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
-
thiobarbituric
- erythrocyte
- wistar
- endothelial
- xanthine
- glutathione-s-transferase
- artery
- cholesterol
- s-transferase
- caspase-3
-
albino
- chlorophyll
- copper
- heme
- creatinine
- myeloperoxidase
- tnf
-
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
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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Temperature Stability
Temperature Stability on EC 1.11.1.6 - catalase
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100
25 - 70
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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
30 - 60
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thermoinactivation kinetics in the presence or absence of substrate H2O2, overview
35 - 50
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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
37
40
40 - 50
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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
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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
45
50
50 - 60
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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
55
60
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
65
70
80
90
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
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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
15 h, incubation below 40°C, retains most of its activity. Activity is quickly lost above 40°C
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30% loss of activity in 30 min, enzyme from acatalasemic liver has 70% loss of activity in 30 min
50
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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
70
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30 min, 40% loss of activity for the first, 60% loss for the second, and 75% for the third isoform, respectively
70
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1.5fold activation for isoenzyme HPII, inactivation for isoenzymes HPI-A, HPI-B
70
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the enzyme retains full activity after incubation for 30 min at 70°C