
-
from seeds
brenda
-
293 cell
brenda
-
56 genotypes
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
diabetic animals treated with BioGHK incorporated collagen (Peptide Incorporated Collagen) show significant higher levels of catalase due to the ability of GHK to attract macrophages and cytokines towards the wound environment
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
overexpression of hepatitis C virus non-structural proteins increases catalase activity
brenda
-
catalase activity is decreased dramatically after forebrain ischemia insult, no significant difference in catalase activity between control group and sham-operated group and curcumin-treted group
brenda
-
-
brenda
highest expression
brenda
-
-
brenda
-
spadix
brenda
-
-
brenda
-
telomerase-deficient MEF cells have lower catalase activity
brenda
-
mouse small mesenteric artery
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
retinal. mRNA transcript for catalase in normal (5.5 mM) glucose medium or high (22 mM) glucose medium after 1, 3, or 5 days of stimulation. The pattern of relative expression of the pericyte catalase transcript at day 1 is essentially unchanged at 3 and 5 days with only a slightly higher value (10%) in high glucose medium, which is statistically significantly increased after 1 (p = 0.037), 3 (p = 0.037), and 5 (p = 0.025) days
brenda
-
-
brenda
-
-
brenda
-
from seeds
brenda
-
-
brenda
-
-
brenda
-
brenda
-
catalase activity is reduced significantly by lesioning, extract of Ginkgo biloba dose-dependently restores the activity
brenda
-
clone T-47DN5
brenda
-
-
brenda
-
-
brenda
-
catalase activity increases with increasing blood lead level
brenda
-
catalase level is statistically decreased in patients with acne vulgaris compared to healthy ones
brenda
-
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
-
brenda
-
-
brenda
-
colon tumor cell, increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
brenda
-
adrenocortical tumor cell, increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
inducible by H2O2, heat-shock, ethanol and stationary-phase conditions
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
inducible at low salt concentrations
brenda
-
-
brenda
Kloeckera sp.
-
methanol grown
brenda
Kloeckera sp. 2201
-
methanol grown
-
brenda
-
-
brenda
-
-
brenda
only present if growth medium is supplemented with hemin
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
KatB inducible by H2O2
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
from liver
brenda
-
isoform CatA
brenda
isoform Cat-1 mainly present
brenda
Cucurbita sp.
-
-
brenda
-
-
brenda
-
0.5% v/v methanol in the cell culture medium
brenda
-
0.5% v/v methanol in the cell culture medium
-
brenda
-
0.5% v/v methanol in the cell culture medium
-
brenda
-
-
brenda
-
-
-
brenda
constitutive expression for the first 3 h post injection of H2O2
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
catalase activity increases with increasing blood lead level
brenda
-
enzyme activity is significantly lower in patients with Parkinsons disease compared to the control
brenda
-
-
brenda
-
activities of catalase activity shows similar behavior after the exhaustive exercise bout, with a maximum activity at 3 h after the exercise. Activity tends to fall at 4 h after the exercise in comparison with 3 h
brenda
-
pentylenetetrazol-induced epileptic seizure is accompanied by significantly reduced catalase activity
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
constitutive expression for the first 3 h post injection of H2O2
brenda
-
-
brenda
-
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
-
brenda
constitutive expression for the first 3 h post injection of H2O2
brenda
-
-
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
activity increased significantly in the diazinon treated group compared with the control group
brenda
-
-
brenda
constitutive expression for the first 3 h post injection of H2O2
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
high expression level
brenda
-
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
fifth instar larval stage
brenda
marked up-regulation of expression in larvae in which H2O2 is overloaded and after wounding through injection
brenda
Beta vulgaris var. cicla
-
-
brenda
tissue extracts
brenda
-
-
brenda
-
activity continouosly increases from day 20 til day 70 after sowing
brenda
stability of enzyme is increased in a light-dependent manner both in C3- and in crassulacean acid metabolism-induced plants, without changes in the level of leaf transcript
brenda
-
-
brenda
-
activity drastically diminishes from 7 to 17 days after sowing
brenda
-
highest activity
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
439793, 439807, 439808, 657432, 685295, 687061, 699601, 700795, 712789, 723827, 725146, 725750, 726417 brenda
-
brenda
-
-
brenda
Capra capra
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
fetal liver
brenda
-
activity is increased by 1.13fold at 4 h after exposure to 50 cGy whole body gamma-irradiation and remains elevated at almost the same level up to 12 h after exposure
brenda
-
activity is increased by 1.13fold at 4 h after exposure to 50 cGy whole body gamma-irradiation and remains elevated at almost the same level up to 12 h after exposure
-
brenda
-
in azathioprine-treated rats a significant decrease in catalase activity is observed 24 h post-treatment. This inhibition is significantly released with pre-treatment with Hibiscus sabdariffa, Rosmarinus officinalisor Salvia officinalis
brenda
Capra capra
-
-
brenda
-
activity remains unaltered after exposure to 50 cGy whole body gamma-irradiation
brenda
-
activity remains unaltered after exposure to 50 cGy whole body gamma-irradiation
-
brenda
constitutive expression for the first 3 h post injection of H2O2
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
highest levels of transcripts in hepatopancreas, followed by a little lower expression in hemocytes and moderate expression in the tissues of brain, eyestalk, gill, intestine and muscle, with the lowest expression in the heart
brenda
-
activity in vivo, intracellularly
brenda
-
activity in vivo, intracellularly
brenda
-
-
brenda
isoform Cat-3 mainly present
brenda
-
inducible by nitrate containing growth medium
brenda
-
brenda
-
brenda
-
-
-
brenda
-
activity in vivo, intracellularly and extracellularly
brenda
-
activity in vivo with different growth temperatures and pH, intracellularly and extracellularly
brenda
-
activity in vivo with different growth temperatures and pH, intracellularly and extracellularly
-
brenda
-
activity in vivo, intracellularly and extracellularly
brenda
-
-
brenda
-
activity in vivo
brenda
-
activity in vivo, intracellularly and extracellularly
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
activity is kept at a high and stable value
brenda
-
activity is kept at a high and stable value
brenda
-
N2 fixing root nodules, transcription of katA from OxyR-dependent promoter
brenda
-
developing, expression and activity increase in non hydrated seeds and during desiccation on the mother plant and after artificial drying on the flowerhead
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
no change in catalase activity after treatment with nicotinamide
brenda
-
no change in catalase activity after treatment with nicotinamide
-
brenda
-
brenda
-
-
-
brenda
additional information
-
the catalase activity is determined upon mild oxidative stress treatment and is significantly correlated with the robustness level of mild-stress-treated cells toward severe oxidative and heat stresses but not toward severe acid stress for cells grown at both refrigeration and optimal temperatures
brenda
additional information
-
the catalase activity is determined upon mild oxidative stress treatment and is significantly correlated with the robustness level of mild-stress-treated cells toward severe oxidative and heat stresses but not toward severe acid stress for cells grown at both refrigeration and optimal temperatures
-
brenda
additional information
catalase activity absolutely depends on exposure to O2 and occurs in cells grown in medium containing a heme source, these cells show higher viability on exposure to H2O2, growth optimum 37°C
brenda
additional information
-
catalase activity absolutely depends on exposure to O2 and occurs in cells grown in medium containing a heme source, these cells show higher viability on exposure to H2O2, growth optimum 37°C
brenda
additional information
-
catalase activity absolutely depends on exposure to O2 and occurs in cells grown in medium containing a heme source, these cells show higher viability on exposure to H2O2, growth optimum 37°C
-
brenda
additional information
-
changes in the level of catalase activity in the three tissues of fat body, midgut and haemolymph of the five selected bivoltine breeds and their 9 quantitative traits, namely larval weight, cocoon weight, shell weight, shell ratio, filament length, filament weight, denier, renditta and effective rearing rate, and correlation between them under high temperature conditions, overview
brenda
additional information
-
constitutive epression, tissue expression analysis, overview
brenda
additional information
-
catalase and bifunctional catalase-peroxidase are growth regulated and expressed mainly during the stationary phase, growth pattern analysis
brenda
additional information
-
germination tests and seed moisture content determination
brenda
additional information
the protein and expression level are reduced during the mycelial saprobic phase compared to the yeast phase of infection
brenda
additional information
-
the protein and expression level are reduced during the mycelial saprobic phase compared to the yeast phase of infection
brenda
additional information
-
the protein and expression level are reduced during the mycelial saprobic phase compared to the yeast phase of infection
-
brenda
additional information
expression in all developmental stages except for 3-h germinated cysts. Highest expression occurs in sporulating hyphae and the least in 3-h germinated cysts
brenda
additional information
expression in all developmental stages except for 3-h germinated cysts. Highest expression occurs in sporulating hyphae and the least in 3-h germinated cysts
brenda
additional information
expression in all developmental stages except for 3-h germinated cysts. Highest expression occurs in sporulating hyphae and the least in 3-h germinated cysts
brenda
additional information
-
expression in all developmental stages except for 3-h germinated cysts. Highest expression occurs in sporulating hyphae and the least in 3-h germinated cysts
brenda
additional information
major catalase in all developmental stages, with the highest expression occurring in sporulating hyphae and the lowest in 3-h germinated cysts. In planta, activity increases dramatically about 8 h after host inocculation
brenda
additional information
major catalase in all developmental stages, with the highest expression occurring in sporulating hyphae and the lowest in 3-h germinated cysts. In planta, activity increases dramatically about 8 h after host inocculation
brenda
additional information
major catalase in all developmental stages, with the highest expression occurring in sporulating hyphae and the lowest in 3-h germinated cysts. In planta, activity increases dramatically about 8 h after host inocculation
brenda
additional information
-
major catalase in all developmental stages, with the highest expression occurring in sporulating hyphae and the lowest in 3-h germinated cysts. In planta, activity increases dramatically about 8 h after host inocculation
brenda
additional information
tissue quantitative real-time RT-PCR expression analysis, overview. Expression level of catalase transcripts both in haemocytes and hepatopancreas changes rapidly and dynamically after Vibrio alginolyticus challenging in the intermoult stage
brenda
additional information
-
tissue quantitative real-time RT-PCR expression analysis, overview. Expression level of catalase transcripts both in haemocytes and hepatopancreas changes rapidly and dynamically after Vibrio alginolyticus challenging in the intermoult stage
brenda
additional information
present in all tissues examined
brenda
additional information
-
present in all tissues examined
brenda
additional information
-
biofilm cultures
brenda
additional information
high enzyme activity when the strain VA1 is grown under aerobic conditions, and decreased activity under anaerobic growth
brenda
additional information
-
high enzyme activity when the strain VA1 is grown under aerobic conditions, and decreased activity under anaerobic growth
brenda
additional information
-
high enzyme activity when the strain VA1 is grown under aerobic conditions, and decreased activity under anaerobic growth
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
-
EsCAT contains a highly conserved proximal active-site signature motif (60FDRERIPERVVHAKGAL76) and a proximal heme-ligand signature motif (350RLFSYNDTH358) and exhibits high similarity with other reported CATs
evolution
the dismutation reaction of H2O2 in microorganisms has evolved in three phylogenetically unrelated protein types: monofunctional catalase, catalase-peroxidase and Mn-catalase, phylogenetic analysis, overview. PktA is a clade 3 catalase. The active sites with His65, Ser104, and Asn138, binding sites of the distal region of heme with Val106, Thr128, and Phe143, and proximal sites of heme with Tyr348 and Arg355 are well conserved
evolution
-
the dismutation reaction of H2O2 in microorganisms has evolved in three phylogenetically unrelated protein types: monofunctional catalase, catalase-peroxidase and Mn-catalase, phylogenetic analysis, overview. PktA is a clade 3 catalase. The active sites with His65, Ser104, and Asn138, binding sites of the distal region of heme with Val106, Thr128, and Phe143, and proximal sites of heme with Tyr348 and Arg355 are well conserved
-
malfunction
-
catalase-negative mutant ROA3 exhibits impaired growth, with the extent of impairment increasing with decreasing temperature, and no growth is detected at 4°C. Aerobic growth in liquid is impaired at 4°C, especially under aeration, but not at higher temperatures (10, 25, or 37°C)
malfunction
the recombinant enzyme shows reduced catalase activity and thermal stability, overview
malfunction
-
catalase-negative mutant ROA3 exhibits impaired growth, with the extent of impairment increasing with decreasing temperature, and no growth is detected at 4°C. Aerobic growth in liquid is impaired at 4°C, especially under aeration, but not at higher temperatures (10, 25, or 37°C)
-
malfunction
-
the recombinant enzyme shows reduced catalase activity and thermal stability, overview
-
physiological function
-
catalase is not required for cryotolerance of Listeria monocytogenes
physiological function
catalase plays a significant role in preventing Serratia marcescens against cellular damage through hydrogen peroxide
physiological function
catalase is an antioxidant and hydroperoxidase enzyme protecting the cellular environment from harmful effects of hydrogen peroxide by facilitating its degradation to oxygen and water. The catalase gene is involved in the cellular stress response and (anti)oxidative processes triggered by stressor and contaminant exposure
physiological function
-
catalase is an antioxidant enzyme and plays a significant role in the protection against oxidative stress by reducing hydrogen peroxide
physiological function
catalase is an antioxidant enzyme involved in redox equilibrium, regulating hydrogen peroxide concentration, a harmful reactive oxygen species that is produced during hypoxia, enzyme activity during hypoxia and reoxygenation, 1 h after hypoxia, overview
physiological function
catalase is an important antioxidant protein that protects organisms against various oxidative stresses by eliminating hydrogen peroxide
physiological function
-
catalase is responsible for the enzymatic destruction/detoxification of hydrogen peroxide, to combat its deleterious effects
physiological function
-
catalases, heme enzymes, which catalyze decomposition of hydrogen peroxide to water and molecular oxygen, belong to the antioxidant defense system of the cell
physiological function
chaperone-specific enzyme regulation, overview
physiological function
-
the catalase activity is determined upon mild oxidative stress treatment and is significantly correlated with the robustness level of mild-stress-treated cells toward severe oxidative and heat stresses but not toward severe acid stress for cells grown at both refrigeration and optimal temperatures, overview
physiological function
the catalase activity of CcO is clearly a side reaction
physiological function
-
formation of chloroplast protrusions and catalase activity are significantly increased under conditions that favour photorespiration, while in darkness or at high CO2 concentration under light, chloroplast protrusions formation is significantly lower
physiological function
-
catalase is not required for cryotolerance of Listeria monocytogenes
-
physiological function
-
the catalase activity of CcO is clearly a side reaction
-
physiological function
-
the catalase activity is determined upon mild oxidative stress treatment and is significantly correlated with the robustness level of mild-stress-treated cells toward severe oxidative and heat stresses but not toward severe acid stress for cells grown at both refrigeration and optimal temperatures, overview
-
physiological function
-
catalase plays a significant role in preventing Serratia marcescens against cellular damage through hydrogen peroxide
-
additional information
-
catalase form III protein and crystal structure analysis, overview
additional information
conserved catalytic active residues are His71, Asn144, and Tyr354
additional information
-
conserved catalytic active residues are His71, Asn144, and Tyr354
additional information
homology modelling, overview
additional information
-
homology modelling, overview
additional information
-
reaction mechanism of catalase activity, overview. The iron in the active site is in an uncoupled high-spin ferric oxidation state. The metal ions can be reduced back to the di-ferrous state with dithionite but the deaminase activity is not recovered. Therefore, addition of an excess of H2O2 to [FeII/FeII]-ADEec irreversibly modifies the protein and stabilizes the [FeIII/FeIII] state
additional information
-
structure-function analysis, overview. H55 and Y338 in the active site are crucial for the activity. The distal heme ligand binding domain 46RERIPERVVHAKG58 encompasses the essential distal histidine residue, and the proximal heme ligand binding domain 334R-F-Y-D340 harbors the essential proximal tyrosine residue. Other catalase specific motifs are 126VGNNTP131, 107RDXRGFAXKFYT118, and 92RFSTV96. Tyr117 from sequence 107RDXRGFAXKFYT118 is crucial for activity
additional information
the enzyme exhibits an extraordinarily high catalase activity, active sites residues are His65, Ser104, and Asn138
additional information
the enzyme is a mono-functional plant catalase
additional information
-
the enzyme is a mono-functional plant catalase
additional information
the enzyme's binuclear active center, residing in subunit I, contains heme a3 and CuB. Apart from its oxygen reductase activity, the protein possesses a peroxidase and a catalase activity
additional information
-
the enzyme's binuclear active center, residing in subunit I, contains heme a3 and CuB. Apart from its oxygen reductase activity, the protein possesses a peroxidase and a catalase activity
additional information
-
the heme-binding pocket contains two highly conserved water molecules on the distal side
additional information
-
the heme-binding pocket contains two highly conserved water molecules on the distal side
-
additional information
-
the enzyme's binuclear active center, residing in subunit I, contains heme a3 and CuB. Apart from its oxygen reductase activity, the protein possesses a peroxidase and a catalase activity
-
additional information
-
the enzyme exhibits an extraordinarily high catalase activity, active sites residues are His65, Ser104, and Asn138
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
110000
about, gel filtration
145000
-
native polyacrylamide gel electrophoresis
185000
-
native polyacrylamide gel electrophoresis
210000
-
ultracentrifugation
220000
Capra capra
-
gel filtration
225000
-
sucrose density gradient centrifugation
227300
-
TvC-II, gel filtration
234000
native enzyme, gel filtration
235000
Beta vulgaris var. cicla
-
gel filtration
258000
-
isoenzyme with optimum at pH 10.0, SDS-PAGE
285000
-
isoenzyme with optimum at pH 6.5, SDS-PAGE
308000
-
isoenzyme with optimum at pH 4.5, SDS-PAGE
33000
x * 33000, calculated including the putative signal peptide, x * 33000, SDS-PAGE of recombinant inactive form
33450
4 * 33450, amino acid sequence calculation, 4 * 38000, SDS-PAGE
337000
-
sedimentation equillibrium analysis
339000
Capra capra
-
gel filtration
360000
-
native electrophoresis
38000
4 * 33450, amino acid sequence calculation, 4 * 38000, SDS-PAGE
385000
-
sedimentation equilibrium analysis
42500
-
4 * 42500, SDS-PAGE
51000
-
4 * 51000, SDS-PAGE
57300
-
4 * 57300, SDS-PAGE
57440
x * 57440, sequence calculation
57900
x * 57900, calculated
58400
x * 58400, calculated
58860
-
4x * 58860, sequence calculation
60300
-
4 * 60300, SDS-PAGE
62900
-
4 * 62900, TvC-II, SDS-PAGE
63000
-
4 * 63000, SDS-PAGE
68000
-
1 * 75000 + 1 * 68000, SDS-PAGE
72000
-
4 * 72000, SDS-PAGE
74000
4 * 74000, recombinant His-tagged catalase-A with bound heme cofactor, SDS-PAGE, 4 * 57000-58000, native enzyme
8300
ring-like arrangement of six monomers, 6 * 7900 (SDS-PAGE), 6 * 8300 calculated
83200
-
x * 83200, SDS-PAGE
150000
-
gel filtration
170000
-
catalase-peroxidase
170000
Pibocella sp.
-
native polyacrylamide gel electrophoresis
230000
-
gel filtration
230000
Cucurbita sp.
-
sucrose density gradient centrifugation
240000
-
gel filtration
240000
Kloeckera sp.
-
gel filtration
240000
KTL38510
gel filtration
320000
-
-
320000
-
sedimentation equilibrium analysis, gel filtration
42000
-
x * 42000, SDS-PAGE
42000
-
x * 42000, SDS-PAGE
48000
-
and 59000, gel filtration
48000
-
and 59000, gel filtration
54000
gel filtration
54000
x * 54000, SDS-PAGE
54000
-
4 * 54000, SDS-PAGE
54000
-
4 * 54000, SDS-PAGE
54000
4 * 54000, SDS-PAGE
54000
-
x * 54000, recombinant His-tagged enzyme, SDS-PAGE
54000
-
4 * 61000, SDS-PAGE, 4 * 54000, calculated
55000
2 * 55000, SDS-PAGE
55000
Cucurbita sp.
-
4 * 55000, SDS-PAGE
56000
x * 56000, SDS-PAGE
56000
-
4 * 56000, gel filtration
56000
x * 56000, calculated, x * 98.5, SDS-PAGE of fusion protein with maltose binding protein
57000
-
x * 57000, SDS-PAGE
57000
-
4 * 57000, SDS-PAGE
57700
4 * 57700, MALDI-TOF
57700
x * 57700, calculated
58000
4 * 58000, SDS-PAGE
58000
-
x * 58000, recombinant isozyme Cat1.4, SDS-PAGE
58500
Beta vulgaris var. cicla
-
4 * 58500, SDS-PAGE
58500
x * 58500, about, sequence calculation
59000
-
and 48000, gel filtration
59000
-
and 48000, gel filtration
59000
-
4 * 59000, SDS-PAGE
59000
4 * 59000, SDS-PAGE
60000
x * 60000, SDS-PAGE
60000
Capra capra
-
4 * 60000, SDS-PAGE
60000
4 * 60000, SDS-PAGE
60000
4 * 60000, SDS-PAGE
60000
-
x * 84000, isoenzyme I, x * 60000, isoenzyme II, x * 80000, isoenzyme III, SDS-PAGE
60000
-
4 * 60000, SDS-PAGE for all three isoforms
61000
x * 61000, SDS-PAGE
61000
4 * 61000, SDS-PAGE
61000
-
4 * 61000, SDS-PAGE, 4 * 54000, calculated
62000
-
4 * 62000, SDS-PAGE
62000
Kloeckera sp.
-
4 * 62000, SDS-PAGE
62000
x * 79000, + x* 74000, + x * 62000, higher molecular masses of subunits coincide with higher catalytic activity
75000
-
2 * 75000, SDS-PAGE
75000
-
1 * 75000 + 1 * 68000, SDS-PAGE
79000
-
4 * 79000, SDS-PAGE
79000
x * 79000, + x* 74000, + x * 62000, higher molecular masses of subunits coincide with higher catalytic activity
79000
-
4 * 79000, wild-type and mutant enzymes, SDS-PAGE
80000
-
80000
-
2 * 80000, SDS-PAGE
80000
-
4 * 80000, SDS-PAGE
80000
-
4 * 80000, SDS-PAGE
80000
-
x * 84000, isoenzyme I, x * 60000, isoenzyme II, x * 80000, isoenzyme III, SDS-PAGE
80000
x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein
84000
calculated from amino acid sequence
84000
-
4 * 84000, SDS-PAGE
84000
-
x * 84000, isoenzyme I, x * 60000, isoenzyme II, x * 80000, isoenzyme III, SDS-PAGE
85000
-
4 * 85000, SDS-PAGE
85000
-
catalase-peroxidase, 2 * 85000, SDS-PAGE
92000
-
4 * 92000, SDS-PAGE
92000
-
2 * 92000, SDS-PAGE
97000
-
4 * 97000, SDS-PAGE
97000
x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hexamer
ring-like arrangement of six monomers, 6 * 7900 (SDS-PAGE), 6 * 8300 calculated
monomer
1 * 80000, isoforms Cat-1, Cat-3
oligomer
x * 79000, + x* 74000, + x * 62000, higher molecular masses of subunits coincide with higher catalytic activity
?
-
x * 58000, recombinant isozyme Cat1.4, SDS-PAGE
?
x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein
?
-
x * 84000, isoenzyme I, x * 60000, isoenzyme II, x * 80000, isoenzyme III, SDS-PAGE
?
-
x * 84000, isoenzyme I, x * 60000, isoenzyme II, x * 80000, isoenzyme III, SDS-PAGE
-
?
-
x * 54000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 65000, SDS-PAGE, His-tagged recombinant protein
?
x * 56000, calculated, x * 98.5, SDS-PAGE of fusion protein with maltose binding protein
?
x * 57440, sequence calculation
?
x * 33000, calculated including the putative signal peptide, x * 33000, SDS-PAGE of recombinant inactive form
?
-
x * 61000, SDS-PAGE
-
?
x * 58500, about, sequence calculation
?
-
x * 66.6, calculation from deduced amino acid sequence
?
-
x * 52000, SDS-PAGE
-
dimer
-
1 * 75000 + 1 * 68000, SDS-PAGE
dimer
-
2 * 92000, SDS-PAGE
dimer
-
2 * 92000, SDS-PAGE
-
dimer
-
2 * 80000, SDS-PAGE
dimer
-
2 * 80000, SDS-PAGE
-
dimer
-
2 * 80000, SDS-PAGE
-
dimer
-
catalase-peroxidase, 2 * 85000, SDS-PAGE
dimer
-
catalase-peroxidase, 2 * 85000, SDS-PAGE
-
dimer
-
2 * 75000, SDS-PAGE
homodimer
2 * 55000, SDS-PAGE
homodimer
-
2 * 55000, SDS-PAGE
-
homotetramer
-
4 * 56000, gel filtration
homotetramer
-
4 * 56000, gel filtration
-
homotetramer
4 * 60000, SDS-PAGE
homotetramer
-
4x * 58860, sequence calculation
homotetramer
-
4 * 80000, SDS-PAGE
homotetramer
-
4 * 79000, wild-type and mutant enzymes, SDS-PAGE
homotetramer
-
4 * 79000, wild-type and mutant enzymes, SDS-PAGE
-
homotetramer
x-ray crystallography
homotetramer
-
4 * 72000, SDS-PAGE
homotetramer
4 * 74000, recombinant His-tagged catalase-A with bound heme cofactor, SDS-PAGE, 4 * 57000-58000, native enzyme
homotetramer
4 * 61000, SDS-PAGE
homotetramer
-
4 * 61000, SDS-PAGE
-
homotetramer
4 * 59000, SDS-PAGE
homotetramer
-
4 * 59000, SDS-PAGE
-
homotetramer
4 * 58000, SDS-PAGE
homotetramer
-
4 * 58000, SDS-PAGE
-
tetramer
4 * 57256, mass spectrometry, 4 * 57000, SDS-PAGE
tetramer
-
4 * 92000, SDS-PAGE
tetramer
-
4 * 97000, SDS-PAGE
tetramer
-
4 * 51000, SDS-PAGE
tetramer
-
4 * 51000, SDS-PAGE
-
tetramer
4 * 60000, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE
-
tetramer
Beta vulgaris var. cicla
-
4 * 58500, SDS-PAGE
tetramer
-
4 * 54000, SDS-PAGE
tetramer
-
4 * 63000, SDS-PAGE
tetramer
Capra capra
-
4 * 60000, SDS-PAGE
tetramer
Cucurbita sp.
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 84000, SDS-PAGE
tetramer
-
4 * 62000, SDS-PAGE
tetramer
-
4 * 60300, SDS-PAGE
tetramer
-
subunit composition of different plants, overview
tetramer
Kloeckera sp.
-
4 * 62000, SDS-PAGE
tetramer
Kloeckera sp. 2201
-
4 * 62000, SDS-PAGE
-
tetramer
-
4 * 54000, SDS-PAGE
tetramer
4 * 57700, MALDI-TOF
tetramer
4 * 54000, SDS-PAGE
tetramer
-
4 * 80000, SDS-PAGE
tetramer
-
tetramer in solution
tetramer
-
4 * 85000, SDS-PAGE
tetramer
-
4 * 57000, SDS-PAGE
tetramer
4 * 33450, amino acid sequence calculation, 4 * 38000, SDS-PAGE
tetramer
-
4 * 33450, amino acid sequence calculation, 4 * 38000, SDS-PAGE
-
tetramer
-
4 * 59000, SDS-PAGE
tetramer
-
4 * 79000, SDS-PAGE
tetramer
-
4 * 61000, SDS-PAGE, 4 * 54000, calculated
tetramer
-
4 * 79000, SDS-PAGE
-
tetramer
4 * 82000, SDS-PAGE
tetramer
-
4 * 75000, SDS-PAGE
tetramer
-
4 * 75000, SDS-PAGE
-
tetramer
-
4 * 42500, SDS-PAGE
tetramer
-
4 * 62900, TvC-II, SDS-PAGE
tetramer
-
4 * 57300, SDS-PAGE
tetramer
KTL38510
4 * 57210, calculated, 4 * 58000, SDS-PAGE
tetramer
-
4 * 57210, calculated, 4 * 58000, SDS-PAGE
-
tetramer
-
4 * 60000, SDS-PAGE for all three isoforms
additional information
-
homology modeling of isozyme Cat1.4
additional information
-
catalase form III structure analysis, overview
additional information
-
dehydration induces the synthesis of a 55 kDa subunit via activation of the CATA1 gene
additional information
-
determination and analysis of secondary enzyme structure
additional information
homology modelling, overview
additional information
-
homology modelling, overview
additional information
sodium dodecylsufate treatment breaks active oligomeric catalse into the less active and putatively dimeric 160000 Da form
additional information
-
sodium dodecylsufate treatment breaks active oligomeric catalse into the less active and putatively dimeric 160000 Da form
additional information
-
enzyme secondary structure analysis
additional information
-
enzyme secondary structure analysis
-
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S2W
-
natural polymorphism. Strain S carries the Ser isoform, strain G3 carries the Trp-isoform which shows a lower specific activity and higher Km value than the Ser-isoform. Mutation S2W destabilizes the functional tetrameric form of the enzyme. Ser/Ser females have a significantly higher fecundity than Trp/Trp females
D270A
-
site-directed mutagenesis
H146A
-
site-directed mutagenesis
H215A
-
site-directed mutagenesis
H55A
-
site-directed mutagenesis
N376A
-
site-directed mutagenesis
N82A
-
site-directed mutagenesis
P391A
-
site-directed mutagenesis
Q332A
-
site-directed mutagenesis
R6A
-
site-directed mutagenesis
V210A
-
site-directed mutagenesis
W257A
-
site-directed mutagenesis
Y117A
-
site-directed mutagenesis
Y338A
-
site-directed mutagenesis
Y397A
-
site-directed mutagenesis
D474N
-
site-directed mutagenesis, catalase inactive mutant
H473N
-
site-directed mutagenesis, catalase inactive mutant
Y111A
-
substantial increase in hexa-xoordinate low-spin heme with the appearance of a transition between the wild-type primarily high-spin and the N-terminal pure low-spin domain alone. Decrease in activity is for catalase activity more substantially than for peroxidase activity
M244A
-
coplete loss of catalase activity, increased peroxidase activity due to enhanced affinity for the peroidatic substrate
S315T
-
mutation at katG codon 315 detected in 17 (63.0%) of the 27 isoniazid-resistant isolates analyzed. The most prevalent mutation observed is AGC315ACC (Ser315Thr), involving 11(65%) of the 17 isoniazid-resistant isolates having a mutation in the sequenced region. Ten isoniazid-resistant and all 29 isoniazid-susceptible isolates sequenced have no mutation in this region. Of the 19 multi-drug-resistant isolates, 15 (78.9%) show a mutation in codon 315, while only two (25%) of the eight isoniazid mono-resistant isolates are found to have a mutation in that codon
W107F
-
mutation in key distal side residue, disrupts high-affinity binding of substrate isonicotinic hydrazide
Y229F
-
mutation in key distal side residue, disrupts high-affinity binding of substrate isonicotinic hydrazide
E316F
kcat/Km is 2fold lower than kcat/Km for wild-type enzyme
E316H
kcat/Km is 2.6fold lower than kcat/Km for wild-type enzyme
H246W
kcat/Km is 5.3fold lower than kcat/Km for wild-type enzyme
H82N
-
site-directed mutagenesis, the mutation results in conversion of the native d-type heme to a b-type heme
I313F
slight increase in kcat/Km as compared to kcat/Km of wild-type enzyme
I314F
kcat/Km is 5.2fold lower than kcat/Km for wild-type enzyme
L321A
kcat/Km is 1.2fold lower than kcat/Km for wild-type enzyme
V123F
-
site-directed mutagenesis
V536A
kcat/Km is 1.6fold lower than kcat/Km for wild-type enzyme
V536W
kcat/Km is 5.1fold lower than kcat/Km for wild-type enzyme
H82N
-
site-directed mutagenesis, the mutation results in conversion of the native d-type heme to a b-type heme
-
V123F
-
site-directed mutagenesis
-
L189W/H225T
almost 3fold decrease in Km-value, 2-2.5fold increase in enzyme velocity, loss of photoinhibition
M129V/E293G
less thermostable mutant enzyme
H72A
KTL38510
mutant in heme-binding residue, almost complete loss of activity
V71A and F158A
KTL38510
channel point mutant, about 20% of wild-type activity
Y353A
KTL38510
mutant in heme-binding residue, almost complete loss of activity
H72A
-
mutant in heme-binding residue, almost complete loss of activity
-
V71A and F158A
-
channel point mutant, about 20% of wild-type activity
-
Y353A
-
mutant in heme-binding residue, almost complete loss of activity
-
additional information
-
systemic reduction in catalase activity by dsRNA-mediated knock-down significantly reduces the reproductive output of mosquito females
additional information
-
immobilization and kinetics of catalase on calcium carbonate nanoparticles attached epoxy support, synthesized by miniemulsion technique, overview. A decrease in Vmax value from 1.50 to 0.42 mM/mg protein is observed after immobilization. Thermal and storage stabilities of catalase improved immensely after immobilization. The immobilized enzyme retains three times than the activity of free enzyme when kept at 75°C for 1 h and the half-life of enzyme increases five times when stored in 0.01 M phosphate, pH 7.0, at 5°C. The enzyme can be reused 30times without any significant loss of its initial activity
additional information
-
switch of the coding region for Pseudomonas aeruginosa KatA enzyme with those for KatA from Bacillus subtilis, and expression of the catalases under the potential katA-regulatory elements in Pseudomonas aeruginosa. Activitiy of the Bacillus subtilis enzyme is less than 40% of the native Pseudomonas enzyme activity. Bacillus subtilis enzyme is rather susceptible to proteinase K, whereas the Pseudomonas enzyme is highly stable against proteinase K. Bacillus subtilis enzyme is not detectable in the extracellular milieu, but it fully rescues the peroxide sensitivity and osmosensitivity of the Pseudomonas katA mutant, as well as the attenuated virulence of the katA mutant in mouse acute infection and Drosophila melanogaster models. However, it does not rescue the peroxide susceptibility of the katA mutant in a biofilm growth state
additional information
-
switch of the coding region for Pseudomonas aeruginosa KatA enzyme with those for KatA from Bacillus subtilis, and expression of the catalases under the potential katA-regulatory elements in Pseudomonas aeruginosa. Activitiy of the Bacillus subtilis enzyme is less than 40% of the native Pseudomonas enzyme activity. Bacillus subtilis enzyme is rather susceptible to proteinase K, whereas the Pseudomonas enzyme is highly stable against proteinase K. Bacillus subtilis enzyme is not detectable in the extracellular milieu, but it fully rescues the peroxide sensitivity and osmosensitivity of the Pseudomonas katA mutant, as well as the attenuated virulence of the katA mutant in mouse acute infection and Drosophila melanogaster models. However, it does not rescue the peroxide susceptibility of the katA mutant in a biofilm growth state
-
additional information
-
enzyme immobilization via precipitation with ammonium sulfate and then crosslinking with glutaraldehyde, method development. The immoblized enzyme shows about 50% of free enzyme activity, its thermal and storage stabilities are improved compared to the free catalase and the remaining activity of immobilized CLEA-CAT-BSA enzyme derivative is 50% of its initial activity at the end of 400 consecutive uses in a batch type-reactor
additional information
-
catalase fusion ezyme with aldehyde deformylating oxygenase, i.e. CAT-ADO, turns over 225times versus 3times for the native ADO, and its expression in Escherichia coli increases catalytic turnovers per active site by fivefold relative to the expression of native ADO. Catalase protects ADO from inhibition by its reaction product H2O2
additional information
both native protein and fusion protein with maltose binding protein show the same specific activity
additional information
-
construction of a mutant strain with a Thr501-truncated KatA and a KapA-deficient mutant strain, only the latter shows 5.5fold reduced KatA activity in the periplasm, the cytoplasmic activities remain unaltered in all cases, site-directed mutagenesis
additional information
deletion of the chromosomally encoded gene ctaDII (coding for subunit I present in aa3 CcO), is complemented on a low copy number plasmid controlled by the promoter of the cta operon
additional information
-
deletion of the chromosomally encoded gene ctaDII (coding for subunit I present in aa3 CcO), is complemented on a low copy number plasmid controlled by the promoter of the cta operon
additional information
-
deletion of the chromosomally encoded gene ctaDII (coding for subunit I present in aa3 CcO), is complemented on a low copy number plasmid controlled by the promoter of the cta operon
-
additional information
-
loss of enzyme activity results in a temperature-dependent hydrogen peroxide sensitivity, correlating with its temperature-inducible expression pattern
additional information
-
construction of a ccmC knockout mutant, which shows a range of other phenotypic changes. The production of the siderophore pyoverdine is very low and growth under the condition of iron limitation is severely restricted, but production of the second siderophore, pyochelin, is increased. The production of pyocyanin, swarming and twitching motility, and rhamnolipid production are affected, the mutant accumulates porphyrins, and catalase production is undetectable, phenotype, overview
additional information
-
the expression of katA is downregulated 7.7fold in biofilm cultures of Pseudomonas aeruginosa
additional information
-
switch of the coding region for KatA enzyme with those for KatA from Bacillus subtilis and CatA from Streptomyces coelicolor, and expression of the catalases under the potential katA-regulatory elements in Pseudomonas aeruginosa. Activities of the Bacillus subtilis and Streptomyces coelicolor enzymes are less than 40% of the native Pseudomonmas enzyme activity. Bacillus subtilis and Streptomyces coelicolor enzymes are rather susceptible to proteinase K, whereas the Pseudomonas enzyme is highly stable against proteinase K. Bacillus subtilis and Streptomyces coelicolor enzymes are not detectable in the extracellular milieu, but they fully rescue the peroxide sensitivity and osmosensitivity of the Pseudomonas katA mutant, respectively, as well as the attenuated virulence of the katA mutant in mouse acute infection and Drosophila melanogaster models. However, neither enzyme rescues the peroxide susceptibility of the katA mutant in a biofilm growth state
additional information
-
switch of the coding region for KatA enzyme with those for KatA from Bacillus subtilis and CatA from Streptomyces coelicolor, and expression of the catalases under the potential katA-regulatory elements in Pseudomonas aeruginosa. Activities of the Bacillus subtilis and Streptomyces coelicolor enzymes are less than 40% of the native Pseudomonmas enzyme activity. Bacillus subtilis and Streptomyces coelicolor enzymes are rather susceptible to proteinase K, whereas the Pseudomonas enzyme is highly stable against proteinase K. Bacillus subtilis and Streptomyces coelicolor enzymes are not detectable in the extracellular milieu, but they fully rescue the peroxide sensitivity and osmosensitivity of the Pseudomonas katA mutant, respectively, as well as the attenuated virulence of the katA mutant in mouse acute infection and Drosophila melanogaster models. However, neither enzyme rescues the peroxide susceptibility of the katA mutant in a biofilm growth state
-
additional information
-
mutant lacking enzymic activity is more sensitive to peracetic acid than wild-type
additional information
-
switch of the coding region for Pseudomonas aeruginosa KatA enzyme with those for CatA from Streptomyces coelicolor and expression of the catalases under the potential katA-regulatory elements in Pseudomonas aeruginosa. Activitiy of the Streptomyces coelicolor enzyme is less than 40% of the native Pseudomomas enzyme activity. Streptomyces coelicolor enzyme is rather susceptible to proteinase K, whereas the Pseudomonas enzyme is highly stable against proteinase K. Streptomyces coelicolor enzyme is not detectable in the extracellular milieu, but it fully rescues the peroxide sensitivity and osmosensitivity of the Pseudomonas katA mutant, as well as the attenuated virulence of the katA mutant in mouse acute infection and Drosophila melanogaster models. However, it does not rescue the peroxide susceptibility of the katA mutant in a biofilm growth state
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25 - 70
-
when the extract is incubated at specified temperature (25-70°C) for various length of time (5-30 min) then tested at room temperature a decrease in catalase activity is found at temperature above 50, 60, and 70°C for pHs of 6.5, 10.0, and 4.5, respectively. After heating at 70°C for 30 min, catalase activity loses about 40, 60, and 75% of the original activity at pH 4.5, 10.0, and 6.5, respectively.
30 - 60
-
thermoinactivation kinetics in the presence or absence of substrate H2O2, overview
35 - 40
-
slightly suppressed activity
35 - 50
-
the half-lives of free catalase at 35 and 50°C were 9.0 and 6.7 h, respectively and these correspondingly are 70.0 and 9.7 h for immobilized catalase onto controlled pore glass
40 - 50
-
the half lives of free catalase at 40 and 50°C are 9.0 and 6.7 h, respectively, and correspondingly 29.1 and 4.8 h for Eupergit C-immobilized catalase
40 - 60
-
the enzyme is stable for 24 h at 40°C with a half-life of 4 h 60°C, at 50°C the half life is about 18 h
50 - 60
-
65% residual activity after 15 min at 50°C, 54% residual activity after 30 min at 50°C, 43% residual activity after 40 min at 50°C, 12% residual activity after 15 min of preincubation at 60°C, preincubation at 65°C for 10 min results in complete loss of activity
58
-
1 h, 83% reduction in activity
60 - 70
at 60°C, the enzyme is stable for 240 min, at 65°C the enzyme retains more than 55% of its activity by incubating the enzyme at pH 7.0 after 225 min, at 70°C, the enzyme can retain 57% of its initial activity after incubating at pH 7.0 for 90 min
68
5 min, no loss of activity
additional information
high thermal stability. HTHP is stable under a wide range of temperatures. Thermal unfolding is measured up to 110°C and in the presence of high concentrations of guanidinium hydrochloride. The melting point of HTHP is estimated to be around 130°C. Catalatic activity is tested after incubation for 10 min at 85°C and 90°C and is found to be reduced by less than 5% under both conditions
100
isoform Cat-1, half-life: 70 min
30
-
85% remaining peroxidase activity after 20 h at pH 9.0
30
-
50% loss of activity in 30 min
30
10 min, loss of 20% activity
37
-
enzyme in homogenous aqueous solution: half-life is 19.0 h, enzyme in aqueous solution with Brij 35: half-life is 17.5 h, enzyme in reverse micelles of 0.1 M Brij 30 in n-heptane: half-life is 14.5 h
37
KTL38510
2h, 80% residual activity
40
15 h, incubation below 40°C, retains most of its activity. Activity is quickly lost above 40°C
40
1 h, 60% residual activity
40
stable up to, a sharp decline in activity above
40
10 h, more than 50% residual activity
40
-
purified native enzyme, 15 min, stable
45
-
30% loss of activity in 30 min, enzyme from acatalasemic liver has 70% loss of activity in 30 min
45
-
60 min, 17% decreased activity
45
KTL38510
40 min, 40% residual activity
45
-
Cat-1 half-life: 12.5 min, Cat-3 half-life: 18 min, Cat-2 stable
50
1 h, 78% residual activity
50
Beta vulgaris var. cicla
-
half-life: 30 min
50
-
enzyme in homogenous aqueous solution: half-life is 35 min, enzyme in aqueous solution with Brij 35: half-life is 12 min, enzyme in reverse micelles of 0.1 M Brij 30 in n-heptane: half-life is 77 min
50
rapid inactivation above
50
-
155% activation during transfer from 4°C in 5 min
50
-
loss of both catalase-peroxidase activities
50
-
188% activation during transfer from 4°C in 5 min
50
-
purified native enzyme, half-life is 7.5 h
55
stable up to
55
-
TvC-I and TvC-II, rapid inactivation
55
10 min, loss of 50% activity
60
78% residual activity at pH 7.0 under 60?C for 30 min
60
-
pH 8.5, stable up to, catalase and peroxidase activities
60
1 h, 19% residual activity
60
Beta vulgaris var. cicla
-
half-life: 10 min
60
1 h, 94.7% residual activity
60
50 min, no loss of activity
60
-
1 min, loss of over 80% of both activities
60
-
60 min, loss of 60% activity
60
-
1 h, complete loss of activity
60
-
pH 10.0, 1 h, 70% residual activity
65
-
half-life: 14 min
70
30 min, almost complete inactivation
70
-
70% decreased activity
70
-
30 min, 40% loss of activity for the first, 60% loss for the second, and 75% for the third isoform, respectively
70
-
1.5fold activation for isoenzyme HPII, inactivation for isoenzymes HPI-A, HPI-B
70
-
the enzyme retains full activity after incubation for 30 min at 70°C
70
20 min, complete loss of activity
70
-
50% of activity retained for peroxidase activity
70
50 min, 60% residual activity
70
-
purified native enzyme, 15 min, inactivation
80
-
95% decreased activity
80
-
complete loss of activity
80
half-life below 10 min
80
-
60 min, inactivation
80
5 min, 80% loss of activity
80
-
pH 8.0, half-life: 330 h
90
-
catalase activity stable up to
90
-
pH 8.0, half-life: 3 h
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3-step procedure, 65fold
-
3.8fold from cell culture supernatant
-
91fold from crude cell extract
acetone precipitation and Sephadex G-150 gel filtration
active native enzyme by ultracentrifugation, streptomycin sulfate treatment, by drophobic interaction, anion exchange, and hydroxyapatite chromatography, gel filtration, followed by another step of anion exchange chromatography
ammonium sulfate precipitation, DEAE column chromatography, and Sephacryl Tm S-200 gel filtration
ammonium sulfate precipitation, DEAE-Sephadex gel filtration, and Sephacryl gel filtration
-
catalase-peroxidase enzyme to homogeneity, catalase enzyme partial
-
development of simple methods for production and purification of catalases, mineral sorbents binding the enzyme from solution, overview
-
enzyme from a Xanthomonas campestris strain
from culture broth of cells grown on ethanol
-
isoforms Cat-1, Cat-2, Cat-3
native enzyme 106fold from seedlings by ammonium sulfate fractionation and immobilized metal affinity chromatography, best results by using Zn2+ affinity
-
native enzyme 11fold by anion exchange and hydrophobic chromatography, followed by ultrafiltration
native enzyme from cytoplasm and cell envelope
-
native enzyme from the soluble fraction, 47.3fold to homogeneity
-
near homogeneity, 3 isoenzymes
-
near homogeneity, chromatography techniques
partial, recombinant isoenzyme
-
purified to homogeneity as holoprotein by affinity chromatography
Q-Sepharose column chromatography, Superdex 200 gel filtration, and Mono Q column chromatography
-
recombinanat wild-type and mutant His-tagged Cat1.4 isozymes from Escherichia coli strain BL21 (DE3) to homogeneity
-
recombinant enzyme from membranes by solubilization with beta--dodecylmaltoside, immuno-affinity chromatography using a Strep-tagged antibody, and ultrafiltration. X-ray crystallography as well as mass spectrometry analysis reveal no signs for any covalent modification of subunit I besides the crosslink between H276 and Y280
recombinant His-tagged and wild-type enzymes from Bacillus subtilis strain BLF03, 195fold, and Enterococcus faecalis strain V583
-
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3) by nickel affinity chromatography
-
recombinant mutant M244A
-
recombinant soluble and inactive His-tagged catalase-A from Escherichia coli strain BL21(DE3) inclusion bodies by EK-affinity chromatography and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 Star (DE3) to homogeneity by anion exchange chromatography and gel filtration
-
to homogeneity by ammonium sulfate fractionation and several chromatographic steps
-
to homogeneity, chromatography steps
to homogeneity, chromatography techniques
to homogeneity, precipitation and chromatography steps
-
to homogeneity, precipitation and chromatography techniques
to homogeneity, three isoforms
-
Triton X-100 supplementation can markedly improve extracellular ratio of KatA
TvC-II, 300fold to homogeneity, TvC-I partially purified, TvC-I separation from TvC-II
-
-
-
partial
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography steps
Cucurbita sp.
-
to homogeneity, chromatography steps
Kloeckera sp.
-
to homogeneity, chromatography steps
Beta vulgaris var. cicla
-
to homogeneity, chromatography steps
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
-
to homogeneity, chromatography techniques
to homogeneity, chromatography techniques
Capra capra
-
to homogeneity, chromatography techniques
-
to homogeneity, precipitation and chromatography techniques
-
to homogeneity, precipitation and chromatography techniques
-
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DNA and amino acid sequence determination and analysis, phylogenetic analyis
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression during hypoxia and reoxygenation, 1 h after hypoxia, overview
DNA and amino acid sequence determination and analysis, quantitative real-time RT-PCR expression analysis, phylogenetic analysis
DNA andminoa cid sequence determination andd analysis, full length cDNA sequence, RT-PCR expression analysis
expressed in Escherichia coli Rosetta (DE3)
expressed in in MCF-7, Caco-2, and Hct-116 cells, catalase overexpression is associated with increased sensitivity to tisse necrosis facor-alpha
-
expression analysis in strain PAO1 of biofilms of Pseudomonas aeruginosa
-
expression as His-tagged enzyme in constructed enzyme-deficient Bacillus subtilis strain BLF03, overexpression of wild-type and His-tagged enzyme in Enterococcus faecalis strain V583 utilizing an Escherichia coli-Enterococcus faecalis-shuttle plasmid
-
expression in Bacillus subtilis
expression in catalase-deficient Escherichia coli streain UM2
expression in Escherichia coli
expression in Escherichia coli as fusion protein with maltose binding protein
expression in Escherichia coli, 100-fold increase in active enzyme in presence of 1 mM Mn2+ in the induction medium
expression in Pichia pastoris
expression of mutant M244A in Haloferax denitrificans
-
expression of soluble and inactive His-tagged catalase-A in Escherichia coli strain BL21(DE3) in inclusion bodies. Specific requirement of a thioredoxin fusion partner, the involvement of trigger factor protein and the low temperature treatment during induction period for synthesis of completely solubilized rice plant catalase-A in recombinant Escherichia coli. The bacteria require the supplementation of delta-aminolevulinic acid to produce bio-active recombinant rice catalase-A
expression of wild-type and mutant enzymes in Escherichia coli strain BL21 Star (DE3)
-
expression of wild-type and mutant His-tagged Cat1.4 isozymes in Escherichia coli strain BL21 (DE3)
-
gene ctaDII, which codes for subunit I of CcO, expression in Escherichia coli strain DH5alpha, the recombinant enzyme shows reduced catalase activity and thermal stability, overview. Expression of subunit I in the wild-type strain increases the catalase activity by 20fold. Overproduction of SU I might impair the correct insertion of heme a3 and CuB because of a deficiency in metal inserting chaperones. An altered distance between heme a3 and CuB and variations in protein structure are possible reasons for the observed increased catalase activity. Co-expression of chaperone-encoding genes genes ctaG and surf1c reduces the catalase activity of the organism, thermal stability is altered about aging, overview
gene expression analysis during flowering and seed development
-
gene katA, DNA and amino acid sequence determination, comparison, and analysis
gene katA, functional expression in lipodopteran insect cells Sf9 and Sf21 from Spodoptera fruiperda, and High5 from Trichoplusia ni via baculovirus-infection, expression analysis, the amount of apoptotic body formation decreased in transfected cells
-
gene katA, screening of a genetic library, and DNA sequence determination and analysis, phylogenetic analysis, temperature-sensitive expression in enzyme-deficient strain Escherichia coli at 28°C, 200-300fold overexpression in a Xanthomonas campestris mutant strain XpHR
gene katE, expression as fusion enzyme with aldehyde deformylating oxygenase, ADO, from Prochlorococcus marinus
-
gene katP, expression of wild-type and mutant enzymes in strain XL-1 Blue and as His-tagged proteins in BL21(DE3)
-
gene katPc, DNA and amino acid sequence determination and analysis
gene PbcatP, DNA and amino acid sequence determination and analysis, expression analysis, phylogenetic analysis
katB, expression in Escherichia coli
-
when the wild-type and mutant (M129V/E293G) genes are overexpressed in Escherichia coli, unmodified or six-His-tagged proteins of the expected size are overproduced as inactive proteins. To overcome this problem, the Mn2+-dependent catalase genes are overexpressed directly in Thermus thermophilus under the control of the Pnar promoter. This promoter belongs to a respiratory nitrate reductase from of Thermus thermophilus HB8, whose transcription is activated by the combined action of nitrate and anoxia. Upon induction in Thermus thermophilus HB8, a 20fold to 30fold increase in catalase specific activity is observed, whereas a 90fold to 110fold increase is detected when the laboratory strain Thermus thermophilus HB27::nar
-
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
KTL38510
expression in Escherichia coli
expression in Escherichia coli
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agriculture
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amendment of sterilized soils with wild-type Pseudomonas putida restores the rate of degradation of peracetic acid to a higher level than observed in the soils amended with the catalase A-deficient mutant. The association of the bacteria with the plant roots results in protection of the wild-type as well as the catalyse-deficient mutant from killing by peracetic acid
diagnostics
catalase activity is significantly higher in patients with renal cell carcinoma than in controls. The marker catalase might be potentially important as an additional biochemical tool for diagnosing renal cell carcinoma
energy production
combination oflaccase and catalase in construction of H2O2-O2 based biocathode for applications in glucose biofuel cells. The deposited enzymes laccase and catalase by means of alternating current electrophoretic deposition (AC-EPD) do not inhibit each other and carry out about 90% of the catalytic reduction process of O2-H2O2
additional information
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the level of catalase activity in fat body may be a reliable biochemical index to recognize thermotolerant breeds in order to develop resistant hybrids for tropical areas
analysis
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quality of catalase activity as a biomarker, the predictive quality is stress specific
analysis
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quality of catalase activity as a biomarker, the predictive quality is stress specific
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biotechnology
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development of simple methods for production and purification of catalases, determination of adsorption capacity and effects upon binding on enzyme activity of different minerals, binding capacities and activities at different pH/pI, one of the most promising adsorbent is hydroxylapatite, overview
biotechnology
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wheat grass detoxifying substance in production or cultivation of Paramecium on wheat grass powder inoculated with Klebsiella pneumoniae
biotechnology
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wheat grass detoxifying substance in production or cultivation of Paramecium on wheat grass powder inoculated with Klebsiella pneumoniae
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biotechnology
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development of simple methods for production and purification of catalases, determination of adsorption capacity and effects upon binding on enzyme activity of different minerals, binding capacities and activities at different pH/pI, one of the most promising adsorbent is hydroxylapatite, overview
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degradation
application of KatA for elimination of H2O2 after cotton fabrics bleaching leads to less consumption of water, steam and electric power by 25%, 12% and 16.7% respectively without productivity and quality loss of cotton fabrics
degradation
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application of KatA for elimination of H2O2 after cotton fabrics bleaching leads to less consumption of water, steam and electric power by 25%, 12% and 16.7% respectively without productivity and quality loss of cotton fabrics
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industry
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enzyme has potential for application in industrial bleaching processes to remove residual hydrogen peroxide from process streams
industry
hydrogen peroxide scavenging enzyme
industry
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hydrogen peroxide scavenging enzyme
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medicine
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systemic reduction in catalase activity by dsRNA-mediated knock-down significantly reduces the reproductive output of mosquito females. Mutation S2W leads to strain G3 which shows a lower specific activity and higher Km value than the wild-type Ser-isoform. Mutation S2W destabilizes the functional tetrameric form of the enzyme. Ser/Ser females have a significantly higher fecundity than Trp/Trp females
medicine
catalase A1 is a good candidate for the development of an immunoassay for serodiagnosis of infections caused by the Scedosporium apiospermum complex in patients with cystic fibrosis
medicine
design and production of a bifunctional protein with mitochondrial superoxide dismutase and catalase activities plus cell penetrating peptide from HIV-1 Tat to enable cellular internalization. Coexpression of catalase-superoxide dismutase and superoxide dismutase -Tat fusion genes allows simultaneous self-assembly of the protein sequences. The protein complex is expected to contain one tetrameric structure of catalase, four tetrameric structures of superoxide dismutase and twelve units of Tat. The complex shows cellular internalization and superior protection against paraquat-induced cell death
synthesis
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development of simple methods for production and purification of catalases, determination of adsorption capacity and effects upon binding on enzyme activity of different minerals, binding capacities and activities at different pH/pI, one of the most promising adsorbent is hydroxylapatite, overview
synthesis
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covalent immobilization of catalase on florisil via glutaraldehyde. Optimal immobilization is at pH 6.0, 10°C, leading to a vmax of immobilized enzyme of 20 mM H2O2 per min and mg protein and a 50fold increase in Km value. the immobilized enzyme retains 40% of initial activtiy after 50 uses and is more stable than free enzyme
synthesis
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high-density fermentation of recombinant Pichia pastoris in a 1-l-fermentor yields 684800 U/l of catalase, measured with permeabilized cells. Catalase shows a half-life of 4 days at 30°C and cells can be reused for synthesis up to 13 times. Permeabilized cells co-expressing catalase and D-amino acid oxidase convert D-phenylalanine into 99% phenylpyruvate within 100 min. In a batchwise conversion of cephalosporin C, about 90% 7-beta-(4-carboxybutanamido)-cephalosporanic acid is obtained at each cycle
synthesis
method for large-scale expression and purification of recombinant catalase in Pichia pastoris
synthesis
production of recombinant Bacillus subtilis catalase and purification from culture fluid. Purified enzyme has a specific activity of 34600 U/mg and is more resistant to acidic conditions than bovine liver catalase
synthesis
a total soluble catalase activity of 78,762 U/ml with the extracellular ratio of 92.5% is achieved by fed-batch fermentation in a 10 l fermentor
synthesis
glutathione-mediated superoxide generation in an aqueous solution is increased by presence of catalase. The catalase-exaggerated extracellular superoxide generation may give a harmful effect to living cells
synthesis
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immobilization of enzyme onto an epoxy support at 25, 40, and 55°C. All preparations show higher stability than the free enzyme at alkaline pH 10.0. The 55°C immobilizate shows the highest thermal stability
synthesis
KJ472212
immobilized whole cells of the bacterium demonstrate the degradation of hydrogen peroxide (H2O2) in a packed bed reactor
synthesis
improvement of thermal stability, resistance to protease degradation, and resistance to ascorbate inhibition, while retaining enzyme structure and activity, by conjugation to poly(acrylic acid). 55-80% and 90-100% activity is retained for all samples synthesized at pH 5.0 and pH 7.0, respectively, Km or Vmax values do not differ significantly from those of the free enzyme. Conjugates synthesized at pH 7.0 are thermally stable up to 85-90°C, and retain 40-90% of their original activities after storing for 10 weeks at 8°C
synthesis
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production of recombinant Bacillus subtilis catalase and purification from culture fluid. Purified enzyme has a specific activity of 34600 U/mg and is more resistant to acidic conditions than bovine liver catalase
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synthesis
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a total soluble catalase activity of 78,762 U/ml with the extracellular ratio of 92.5% is achieved by fed-batch fermentation in a 10 l fermentor
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synthesis
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development of simple methods for production and purification of catalases, determination of adsorption capacity and effects upon binding on enzyme activity of different minerals, binding capacities and activities at different pH/pI, one of the most promising adsorbent is hydroxylapatite, overview
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