1.11.1.6: catalase
This is an abbreviated version!
For detailed information about catalase, go to the full flat file.
Word Map on EC 1.11.1.6
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1.11.1.6
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dismutase
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sod
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malondialdehyde
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gsh
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ascorbate
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necrosis
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thiobarbituric
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erythrocyte
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wistar
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endothelial
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xanthine
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glutathione-s-transferase
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artery
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cholesterol
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s-transferase
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caspase-3
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albino
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chlorophyll
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copper
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heme
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creatinine
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myeloperoxidase
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tnf
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anti-oxidant
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peroxisomal
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gsh-px
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tbars
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biotechnology
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streptozotocin
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agriculture
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ache
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analysis
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comet
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hydroperoxide
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hepatoprotective
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nephrotoxicity
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neuroprotective
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sacrificed
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mannitol
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defenses
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h2o2-induced
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urease
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cadmium
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alt
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industry
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hepatotoxicity
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degradation
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ischemia
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diagnostics
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gill
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pro-oxidant
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synthesis
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alpha-tocopherol
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acetylcholinesterase
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aquatic
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medicine
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reperfusion
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polyphenols
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energy production
- 1.11.1.6
- dismutase
- sod
- malondialdehyde
- gsh
- ascorbate
- necrosis
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thiobarbituric
- erythrocyte
- wistar
- endothelial
- xanthine
- glutathione-s-transferase
- artery
- cholesterol
- s-transferase
- caspase-3
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albino
- chlorophyll
- copper
- heme
- creatinine
- myeloperoxidase
- tnf
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anti-oxidant
- peroxisomal
- gsh-px
-
tbars
- biotechnology
- streptozotocin
- agriculture
-
ache
- analysis
- comet
- hydroperoxide
-
hepatoprotective
-
nephrotoxicity
-
neuroprotective
-
sacrificed
- mannitol
-
defenses
-
h2o2-induced
- urease
- cadmium
-
alt
- industry
-
hepatotoxicity
- degradation
- ischemia
- diagnostics
- gill
-
pro-oxidant
- synthesis
- alpha-tocopherol
- acetylcholinesterase
-
aquatic
- medicine
-
reperfusion
- polyphenols
- energy production
Reaction
2 H2O2
=
Synonyms
Ab-catalase, BNC, caperase, CAT, CAT-1, CAT-A, CAT-P, Cat1.4, CatA, catalase, catalase A, catalase C, catalase form III, catalase P, catalase-1, catalase-A, catalase-peroxidase, catalase-phenol oxidase, CatB, CATC, CatF, CatG, CatP, CATPO, CcmC, CP, equilase, H2O2:H2O2 oxidoreductase, haem catalase, HPI-A, HPI-B, HPII, HTHP, hydrogen peroxide oxidoreductase, KAT, Kat E catalase, KatA, KatB, KatC, KatP, KpA, manganese catalase, More, optidase, PktA, polyethylene glycol-catalase, tyrosine-coordinated heme protein, VktA
ECTree
1.11.1.6 catalaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 1.11.1.6 - catalase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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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
dinitrosyl iron complex
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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
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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
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purified on catalase-Sepharose from bovine, different inhibition sensitivities for three isoforms
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gamma-linolenic acid
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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
inositol phosphoglycan-like compound from Bos taurus thyroid gland
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produced by the hydrolysis of the membrane-bound glycosyl phosphoinositides, noncompetitive inhibition. 50% residual activity, the site of action is not the prosthetic group
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inositol phosphoglycan-like compound from Escherichia coli
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produced by the hydrolysis of the membrane-bound glycosyl phosphoinositides, noncompetitive inhibition. 50% residual activity, the site of action is not the prosthetic group
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linoleic acid
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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
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
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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
p-chloromercuribenzoate
Capra capra
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complete inhibition at 0.33 mM, summation effect with 2-mercaptoethanol
palmitic acid
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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
pyocyanin
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may decrease cellular catalase activity via both transcriptional regulation and direct inactivation of the enzyme
stearic acid
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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
2-mercaptoethanol
Capra capra
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complete inhibition at 23 mM, summation effect with p-chloromercuribenzoate
3-Amino-1,2,4-triazole
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inhibitory. Inhibition of extracellular catalase activity leads to a striking inactivation of secreted cysteine cathepsins
3-Amino-1,2,4-triazole
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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
500 microM reduces the reactivity of catalase to 50%
3-amino-1H-1,2,4-triazole
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retains 38% of its initial activity in the presence of 40 mM
3-amino-1H-1,2,4-triazole
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isoenzyme HPI: 25% inhibition at 10 mM, isoenzyme HPII: 70-80% inhibition at 10 mM
3-amino-1H-1,2,4-triazole
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no effect on catalase-peroxidase enzyme
3-amino-1H-1,2,4-triazole
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strong inhibition for isoforms Cat-1, Cat-2, 32% inhibition for isoform Cat-3 at 10 mM
azide
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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
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very strong inhibitor of erythrocytic CAT but a relatively weak CAT inhibitor in human hemolysates
azide
irreversible inhibitor, effective at concentrations less than1 mM
Cd2+
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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
cyanide
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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
dithiothreitol
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the activity can be inhibited by 75% by addition of 5 mM dithiothreitol
Glutaraldehyde
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the presence of trace amount of glutaraldehyde in immobilization medium causes the catalase activity to decline
H2O2
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excess H2O2 inhibits the enzyme. In the presence of excess H2O2, [FeII/FeII]-ADEec rapidly loses its ability to deaminate adenine
H2O2
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50% inhibition for catalase at 4.5 mM, for peroxidase at 0.4 mM
hydroxylamine
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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
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50% inhibition for catalase at 0.002 mM, for peroxidase at 0.078 mM
KCN
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inhibitory. Inhibition of extracellular catalase activity leads to a striking inactivation of secreted cysteine cathepsins
KCN
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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
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50% inhibition of both catalase and peroxidase activities at 0.02 mM
NaCl
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50 mM, 30% residual activity in leaf, 24% residual activity in nodule
NaN3
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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
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50% inhibition for catalase at 0.15 mM, for peroxidase at 0.73 mM
nitrite
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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
Sodium cyanide
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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
additional information
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enzyme inhibition by flavonoids, structure-function relationship, overview
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additional information
not inhibited by exposure of cells to 3-amino-1,2,4-triazole
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additional information
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not inhibited by exposure of cells to 3-amino-1,2,4-triazole
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additional information
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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
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additional information
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oxygenation of active site residues, inhibiting catalase activity, occurs via release of hydroxyl radicals
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additional information
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tissue necrosis factor-alpha treatment causes downregulation of catalase expression in MCF-7, Caco-2 and Hct-116 cancer cell lines
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additional information
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acetazolamide and nitrate at concentrations up to 0.1 mM do not inhibit erythrocytic CAT activity
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additional information
enzyme is not inhibited by presence of 5 mM sodium azide
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additional information
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enzyme is not inhibited by presence of 5 mM sodium azide
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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%
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additional information
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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%
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additional information
no effect by 0.01 mM hydrogen peroxide or 100 nM paraquat
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additional information
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no effect by 0.01 mM hydrogen peroxide or 100 nM paraquat
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additional information
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Ni2+, Ca2+, Mg2+ and Mn2+ have both enhancing and inhibitory effects
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