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
-
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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Engineering
Engineering on EC 1.11.1.6 - catalase
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S2W
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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
Y111A
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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
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coplete loss of catalase activity, increased peroxidase activity due to enhanced affinity for the peroidatic substrate
S315T
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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
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mutation in key distal side residue, disrupts high-affinity binding of substrate isonicotinic hydrazide
Y229F
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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
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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
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
Mycothermus thermophilus ATCC 16454
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site-directed mutagenesis, the mutation results in conversion of the native d-type heme to a b-type heme
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L189W/H225T
almost 3fold decrease in Km-value, 2-2.5fold increase in enzyme velocity, loss of photoinhibition
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
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mutant in heme-binding residue, almost complete loss of activity
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V71A and F158A
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channel point mutant, about 20% of wild-type activity
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Y353A
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mutant in heme-binding residue, almost complete loss of activity
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additional information
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systemic reduction in catalase activity by dsRNA-mediated knock-down significantly reduces the reproductive output of mosquito females
additional information
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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
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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
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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
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additional information
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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
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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
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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
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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
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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
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additional information
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loss of enzyme activity results in a temperature-dependent hydrogen peroxide sensitivity, correlating with its temperature-inducible expression pattern
additional information
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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
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the expression of katA is downregulated 7.7fold in biofilm cultures of Pseudomonas aeruginosa
additional information
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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
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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
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additional information
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mutant lacking enzymic activity is more sensitive to peracetic acid than wild-type
additional information
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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