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
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tbars
- biotechnology
- streptozotocin
- agriculture
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ache
- analysis
- comet
- hydroperoxide
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hepatoprotective
-
nephrotoxicity
-
neuroprotective
-
sacrificed
- mannitol
-
defenses
-
h2o2-induced
- urease
- cadmium
-
alt
- industry
-
hepatotoxicity
- degradation
- ischemia
- diagnostics
- gill
-
pro-oxidant
- synthesis
- alpha-tocopherol
- acetylcholinesterase
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aquatic
- medicine
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reperfusion
- polyphenols
- energy production
Reaction
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
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General Information
General Information on EC 1.11.1.6 - catalase
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evolution
malfunction
physiological function
additional information
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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
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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
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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
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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)
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malfunction
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the recombinant enzyme shows reduced catalase activity and thermal stability, overview
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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
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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
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catalase is responsible for the enzymatic destruction/detoxification of hydrogen peroxide, to combat its deleterious effects
physiological function
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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
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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
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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
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catalase is not required for cryotolerance of Listeria monocytogenes
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physiological function
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the catalase activity of CcO is clearly a side reaction
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physiological function
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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
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physiological function
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catalase plays a significant role in preventing Serratia marcescens against cellular damage through hydrogen peroxide
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catalase form III protein and crystal structure analysis, overview
additional information
conserved catalytic active residues are His71, Asn144, and Tyr354
additional information
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conserved catalytic active residues are His71, Asn144, and Tyr354
additional information
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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
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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'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
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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
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the heme-binding pocket contains two highly conserved water molecules on the distal side
additional information
Mycothermus thermophilus ATCC 16454
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the heme-binding pocket contains two highly conserved water molecules on the distal side
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additional information
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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
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additional information
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the enzyme exhibits an extraordinarily high catalase activity, active sites residues are His65, Ser104, and Asn138
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