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
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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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Application
Application on EC 1.11.1.6 - catalase
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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
analysis
biotechnology
degradation
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
industry
medicine
synthesis
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
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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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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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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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enzyme has potential for application in industrial bleaching processes to remove residual hydrogen peroxide from process streams
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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
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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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