Information on EC 1.11.1.6 - catalase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.11.1.6
-
RECOMMENDED NAME
GeneOntology No.
catalase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 H2O2 = O2 + 2 H2O
show the reaction diagram
A hemoprotein. This enzyme can also act as a peroxidase, EC 1.11.1.7, for which several organic substances, especially ethanol, can act as a hydrogen donor. A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase. Enzymes from some microorganisms, such as Penicillium simplicissimum, which exhibit both catalase and peroxidase activity, have sometimes been referred to as catalase-peroxidase
-
-
-
2 H2O2 = O2 + 2 H2O
show the reaction diagram
reaction mechanism, overview
-
2 H2O2 = O2 + 2 H2O
show the reaction diagram
reaction mechanism, overview
Scytalidium thermophilum ATCC 16454
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
conversions
-
-
ethanol degradation IV
-
-
Glyoxylate and dicarboxylate metabolism
-
-
methanol oxidation to formaldehyde IV
-
-
reactive oxygen species degradation
-
-
superoxide radicals degradation
-
-
Tryptophan metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen-peroxide:hydrogen-peroxide oxidoreductase
A hemoprotein. A manganese protein containing MnIII in the resting state, which also belongs here, is often called pseudocatalase. The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor. Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21, catalase-peroxidase.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
caperase
-
-
-
-
CAT
-
-
-
-
catalase-peroxidase
-
-
-
-
equilase
-
-
-
-
optidase
-
-
-
-
polyethylene glycol-catalase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-05-2
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme expression is induced under phosphate-limiting growth conditions
-
-
Manually annotated by BRENDA team
isoform CatA
-
-
Manually annotated by BRENDA team
isoform CatB
-
-
Manually annotated by BRENDA team
isozyme Cat1.4
-
-
Manually annotated by BRENDA team
strain OF4
-
-
Manually annotated by BRENDA team
Bacillus firmus OF4
strain OF4
-
-
Manually annotated by BRENDA team
strain ATCC 14581
-
-
Manually annotated by BRENDA team
strain 13
-
-
Manually annotated by BRENDA team
strain N2a
-
-
Manually annotated by BRENDA team
strain 13
-
-
Manually annotated by BRENDA team
strain N2a
-
-
Manually annotated by BRENDA team
Bacillus subtilis KatA
KatA
Uniprot
Manually annotated by BRENDA team
Bacillus subtilis KatA
KatA
-
-
Manually annotated by BRENDA team
Beta vulgaris var. cicla
-
-
-
Manually annotated by BRENDA team
originally isolated from honeybee intestine, gene katA
UniProt
Manually annotated by BRENDA team
Bifidobacterium asteroides JCM 8230
originally isolated from honeybee intestine, gene katA
UniProt
Manually annotated by BRENDA team
commercial preparation
-
-
Manually annotated by BRENDA team
Brassica oleracea gongylodes, kohlrabi
-
-
Manually annotated by BRENDA team
three enzyme isoforms
-
-
Manually annotated by BRENDA team
bifunctional catalase-peroxidase KatG
UniProt
Manually annotated by BRENDA team
Capra capra
goat
-
-
Manually annotated by BRENDA team
microfungus isolated from soil collected in arctic tundra
-
-
Manually annotated by BRENDA team
Colwellia sp.
strain MH2
-
-
Manually annotated by BRENDA team
Colwellia sp. MH2
strain MH2
-
-
Manually annotated by BRENDA team
Pacific oyster
-
-
Manually annotated by BRENDA team
Cucurbita sp.
pumpkin
-
-
Manually annotated by BRENDA team
bifunctional catalase-peroxidase KatG
-
-
Manually annotated by BRENDA team
gene katE
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
strain O157:H7, gene katP
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
LLR02022, contains a catalase and a bifunctional catalase-peroxidase
-
-
Manually annotated by BRENDA team
bifunctional catalase-peroxidase KatG
-
-
Manually annotated by BRENDA team
cv. Fructidor
-
-
Manually annotated by BRENDA team
catalase activity in an msr strain is one-half that of the parent strain. This difference is only observed under oxidative stress conditions, and the activity is restored to nearly wild-type levels by adding methionine sulfoxide reductase plus dithiothreitol to msr strain extracts
-
-
Manually annotated by BRENDA team
strain 26695, gene katA, enzyme KatA
-
-
Manually annotated by BRENDA team
strain Taiwanese TW-34, gene katA, enzyme KatA
-
-
Manually annotated by BRENDA team
strain 26695, gene katA, enzyme KatA
-
-
Manually annotated by BRENDA team
Helicobacter pylori Taiwanese TW-34
strain Taiwanese TW-34, gene katA, enzyme KatA
-
-
Manually annotated by BRENDA team
patients with acne vulgaris
-
-
Manually annotated by BRENDA team
strain IFO 14940
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae IFO 14940
strain IFO 14940
-
-
Manually annotated by BRENDA team
Kloeckera sp.
strain 2201
-
-
Manually annotated by BRENDA team
Kloeckera sp. 2201
strain 2201
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
Listeria monocytogenes F2365
-
-
-
Manually annotated by BRENDA team
ATCC 51441, ATCC 51442, and ATCC 51440
-
-
Manually annotated by BRENDA team
microfungus isolated from soil collected in arctic tundra
-
-
Manually annotated by BRENDA team
microfungus isolated from soil collected in arctic tundra, 2 strains
-
-
Manually annotated by BRENDA team
Balb/c mice
-
-
Manually annotated by BRENDA team
male C57BL/6 mice and type II diabetic mice
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
Balb/c mice
-
-
Manually annotated by BRENDA team
strain JC1, DSM 3803
-
-
Manually annotated by BRENDA team
Mycobacterium sp. JC1
strain JC1, DSM 3803
-
-
Manually annotated by BRENDA team
bifunctional catalase-peroxidase KatG
-
-
Manually annotated by BRENDA team
clinical isolates from Malatya, Turkey
-
-
Manually annotated by BRENDA team
microfungus isolated from soil collected in arctic tundra, 2 strains
-
-
Manually annotated by BRENDA team
isoform Cat-2
SwissProt
Manually annotated by BRENDA team
isoforms Cat-1, Cat-2, Cat-3
-
-
Manually annotated by BRENDA team
no activity in Amphiprora kufferathii
-
-
-
Manually annotated by BRENDA team
subspecies Oceanobacillus oncorhynchi incaldaniensis, strain 20AG
-
-
Manually annotated by BRENDA team
CAT-A
UniProt
Manually annotated by BRENDA team
isoform catalase-B
UniProt
Manually annotated by BRENDA team
Pb01, ATCC-MYA-826
SwissProt
Manually annotated by BRENDA team
strain ATCC MYA-826
UniProt
Manually annotated by BRENDA team
Paracoccidioides brasiliensis ATCC MYA-826
-
SwissProt
Manually annotated by BRENDA team
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
Pb01, ATCC-MYA-826
SwissProt
Manually annotated by BRENDA team
cytochrome c oxidase with catalase activity; gene ctaG
UniProt
Manually annotated by BRENDA team
Paracoccus denitrificans AO1
cytochrome c oxidase with catalase activity; gene ctaG
UniProt
Manually annotated by BRENDA team
microfungus isolated from soil collected in arctic tundra
-
-
Manually annotated by BRENDA team
strain 1, microfungus isolated from soil collected in arctic tundra
-
-
Manually annotated by BRENDA team
Penicillium cyclopium 1
strain 1, microfungus isolated from soil collected in arctic tundra
-
-
Manually annotated by BRENDA team
isoform Cat1
UniProt
Manually annotated by BRENDA team
isoform Cat2
UniProt
Manually annotated by BRENDA team
isoform Cat3
UniProt
Manually annotated by BRENDA team
Pibocella sp.
strain MH3
-
-
Manually annotated by BRENDA team
Pibocella sp. MH3
strain MH3
-
-
Manually annotated by BRENDA team
microfungus isolated from soil collected in arctic tundra
-
-
Manually annotated by BRENDA team
enzyme expression is induced under phosphate-limiting growth conditions
-
-
Manually annotated by BRENDA team
strain PAO1, gene katA
-
-
Manually annotated by BRENDA team
strains ATCC 17400 and PAO1, gene ccmC
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PA14 KatA
KatA
-
-
Manually annotated by BRENDA team
strain mt-2. Expression of the katB gene encoding isoform catalase B is specific to the stationary phase and entirely dependent on the rpoS gene, while the katA gene expressed during log phase partially requires rpoS
-
-
Manually annotated by BRENDA team
Pseudomonas putida mt-2.
strain mt-2. Expression of the katB gene encoding isoform catalase B is specific to the stationary phase and entirely dependent on the rpoS gene, while the katA gene expressed during log phase partially requires rpoS
-
-
Manually annotated by BRENDA team
pv. syringae 61
-
-
Manually annotated by BRENDA team
isolated from the drain pool of a plant that uses H2O2 as a bleaching agent
UniProt
Manually annotated by BRENDA team
Psychrobacter piscatorii T-3
isolated from the drain pool of a plant that uses H2O2 as a bleaching agent
UniProt
Manually annotated by BRENDA team
strain VA1, hyperthermophilic archaeon, facultatively anaerobic, gene katPc
SwissProt
Manually annotated by BRENDA team
Pyrobaculum calidifontis VA1
strain VA1, hyperthermophilic archaeon, facultatively anaerobic, gene katPc
SwissProt
Manually annotated by BRENDA team
Rattus norvegicus Wistar
Wistar
-
-
Manually annotated by BRENDA team
enzyme does not show peroxidase activity
-
-
Manually annotated by BRENDA team
Rhodospirillum rubrum S1
strain S1
-
-
Manually annotated by BRENDA team
Roseibacterium elongatum OCh 323
OCh 323
-
-
Manually annotated by BRENDA team
strain EL-88
-
-
Manually annotated by BRENDA team
Roseisalinus antarcticus EL-88
strain EL-88
-
-
Manually annotated by BRENDA team
Sclerotium sp.
isolated from soil collected in arctic tundra
-
-
Manually annotated by BRENDA team
bifunctional catalase-phenol oxidase
-
-
Manually annotated by BRENDA team
type culture Humicola insolens, ATCC 16454
-
-
Manually annotated by BRENDA team
Scytalidium thermophilum ATCC 16454
gene catpo
-
-
Manually annotated by BRENDA team
Serratia marcescens SYBC08
-
UniProt
Manually annotated by BRENDA team
isoform KatA, enzyme expression is induced under phosphate-limiting growth conditions resulting in dramatic increase in H2O2 resistance of wild-type cells, but not of promoter phoB mutant cells
-
-
Manually annotated by BRENDA team
Stenotrophomonas maltophilia WZ2
strain WZ2
-
-
Manually annotated by BRENDA team
Sulfitobacter sp.
strain MH1
-
-
Manually annotated by BRENDA team
Sulfitobacter sp. MH1
strain MH1
-
-
Manually annotated by BRENDA team
microfungus isolated from soil collected in arctic tundra, 2 strains
-
-
Manually annotated by BRENDA team
strain F-648
-
-
Manually annotated by BRENDA team
strains F-648 and A-3
-
-
Manually annotated by BRENDA team
Talaromyces piceae F-648
strain F-648
-
-
Manually annotated by BRENDA team
2 enzymes TvC-I and TvC-II
-
-
Manually annotated by BRENDA team
catalase VktA
UniProt
Manually annotated by BRENDA team
strain HY34
-
-
Manually annotated by BRENDA team
Wenxinia marina HY34
strain HY34
-
-
Manually annotated by BRENDA team
pv. phaseoli, gene katA, enzyme KatA is the major enzyme of 2 different occurring in the organism
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
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
B3FXQ9
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
Psychrobacter piscatorii T-3
-
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
-
malfunction
-
catalase-negative mutant ROA3 exhibits impaired growth, with the extent of impairment increasing with decreasing temperature, and no growth is detected at 4C. Aerobic growth in liquid is impaired at 4C, especially under aeration, but not at higher temperatures (10, 25, or 37C)
malfunction
P08303
the recombinant enzyme shows reduced catalase activity and thermal stability, overview
malfunction
Listeria monocytogenes F2365
-
catalase-negative mutant ROA3 exhibits impaired growth, with the extent of impairment increasing with decreasing temperature, and no growth is detected at 4C. Aerobic growth in liquid is impaired at 4C, especially under aeration, but not at higher temperatures (10, 25, or 37C)
-
physiological function
-
catalase is not required for cryotolerance of Listeria monocytogenes
physiological function
D7RJ66
catalase plays a significant role in preventing Serratia marcescens against cellular damage through hydrogen peroxide
physiological function
A0S5U0
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
-
catalase is an antioxidant enzyme and plays a significant role in the protection against oxidative stress by reducing hydrogen peroxide
physiological function
Q6R2J1
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
C8XTA9
catalase is an important antioxidant protein that protects organisms against various oxidative stresses by eliminating hydrogen peroxide
physiological function
-
catalase is responsible for the enzymatic destruction/detoxification of hydrogen peroxide, to combat its deleterious effects
physiological function
-
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
A3REN3
chaperone-specific enzyme regulation, overview
physiological function
-
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
P08303
the catalase activity of CcO is clearly a side reaction
physiological function
-
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
Listeria monocytogenes F2365
-
catalase is not required for cryotolerance of Listeria monocytogenes
-
physiological function
Paracoccus denitrificans AO1
-
the catalase activity of CcO is clearly a side reaction
-
physiological function
Serratia marcescens SYBC08
-
catalase plays a significant role in preventing Serratia marcescens against cellular damage through hydrogen peroxide
-
malfunction
Paracoccus denitrificans AO1
-
the recombinant enzyme shows reduced catalase activity and thermal stability, overview
-
additional information
-
catalase form III protein and crystal structure analysis, overview
additional information
C8XTA9
conserved catalytic active residues are His71, Asn144, and Tyr354
additional information
A0S5U0
homology modelling, overview
additional information
-
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
-
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
B3FXQ9
the enzyme exhibits an extraordinarily high catalase activity, active sites residues are His65, Ser104, and Asn138
additional information
A3REN3
the enzyme is a mono-functional plant catalase
additional information
P08303
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
-
the heme-binding pocket contains two highly conserved water molecules on the distal side
additional information
Paracoccus denitrificans AO1
-
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
Psychrobacter piscatorii T-3
-
the enzyme exhibits an extraordinarily high catalase activity, active sites residues are His65, Ser104, and Asn138
-
additional information
Scytalidium thermophilum ATCC 16454
-
the heme-binding pocket contains two highly conserved water molecules on the distal side
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-H-pyrrol-2-carbohydrazide
?
show the reaction diagram
-
analysis of association and dissociation rate constants
-
-
-
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
P00432
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
P08303
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
A0S5U0
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
B3FXQ9
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
A3REN3
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
C8XTA9
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Q6R2J1
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
L8B3D7
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
via intermediate Compound I
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
via Compound I and Compound II intermediates
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Paracoccus denitrificans AO1
P08303
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Bifidobacterium asteroides JCM 8230
L8B3D7
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Psychrobacter piscatorii T-3
B3FXQ9
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Scytalidium thermophilum ATCC 16454
-
via Compound I and Compound II intermediates
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
show the reaction diagram
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
show the reaction diagram
Bacillus firmus, Bacillus firmus OF4
-
only isoenzyme I has peroxidase activity
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
show the reaction diagram
Penicillium simplicissimum CBS 170.90
-
-
-
?
2,6-dimethoxyphenol + H2O2
? + H2O
show the reaction diagram
Penicillium simplicissimum, Penicillium simplicissimum CBS 170.90
-
-
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
show the reaction diagram
-
-
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
show the reaction diagram
-
-
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
show the reaction diagram
-
-
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
show the reaction diagram
Q8X182
isoform Cat-2
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
show the reaction diagram
Penicillium simplicissimum CBS 170.90
-
-
-
?
3,3'-dimethoxybenzidine + H2O2
? + H2O
show the reaction diagram
Penicillium simplicissimum, Penicillium simplicissimum CBS 170.90
-
-
-
?
4-aminoantipyrine + H2O2
? + H2O
show the reaction diagram
-
-
-
?
ascorbate + H2O2
? + H2O
show the reaction diagram
-
-
-
?
ascorbate + H2O2
? + H2O
show the reaction diagram
-
-
-
?
ascorbate + H2O2
? + H2O
show the reaction diagram
Q8X182
isoform Cat-2
-
?
benzoic hydrazide
?
show the reaction diagram
-
analysis of association and dissociation rate constants
-
-
-
beta-(3,4-dihydroxyphenyl)-L-alanine + H2O2
? + H2O
show the reaction diagram
-
-
-
-
beta-(3,4-dihydroxyphenyl)-L-alanine + H2O2
? + H2O
show the reaction diagram
Kloeckera sp., Kloeckera sp. 2201
-
low activity
-
?
catechol + H2O2
? + H2O
show the reaction diagram
-
-
-
?
ethanol + H2O2
acetaldehyde + ?
show the reaction diagram
-
-
-
?
ethanol + H2O2
acetaldehyde + ?
show the reaction diagram
-
-
-
?
ethanol + H2O2
acetaldehyde + ?
show the reaction diagram
-
no peroxidase activity
-
?
ethyl hydrogen peroxide + ethanol
acetaldehyde + ?
show the reaction diagram
-
-
-
?
ethyl hydrogen peroxide + methanol
acetaldehyde + ?
show the reaction diagram
-
-
-
?
ethyl hydrogen peroxide + nitrite
acetaldehyde + ?
show the reaction diagram
-
-
-
?
formic acid + H2O2
?
show the reaction diagram
-
-
-
?
furoic hydrazide
?
show the reaction diagram
-
analysis of association and dissociation rate constants
-
-
-
H2O
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q9AQQ9
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q9XHH3
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Cucurbita sp.
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Kloeckera sp.
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q9C4N4
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Beta vulgaris var. cicla
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Capra capra
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Capra capra
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q8X220
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q8L2Z7
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
A5XB38
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
P04040
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
A8CFD3
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q5LLG6
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q6RSH8
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
P04762
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
D7RJ66
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q9C168
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
no peroxidase activity
-
?
H2O2
O2 + H2O
show the reaction diagram
-
no peroxidase activity
-
?
H2O2
O2 + H2O
show the reaction diagram
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
Q8X182
two monofunctional catalases, Cat-1 and Cat-3, one catalase-peroxidase enzyme, Cat-2
-
?
H2O2
O2 + H2O
show the reaction diagram
-
no peroxidase-activity
-
?
H2O2
O2 + H2O
show the reaction diagram
-
three isoenzymes, Cat-1, Cat-2 and Cat-3
-
?
H2O2
O2 + H2O
show the reaction diagram
-
one catalase-peroxidase, one catalase enzyme
-
?
H2O2
O2 + H2O
show the reaction diagram
-
abnormal reaction kinetics
-
?
H2O2
O2 + H2O
show the reaction diagram
-
abnormal reaction kinetics
-
?
H2O2
O2 + H2O
show the reaction diagram
-
monofunctional catalase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
monofunctional catalase
-
?
H2O2
O2 + H2O
show the reaction diagram
O93662
monofunctional catalase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
KatA catalase important for resistance of planctonic and biofilm cells to H2O2
-
?
H2O2
O2 + H2O
show the reaction diagram
-
one monofunctional, two bifunctional catalases
-
?
H2O2
O2 + H2O
show the reaction diagram
-
two monofunctional, one bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
involved in acatalasemia
-
?
H2O2
O2 + H2O
show the reaction diagram
-
involved in acatalasemia
-
?
H2O2
O2 + H2O
show the reaction diagram
-
regulator of H2O2-levels or protective function for hemoglobin or other SH-proteins
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification and protection enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q6LA34
detoxification enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification enzyme, enzyme is naturally adapted to the cold climate of the arctic tundra
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification enzyme, enzyme protects the cell against high concentrations of peroxide
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
enzyme is responsible for prevention of dehydration-related oxidative damage during seed desiccation, H2O2 may play a role for enzyme expression regulation and in the transduction pathway
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
enzyme is responsible for the protection of the Helicobacter pylori cells against phagocyte attack in the gastric mucosa by disumtation of H2O2
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q8X220
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
H2O2 decomposition is accompanied by enzyme inactivation which can be minimized in vitro by immobilization of the enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q8L2Z7
protective role of the enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
catalase activity
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q6LA34
with pyrogallol as electron donor
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
essential for optimal resistance to H2O2. KatB was not produced during the normal growth cycle. Catalase activity is greater in nonmucoid than in mucoid, alginate-producing organisms. When exposed to hydrogen peroxide and, to a greater extent, paraquat, total catalase activity was elevated 7fold to 16fold, respectively
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Bacillus firmus OF4
-
two monofunctional, one bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
Penicillium cyclopium 1
-
detoxification enzyme, enzyme is naturally adapted to the cold climate of the arctic tundra
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Rhodospirillum rubrum S1
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Kloeckera sp. 2201
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Stenotrophomonas maltophilia WZ2
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Listeria monocytogenes F2365
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Mycobacterium sp. JC1
-
catalase activity
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Paracoccidioides brasiliensis ATCC MYA-826
Q8X220
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
enzyme is responsible for the protection of the Helicobacter pylori cells against phagocyte attack in the gastric mucosa by disumtation of H2O2
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Klebsiella pneumoniae IFO 14940
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Mycobacterium sp. JC1 DSM 3803
-
catalase activity
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Helicobacter pylori Taiwanese TW-34
-
detoxification and protection enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
Q8X220
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Talaromyces piceae F-648
-
H2O2 decomposition is accompanied by enzyme inactivation which can be minimized in vitro by immobilization of the enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Serratia marcescens SYBC08
D7RJ66
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Pyrobaculum calidifontis VA1
Q6LA34
detoxification enzyme, with pyrogallol as electron donor
-
-
?
H2O2 + 2-aminophenol
?
show the reaction diagram
-
-
-
-
?
H2O2 + 3-chlorophenol
?
show the reaction diagram
-
-
-
-
?
H2O2 + 4-chlorophenol
?
show the reaction diagram
-
-
-
-
?
H2O2 + 4-nitrophenol
?
show the reaction diagram
-
-
-
-
?
H2O2 + dimethylaniline
?
show the reaction diagram
-
low activity
-
-
?
H2O2 + methanol
formaldehyde + H2O
show the reaction diagram
Mycobacterium sp., Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803
-
peroxidase activity
-
-
?
H2O2 + o-dianisidine
? + H2O
show the reaction diagram
Mycobacterium sp., Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803
-
peroxidase activity
-
-
?
H2O2 + phenol
?
show the reaction diagram
-
-
-
-
?
H2O2 + propyl gallate
?
show the reaction diagram
-
best peroxidase substrate
-
-
?
H2O2 + pyrocatechol
?
show the reaction diagram
-
-
-
-
?
isonicotinic hydrazide
?
show the reaction diagram
-
antituberculosis drug, bactericidal function neeeds activation by bifunctional catalase-peroxidase KatG to produce an acyl-NAD adduct. Substrate binds with high affinity to a small protion of ferric enzyme in a six-coordinate heme iron form
-
-
?
methanol + H2O2
formaldehyde + ?
show the reaction diagram
-
-
-
?
methanol + H2O2
formaldehyde + ?
show the reaction diagram
-
-
-
?
methanol + H2O2
formaldehyde + ?
show the reaction diagram
Kloeckera sp., Kloeckera sp. 2201
-
only in the presence of glucose and glucose oxidase
-
?
NADH + H2O2
NAD+ + H2O
show the reaction diagram
-
-
-
?
NADPH + H2O2
NADP+ + H2O
show the reaction diagram
-
-
-
?
nicotinic hydrazide
?
show the reaction diagram
-
analysis of association and dissociation rate constants
-
-
-
o-dianisidine + H2O2
? + H2O
show the reaction diagram
-
-
-
?
o-dianisidine + H2O2
? + H2O
show the reaction diagram
-
-
-
?
o-dianisidine + H2O2
? + H2O
show the reaction diagram
Q8X182
isoform Cat-2
-
?
o-dianisidine + H2O2
? + H2O
show the reaction diagram
-
peroxidatic activity
-
?
o-methoxyphenol + H2O2
? + H2O
show the reaction diagram
Q8X182
isoform Cat-2
-
?
o-methoxyphenol + H2O2
? + H2O
show the reaction diagram
-
only isoenzyme I has peroxidase activity
-
?
o-methoxyphenol + H2O2
? + H2O
show the reaction diagram
Q8X182
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
show the reaction diagram
-
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
show the reaction diagram
-
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
show the reaction diagram
-
i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
show the reaction diagram
Bacillus firmus OF4
-
only isoenzyme I has peroxidase activity, i.e. guaiacol
-
?
o-methoxyphenol + H2O2
? + H2O
show the reaction diagram
Penicillium simplicissimum CBS 170.90
-
i.e. guaiacol
-
?
picolinic hydrazide
?
show the reaction diagram
-
analysis of association and dissociation rate constants
-
-
-
pyrogallol + H2O2
? + H2O
show the reaction diagram
-
-
-
?
pyrogallol + H2O2
? + H2O
show the reaction diagram
-
-
-
?
reduced cytochrome c + H2O2
oxidized cytochrome c + H2O
show the reaction diagram
-
-
-
?
methyl hydrogen peroxide
formaldehyde + ?
show the reaction diagram
-
-
-
?
additional information
?
-
-
regulation of enzyme expression and activity by drying occurs on transcriptional level, increase in enzyme activity during drying is associated with an decrease of H2O2 level and lipid peroxidation
-
-
-
additional information
?
-
-
the enzyme has negligible inhibitory effects on endothelium-dependent relaxations in mouse isolated aorta and small mesenteric artery which are not caused by H2O2, endothelium-independent relaxations are caused by H2O2 and are abolished by the enzyme, overview
-
-
-
additional information
?
-
-
2 enzymes TvC-I and TvC-II do not show peroxidase ctivity
-
-
-
additional information
?
-
-
enzyme also shows alkaline peroxidase activity, which is much lower than the catalase activity, no peroxidase activity with 3-aminophenol, 2,4,6-trichlorophenol, and 3-nitrophenol
-
-
-
additional information
?
-
-
enzyme is easiliy reduced by dithionite, no peroxidase activity with o-dianisidine and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
-
additional information
?
-
-
the enzyme contains a unique tetra-lysine motif at the C-terminus which probably is required for interaction with protein KapA
-
-
-
additional information
?
-
-
the enzyme does not interact with Brij 35 micelles, enzyme exhibits superactivity in the reverse micells formed by 0.1 M Brij 30 in heptane, isooctane, and dodecane, but not in decaline
-
-
-
additional information
?
-
-
peroxidase and catalase activities are involved in direct adventitious shoot formation induced by thidiazuron in zygotic embryos
-
-
-
additional information
?
-
-
no detectable peroxidase activity
-
-
-
additional information
?
-
-
CcmC is a key determinant for cytochrome c biogenesis, pyoverdine maturation, and expression of some quorum sensing-regulated traits
-
-
-
additional information
?
-
-
the enzyme is involved in protection against peroxides and oxidative DNA damage, it is downregulated in biofilm cultures of Pseudomonas aeruginosa, that display up to a 105fold increase in mutability compared with planktonic cultures
-
-
-
additional information
?
-
-
BNC does not show any peroxidatic activity with 4-aminoantipyrine or pyrogallol as substrate
-
-
-
additional information
?
-
-
adenine deaminase, EC 3.5.4.2, from the amidohydrolase superfamily of enzymes catalyzes the conversion of adenine to hypoxanthine and ammonia. But it also catalyzes the catalase reaction converting H2O2 to H2O and O2. [MnII/MnII]-ADEec is active as a deaminase but not as a catalase. In contrast, [FeII/FeII]-ADEec catalyzes both reactions
-
-
-
additional information
?
-
P08303
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
-
additional information
?
-
-
the bifunctional catalase with phenol oxidase activity catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds
-
-
-
additional information
?
-
Rhodospirillum rubrum S1
-
no detectable peroxidase activity
-
-
-
additional information
?
-
Paracoccus denitrificans AO1
P08303
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
-
additional information
?
-
-
enzyme also shows alkaline peroxidase activity, which is much lower than the catalase activity, no peroxidase activity with 3-aminophenol, 2,4,6-trichlorophenol, and 3-nitrophenol
-
-
-
additional information
?
-
-
the enzyme contains a unique tetra-lysine motif at the C-terminus which probably is required for interaction with protein KapA
-
-
-
additional information
?
-
-
BNC does not show any peroxidatic activity with 4-aminoantipyrine or pyrogallol as substrate
-
-
-
additional information
?
-
Scytalidium thermophilum ATCC 16454
-
the bifunctional catalase with phenol oxidase activity catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
P00432
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
P08303
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
A0S5U0
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
B3FXQ9
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
A3REN3
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
C8XTA9
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Q6R2J1
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
L8B3D7
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
-
via intermediate Compound I
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Paracoccus denitrificans AO1
P08303
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Bifidobacterium asteroides JCM 8230
L8B3D7
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Psychrobacter piscatorii T-3
B3FXQ9
-
-
-
?
2 H2O2
O2 + 2 H2O
show the reaction diagram
Scytalidium thermophilum ATCC 16454
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Cucurbita sp.
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Kloeckera sp.
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q9C4N4
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Beta vulgaris var. cicla
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Capra capra
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Capra capra
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q9C168
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
no peroxidase activity
-
?
H2O2
O2 + H2O
show the reaction diagram
-
no peroxidase activity
-
?
H2O2
O2 + H2O
show the reaction diagram
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
Q8X182
two monofunctional catalases, Cat-1 and Cat-3, one catalase-peroxidase enzyme, Cat-2
-
?
H2O2
O2 + H2O
show the reaction diagram
-
no peroxidase-activity
-
?
H2O2
O2 + H2O
show the reaction diagram
-
three isoenzymes, Cat-1, Cat-2 and Cat-3
-
?
H2O2
O2 + H2O
show the reaction diagram
-
one catalase-peroxidase, one catalase enzyme
-
?
H2O2
O2 + H2O
show the reaction diagram
-
abnormal reaction kinetics
-
?
H2O2
O2 + H2O
show the reaction diagram
-
abnormal reaction kinetics
-
?
H2O2
O2 + H2O
show the reaction diagram
-
monofunctional catalase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
monofunctional catalase
-
?
H2O2
O2 + H2O
show the reaction diagram
O93662
monofunctional catalase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
KatA catalase important for resistance of planctonic and biofilm cells to H2O2
-
?
H2O2
O2 + H2O
show the reaction diagram
-
one monofunctional, two bifunctional catalases
-
?
H2O2
O2 + H2O
show the reaction diagram
-
two monofunctional, one bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
-
involved in acatalasemia
-
?
H2O2
O2 + H2O
show the reaction diagram
-
involved in acatalasemia
-
?
H2O2
O2 + H2O
show the reaction diagram
-
regulator of H2O2-levels or protective function for hemoglobin or other SH-proteins
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification and protection enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q6LA34
detoxification enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification enzyme, enzyme is naturally adapted to the cold climate of the arctic tundra
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
detoxification enzyme, enzyme protects the cell against high concentrations of peroxide
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
enzyme is responsible for prevention of dehydration-related oxidative damage during seed desiccation, H2O2 may play a role for enzyme expression regulation and in the transduction pathway
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
enzyme is responsible for the protection of the Helicobacter pylori cells against phagocyte attack in the gastric mucosa by disumtation of H2O2
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q8X220
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
H2O2 decomposition is accompanied by enzyme inactivation which can be minimized in vitro by immobilization of the enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q8L2Z7
protective role of the enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
essential for optimal resistance to H2O2. KatB was not produced during the normal growth cycle. Catalase activity is greater in nonmucoid than in mucoid, alginate-producing organisms. When exposed to hydrogen peroxide and, to a greater extent, paraquat, total catalase activity was elevated 7fold to 16fold, respectively
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Bacillus firmus OF4
-
two monofunctional, one bifunctional catalase-peroxidase
-
?
H2O2
O2 + H2O
show the reaction diagram
Penicillium cyclopium 1
-
detoxification enzyme, enzyme is naturally adapted to the cold climate of the arctic tundra
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Kloeckera sp. 2201
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Listeria monocytogenes F2365
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
enzyme is responsible for the protection of the Helicobacter pylori cells against phagocyte attack in the gastric mucosa by disumtation of H2O2
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Klebsiella pneumoniae IFO 14940
-
detoxification enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Helicobacter pylori Taiwanese TW-34
-
detoxification and protection enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
Q8X220
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Talaromyces piceae F-648
-
H2O2 decomposition is accompanied by enzyme inactivation which can be minimized in vitro by immobilization of the enzyme
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Pyrobaculum calidifontis VA1
Q6LA34
detoxification enzyme
-
-
?
additional information
?
-
-
regulation of enzyme expression and activity by drying occurs on transcriptional level, increase in enzyme activity during drying is associated with an decrease of H2O2 level and lipid peroxidation
-
-
-
additional information
?
-
-
the enzyme has negligible inhibitory effects on endothelium-dependent relaxations in mouse isolated aorta and small mesenteric artery which are not caused by H2O2, endothelium-independent relaxations are caused by H2O2 and are abolished by the enzyme, overview
-
-
-
additional information
?
-
-
peroxidase and catalase activities are involved in direct adventitious shoot formation induced by thidiazuron in zygotic embryos
-
-
-
additional information
?
-
-
CcmC is a key determinant for cytochrome c biogenesis, pyoverdine maturation, and expression of some quorum sensing-regulated traits
-
-
-
additional information
?
-
-
the enzyme is involved in protection against peroxides and oxidative DNA damage, it is downregulated in biofilm cultures of Pseudomonas aeruginosa, that display up to a 105fold increase in mutability compared with planktonic cultures
-
-
-
additional information
?
-
-
adenine deaminase, EC 3.5.4.2, from the amidohydrolase superfamily of enzymes catalyzes the conversion of adenine to hypoxanthine and ammonia. But it also catalyzes the catalase reaction converting H2O2 to H2O and O2. [MnII/MnII]-ADEec is active as a deaminase but not as a catalase. In contrast, [FeII/FeII]-ADEec catalyzes both reactions
-
-
-
additional information
?
-
P08303
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
-
additional information
?
-
-
the bifunctional catalase with phenol oxidase activity catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds
-
-
-
additional information
?
-
Paracoccus denitrificans AO1
P08303
bifunctional aa3 cytochrome c oxidase, CcO, possesses a peroxidase and a catalase activity
-
-
-
additional information
?
-
Scytalidium thermophilum ATCC 16454
-
the bifunctional catalase with phenol oxidase activity catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
Q8X182
all isoforms have chlorine instead of ferro-protoheme IX at the active site; all isoforms have chlorine instead of ferro-protoheme IX at the active site
heme
Beta vulgaris var. cicla
-
-
heme
-
ferro-hemoprotein
heme
-
three molecules protoheme IX per tetramer
heme
O93662
ferro-hemoprotein
heme
-
protoheme IX
heme
-
the monofunctional catalase contains a chlorine-type heme, the catalase-peroxidase has protoheme IX
heme
-
0.78 protoheme per tetramer
heme
-
isoenzymes I and II contain protoheme, isoenzyme II contains chlorine-type heme
heme
-
1.43 hemes per tetramer
heme
-
1-1.2 protoheme IX per tetramer
heme
-
one molecule heme per subunit
heme
-
one molecule heme per subunit; protoheme IX
heme
-
2.07 molecules protoheme IX per tetramer
heme
-
ferric heme
heme
-
ferric chlorine
heme
Capra capra
-
-
heme
-
heme d
heme
-
heme d
heme
-
dependent on, contains 1 protoheme IX group per KatA 54 kDa polypeptide
heme
P42321
-
heme
-
substrate isonicotinic hydrazide binds with high affinity to a small protion of ferric enzyme in a six-coordinate heme iron form, binding is associated with a large enthalpie loss. Binding parameters do not depend on pH in the range of pH 5-8
heme
A5XB38
deduced from sequence
heme
-
in wild-type, primarily high-spin. In mutant Y111A, substantial increase in hexa-coordinate low-spin heme
heme
-
the active site of the enzyme contains heme
heme
-
contains 1 heme per homodimer
heme
Q9C168
CAT-1 tetramer includes 3450 water molecules and four heme groups
heme
-
-
heme
D7RJ66
-
heme
-
Cat is a heme b-containing protein
heme
-
EsCAT contains a proximal heme-ligand signature motif, 350RLFSYNDTH358. Each monomer contains a single heme
heme
B3FXQ9
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
heme
A3REN3
-
NADPH
A5XB38
deduced from sequence
NADPH
-
Each monomer contains a NADPH bound on the surface of each monomer by 12 amino acid residues and protects the enzyme from oxidation by its substrate, H2O2
heme c
-
8 molecules per teramer
additional information
-
no protoheme IX
-
additional information
-
the heme component is cis-hydroxychlorin gamma-spirolactone
-
additional information
B3FXQ9
the enzyme contains a NADPH-binding site with His184, Arg193, Val292 and Lys295
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
-
less than 0.2 g-atom cupper per mol enzyme
Fe2+
-
enzyme contains heme
Fe2+
-
TvC-II, heme-containing
Fe2+
-
heme-containing enzyme
Fe2+
-
contains 1 atom Fe2+ per homodimer
Fe2+
-
enzyme-bound, [FeII/FeII]-enzyme, required for activity. Disproportionation of H2O2 by the iron-bound enzyme involves the cycling of the binuclear metal center between the di-ferric and di-ferrous oxidation states
Fe3+
-
the active site of the enzyme contains Fe3+
Iron
-
1 mol iron per subunit
Iron
-
3.4 g-atom iron per mol enzyme
Iron
-
presence of a ferric component
K+
-
stimulatory effect at 2 mM
Mg2+
-
stimulatory effect at 2 mM
Mn2+
-
required for catalase activity
Mn2+
Q6LA34
activates at 0.001 mM in vivo, 1.32 atoms bound per subunit
Na+
-
stimulatory effect at 2 mM
NaCl
-
there is a stimulation of catalase by addition of NaCl 10 mM (176%)
Mn2+
-
stimulatory effect at 2 mM
additional information
-
effects of mineral sorbents on enzyme activity, binding capacities, overview
additional information
Q6LA34
enzyme contains no heme and no Fe2+
additional information
-
no acatalase acivit with Zn2+ or Mn2+-substituted enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+)-catechin
-
-
(-)-epigallocatechin
-
-
1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one
-
-
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
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
2-mercaptoethanol
Beta vulgaris var. cicla
-
50% inhibition at 3 mM
2-mercaptoethanol
-
36% inhibition at 1 mM
2-mercaptoethanol
Capra capra
-
complete inhibition at 23 mM, summation effect with p-chloromercuribenzoate
2-mercaptoethanol
-
slight inhibition for all three isoforms at 10 mM
2-mercaptoethanol
Capra capra
-
complete inactivation
2-mercaptoethanol
-
rapid inactivation
2-mercaptoethanol
-
-
3-Amino-1,2,4-triazole
-
strong inhibition
3-Amino-1,2,4-triazole
Q8L2Z7
strong inhibition
3-Amino-1,2,4-triazole
-
TvC-I and TvC-II, inactivation
3-Amino-1,2,4-triazole
-
10 mM, 81% inhibition
3-Amino-1,2,4-triazole
-
inhibitory. Inhibition of extracellular catalase activity leads to a striking inactivation of secreted cysteine cathepsins
3-Amino-1,2,4-triazole
-
10 mM, 26% residual activity
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
Q5LLG6
500 microM reduces the reactivity of catalase to 50%
3-Amino-1,2,4-triazole
-
potent catalase inhibitor, maximum inhibition at 10 mM
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
-
3-Amino-1,2,4-triazole
-
3-amino-1,2,4-triazole at concentrations of 10 mM has no inhibition on the activity
3-Amino-1,2,4-triazole
-
very weak inhibitor of erythrocytic CAT activity
3-Amino-1,2,4-triazole
Q8X220
specific irreversible inhibitor, complete inhibition at 20 mM
3-amino-1H-1,2,4-triazole
-
-
3-amino-1H-1,2,4-triazole
Q8X182
50% inactivation in 1 h
3-amino-1H-1,2,4-triazole
-
retains 38% of its initial activity in the presence of 40 mM
3-amino-1H-1,2,4-triazole
-
56% inactivation at 20 mM
3-amino-1H-1,2,4-triazole
O93662
IC50: 80 mM
3-amino-1H-1,2,4-triazole
-
no effect on catalase-peroxidase enzyme
3-amino-1H-1,2,4-triazole
-
33% inactivation at 20 mM in 2.5 h
3-amino-1H-1,2,4-triazole
-
98% inhibition at 10 mM
3-amino-1H-1,2,4-triazole
-
not inhibitory
3-amino-1H-1,2,4-triazole
-
not inhibitory
3-amino-1H-1,2,4-triazole
-
59% inhibition at 20 mM
3-amino-1H-1,2,4-triazole
-
not inhibitory
3-amino-1H-1,2,4-triazole
-
90% inhibition at 20 mM
3-amino-1H-1,2,4-triazole
-
isoenzyme HPI: 25% inhibition at 10 mM, isoenzyme HPII: 70-80% inhibition at 10 mM
3-amino-1H-1,2,4-triazole
-
exclusive in vivo inhibitor
3-amino-1H-1,2,4-triazole
-
strong inhibition for isoforms Cat-1, Cat-2, 32% inhibition for isoform Cat-3 at 10 mM
3-amino-1H-1,2,4-triazole
-
reaction occurs only in vivo, irreversible inhibition
4-aminoantipyrine
-
inhibition of catalase activity
5,5-dithiobis(2-nitrobenzoic acid)
Capra capra
-
complete inhibition at 0.4 mM
6-Chloropurine
-
-
acetic acid
-
in vitro inhibitor
apigenin
-
-
ascorbate
-
in vitro inhibitor
Astragalin
-
-
azide
-
-
azide
-
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
-
very strong inhibitor of erythrocytic CAT but a relatively weak CAT inhibitor in human hemolysates
azide
Q8X220
irreversible inhibitor, effective at concentrations less than1 mM
Ba2+
-
partial inhibition at 2 mM
beta-mercaptoethanol
-
-
BO3-
Capra capra
-
weak inhibition at 1 mM
-
BrCN
-
acting in vitro
BrCN
-
selective modification of the active site, only in vitro
CaCl2
-
irreversible loss of activity at 2 M
CAS 1609
-
-
catechol
-
-
Cd2+
-
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
Cd2+
-
Cd2+ has a small role in the reduction of CAT activity
CN-
-
strong inhibition
CN-
-
TvC-I and TvC-II, at micromolar range
Co2+
-
partial inhibition at 2 mM
Cu2+
Beta vulgaris var. cicla
-
47% inhibition at 0.2 mM
Cu2+
Capra capra
-
55% inhibition at 0.2 mM
Cu2+
-
-
cyanide
-
most potent inhibitor of root nodule catalase
cyanide
-
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
dinitrosyl iron complex
-
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
dithiothreitol
Beta vulgaris var. cicla
-
50% inhibition at 10 mM
dithiothreitol
Capra capra
-
complete inhibition at 33 mM
dithiothreitol
-
slight inhibition at 10 mM for all three isoforms
dithiothreitol
Capra capra
-
complete inactivation
dithiothreitol
-
slight inactivation
dithiothreitol
-
the activity can be inhibited by 75% by addition of 5 mM dithiothreitol
EDTA
-
10 mM EDTA reduces activity by 27%
EDTA
-
-
eicosapentaenoic acid
-
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
-
purified on catalase-Sepharose from bovine, different inhibition sensitivities for three isoforms
-
Epicatechin gallate
-
-
epigallocatechin gallate
-
-
ethanol
-
in vitro inhibitor
ethanol-1,2-diol
-
activity at 30-60C in presence of ethanol-1,2-diol, overview
-
F-
-
in vitro inhibitor
Fe2+
Beta vulgaris var. cicla
-
14% inhibition at 1.5 mM
Fe2+
-
-
formaldehyde
Capra capra
-
non-competitive inhibition
formic acid
-
in vitro inhibitor
galangin
-
-
gallic acid
-
-
gamma-linolenic acid
-
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
Glutaraldehyde
Beta vulgaris var. cicla
-
24% inactivation at 8%
Glutaraldehyde
-
the presence of trace amount of glutaraldehyde in immobilization medium causes the catalase activity to decline
glycerol trinitrate
-
-
H2O2
Beta vulgaris var. cicla
-
55% inactivation at 10 mM in 60 min
H2O2
-
50% inhibition for catalase at 4.5 mM, for peroxidase at 0.4 mM
H2O2
Kloeckera sp.
-
inhibition above 50 mM
H2O2
-
inactivation half-life: 20-30 min at 2 mM
H2O2
-
rapid inactivation above 0.1 M
H2O2
Q0D9C4
substrate inhibition, no detectable activity above 60 mM H2O2
H2O2
-
catalase activity at pH 4.5 is inhibited by 5 mM H2O2 and above
H2O2
-
H2O2 causes 17% inhibition at 80 mM
H2O2
-
inactivation at temperatures above 40C, overview
H2O2
-
excess H2O2 inhibits the enzyme. In the presence of excess H2O2, [FeII/FeII]-ADEec rapidly loses its ability to deaminate adenine
histidine
-
10 mM histidine reduces activity by 19%
hydroxyl radicals
Q8X182
inactivation of isoform Cat-1
hydroxylamine
-
85.1% inactivation at 0.005 mM
hydroxylamine
-
50% inhibition for catalase at 0.002 mM, for peroxidase at 0.078 mM
hydroxylamine
-
in vitro inhibitor
hydroxylamine
-
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
-
0.00011 mM, 50% inhibition
hydroxylamine
-
-
hydroxylamine
-
-
hydroxylamine
Q8X220
-
Hydroxylamine hydrochloride
-
strong inhibition
indole acetic acid
Capra capra
-
non-competitive inhibition
inositol phosphoglycan-like compound from Bos taurus thyroid gland
-
produced by the hydrolysis of the membrane-bound glycosyl phosphoinositides, noncompetitive inhibition. 50% residual activity, the site of action is not the prosthetic group
-
inositol phosphoglycan-like compound from Escherichia coli
-
produced by the hydrolysis of the membrane-bound glycosyl phosphoinositides, noncompetitive inhibition. 50% residual activity, the site of action is not the prosthetic group
-
iodoacetamide
Beta vulgaris var. cicla
-
50% inhibition at 2 mM
iodoacetamide
Capra capra
-
complete inhibition at 11.7 mM
isosorbide dinitrate
-
-
kaempferol
-
-
KCN
Q8X182
isoform Cat-2, IC50: 0.146 mM, catalase activity, IC50: 0.168 mM, peroxidase activity
KCN
Q9C4N4
50% inhibition at 0.08 mM
KCN
Beta vulgaris var. cicla
-
50% inhibition at 0.65 mM
KCN
-
73% inactivation at 0.01 mM
KCN
O93662
IC50: 0.005 mM
KCN
-
72.5% inactivation at 0.005 mM
KCN
-
effective inhibition
KCN
-
50% inhibition of both catalase and peroxidase activities at 0.02 mM
KCN
-
acting in vitro
KCN
-
strong inhibition for all three isoforms at 1 mM
KCN
-
97% inhibition at 1 mM
KCN
-
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
-
inhibitory. Inhibition of extracellular catalase activity leads to a striking inactivation of secreted cysteine cathepsins
KNO2
-
37% inhibition at 1 mM
KNO3
-
14% inhibition at 1 mM
L-aspartic acid
Beta vulgaris var. cicla
-
92% inhibition at 30 mM
L-aspartic acid
Capra capra
-
25% inhibition at 16 mM
L-cysteine
Capra capra
-
35% inhibition at 3.3 mM
L-Glutamic acid
Beta vulgaris var. cicla
-
84% inhibition at 30 mM
L-lactic acid
Capra capra
-
63% inhibition at 25 mM
L-Malic acid
Capra capra
-
50% inhibition at 6 mM
L-tryptophan
Capra capra
-
80% inhibition at 1.6 mM
L-tyrosine
Capra capra
-
80% inhibition at 5 mM
linoleic acid
-
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
luteolin
-
-
Maleic acid
Capra capra
-
51% inhibition at 0.8 mM
methanol
-
in vitro inhibitor
MgCl2
-
irreversible loss of activity at 2 M
Mn2+
Beta vulgaris var. cicla
-
56% inhibition at 1 mM
myricetin
-
-
N-bromosuccinimide
Capra capra
-
complete inhibition at 3.34 mM
N-ethylmaleimide
Capra capra
-
complete inhibition at 18.3 mM
NaCl
-
50 mM, 17% residual activity in leaf, 54% residual activity in nodule
NaCl
-
50 mM, 30% residual activity in leaf, 24% residual activity in nodule
NaCN
-
50% inhibition at 300 mM
NaCN
-
50% inhibition at 60 mM
NaCN
-
50% inhibition at 35 mM
NaCN
-
50% inhibition at 30 mM
NaCN
-
50% inhibition at 15 mM
NaCN
-
50% inhibition at 9 mM
NaCN
-
50% inhibition at 150 mM
NaCN
-
50% inhibition at 20 mM
NaCN
-
50% inhibition at 25 mM
NaCN
-
50% inhibition at 60 mM
NaCN
-
50% inhibition at 80 mM
NaCN
-
50% inhibition at 12 mM
NaCN
-
50% inhibition at 35 mM
NaCN
-
50% inhibition at 80 mM
NaCN
-
50% inhibition at 15 mM
NaN3
Q9C4N4
50% inhibition at 0.001 mM
NaN3
Beta vulgaris var. cicla
-
50% inhibition at 0.0018 mM
NaN3
-
97% inactivation at 0.1 mM
NaN3
O93662
IC50: 0.001 mM
NaN3
-
76.4% inactivation at 0.005 mM
NaN3
-
complete inhibition at 0.01 mM
NaN3
Capra capra
-
non-competitive inhibition
NaN3
-
effective inhibition
NaN3
-
50% inhibition for catalase at 0.15 mM, for peroxidase at 0.73 mM
NaN3
-
acting in vitro
NaN3
-
strong inhibition for all three isoforms at 0.001 mM
NaN3
-
98% inhibition at 1 mM
NaN3
Q8L2Z7
strong inhibition
NaN3
-
TvC-I and TvC-II, at micromolar range
NaN3
-
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
-
-
nitrite
-
in vitro inhibitor
nitrite
-
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
-
uncompetitive inhibitor
NO
P00432
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
-
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
oxalic acid
Capra capra
-
51% inhibition at 4 mM
p-chloromercuribenzoate
Capra capra
-
complete inhibition at 0.33 mM, summation effect with 2-mercaptoethanol
palmitic acid
-
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
pentaerythritol tetranitrate
-
-
Phenol
-
inhibition of catalase activity
pyocyanin
-
may decrease cellular catalase activity via both transcriptional regulation and direct inactivation of the enzyme
pyrogallol
-
-
Pyruvic acid
Capra capra
-
16% inhibition at 5 mM
quercetin
-
-
rutin
-
-
S-nitrosocysteine
-
-
S-nitrosoglutathione
-
-
S-nitrosoglutathione
-
-
SDS
Beta vulgaris var. cicla
-
55% inhibition at 0.01%
SO3-
Capra capra
-
weak inhibition at 4 mM
Sodium azide
Q6LA34
only 10% inhibition at 1 mM
Sodium azide
-
0.00052 mM, 50% inhibition
Sodium azide
-
strong inhibition
Sodium azide
-
-
Sodium cyanide
-
0.0115 mM, 50% inhibition
Sodium cyanide
-
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
Sodium dithionite
-
inhibitory
sodium nitroprusside
-
-
stearic acid
-
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
Urea
Beta vulgaris var. cicla
-
50% inhibition at 4 M in 3.5 min
Mn2+
Capra capra
-
30% inhibition at 1 mM
additional information
-
no inhibition by H2O2 up to 450 mM
-
additional information
-
no reduction of TvC-II by dithionite
-
additional information
Q6LA34
no effect by 0.01 mM hydrogen peroxide or 100 nM paraquat
-
additional information
Q0D9C4
exposure to white light of nearly 0.800 mE per square meter and second for 120 min at 25C inactivates the wild-type enzyme activity by about 50%
-
additional information
Q4F6N6
not inhibited by exposure of cells to 3-amino-1,2,4-triazole
-
additional information
A8CFD3
enzyme is not inhibited by presence of 5 mM sodium azide
-
additional information
-
telomerase deficiency reduces catalase activity
-
additional information
-
tissue necrosis factor-alpha treatment causes downregulation of catalase expression in MCF-7, Caco-2 and Hct-116 cancer cell lines
-
additional information
-
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
-
additional information
-
acetazolamide and nitrate at concentrations up to 0.1 mM do not inhibit erythrocytic CAT activity
-
additional information
-
enzyme inhibition by flavonoids, structure-function relationship, overview
-
additional information
-
Ni2+, Ca2+, Mg2+ and Mn2+ have both enhancing and inhibitory effects
-
additional information
-
oxygenation of active site residues, inhibiting catalase activity, occurs via release of hydroxyl radicals
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
18% activation of catalase activity and unaltered peroxidase activity at 0.1 mM, 56% activation of catalase activity and 21% activation of peroxidase activity at 10 mM
all-trans-retinol
-
treatment of cultured Sertoli cells leads to activation of catalase by increasing its protein content, but without alteration of its mRNA expression. Retinol treatment also increases cell lipoperoxidation and intracellular reactive species production. All effects induced by retinol are inhibited by the antioxidant Trolox
AnkB
-
the periplasmic ankyrin-like protein is required for optimal catalase B (KatB) activity and resistance to hydrogen peroxide
-
bensulfuron methyl
-
-
bensulfuron methyl
-
the catalase activity is higher with bensulfuron-methyl than with quinclorac
Ca2+
-
stimulates
Chloramphenicol
-
24% activation at 0.1 mM in 1 min
Fe2+
-
the catalase activity shows a strong positive dependence on the intracellular iron concentration in Fe-replete medium and low activity under Fe-limited growth conditions
Hemin
-
0.002-0.01 mM required for half-maximal to maximal enzyme production
histidine
-
stimulation
Ibuprofen
-
induces a variety of enzymes associated with the oxidative stress response, including catalase, glucose-6-phosphate-dehydrogenase, and aldehyde reductase in a dose-related manner
imidazole
-
up to 20 mM: enhancement of Vmax
imidazole
-
2fold activation at 10 mM
Leucine-enkephalin
-
the intracellular and extracellular CAT activity is increased with increasing concentration (0.001-0.05 mg/ml) of leucine-enkephalin
Mg2+
-
stimulates
NaCl
-
highest activity for catalase at 2 M, for peroxidase at 1 M
NADPH
Q8X220
addition of NADPH stimulates the activity of CatP in a dose-dependent manner most likely by preventing the inactivation from oxidative damage through its substrate H2O2
Ni2+
-
stimulates
peracetic acid
-
low doses induce enzyme promoter activity and increase total enzymic activity in cell extracts
phosphatidylcholine
P08303
-
progesterone receptor isoform B
-
-
-
retinal
-
retinal (0.007 and 0.014 mM) increases CAT activity after 24 h of treatment
retinoic acid
-
retinoic acid (100 nM and 0.001 mM) increases CAT activity after 24 h of treatment
Sodium arsenate
-
CAT activity is activated by 200 mM arsenate up to 120% compared to the control
Sodium arsenate
-
CAT activity is activated by 200 mM arsenate up to 133% compared to the control
Sodium arsenate
-
CAT activity is activated by 200 mM arsenate up to 300% compared to the control
Tris
-
stimulation at 10 mM
Mn2+
-
stimulates
additional information
-
the periplasmic enzyme is dependent on the twin-arginine target protein KapA for activity
-
additional information
-
increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
-
additional information
Q6LA34
no effect by 0.01 mM hydrogen peroxide or 100 nM paraquat, 3.4fold increase in intracellular activity by elimination of thiosulfate from the aerobic growth medium
-
additional information
-
stimulation of the enzyme by natural and artificial drying
-
additional information
-
strong induction of both catalase and bifunctional catalase-peroxidase by raising the intracelllar H2O2 level with paraquat, but not by exogenous H2O2
-
additional information
Q8X220
H2O2 induces enzyme expression
-
additional information
-
addition of non-toxic concentrations of H2O2 to cultured THP-1 cells neither influences catalase activity nor mRNA expression levels and activity of cathepsins
-
additional information
A9LSF7, A9QNB5, A9QNB6
in planta, activity increases dramatically about 8 h after infection of host tobacco plants; in planta, activity increases dramatically about 8 h after infection of host tobacco plants; in planta, activity increases dramatically about 8 h after infection of host tobacco plants
-
additional information
Q6RSH8
the activity of CatA increases when the fungus is grown under endogenous oxidative stress, i.e. in oleic acid. CatP and PbCatC demonstrat no alteration in activity under these conditions
-
additional information
-
3alpha-hydroxy tibolone has no activating effect
-
additional information
P04762
daidzein shows a significant induction of catalase promoter activity at 0.1 mM in a reporter gene assay and at 0.2 mM in Northern blot experiments
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
H2O2
-
-
0.0847
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0)
0.0867
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0)
0.14
H2O2
-
peroxidase activity
0.64
H2O2
-
second isoform, 25C, pH 6.5
0.64
H2O2
-
isoenzyme with optimum at pH 6.5
0.67
H2O2
-
catalase activity, pH 8.5, 30C
1
H2O2
-
first isoform, 25C, pH 4.5
1
H2O2
-
isoenzyme with optimum at pH 4.5
1.47
H2O2
-
peroxidase activity, pH 4.5, 30C
2
H2O2
-
isoenzyme I
3
H2O2
-
peroxidase activity, pH 7.0, 25C
3.5
H2O2
-
wild-type, pH 7.0, 23C
3.7
H2O2
-
catalase activity
3.7
H2O2
-
isoenzyme HPI
3.9
H2O2
-
-
4
H2O2
Q0D9C4
mutant L189W/H225T
5.16
H2O2
-
pH 6.0, 25C
5.2
H2O2
-
mutant Y111A, pH 7.0, 23C
6.3
H2O2
-
catalase activity, pH 7.0, 30C
10
H2O2
-
isoenzyme HPII, pH 10.5
11
H2O2
Q0D9C4
wild-type
13
H2O2
Q8X182
isoform Cat-2
13.4
H2O2
-
third isoform, 25C, pH 10.0
13.4
H2O2
-
isoenzyme with optimum at pH 10.0
13.74
H2O2
-
recombinant wild-type enzyme, pH 7.0, 25C
16.2
H2O2
-
pH 7.0, 40C
17.2
H2O2
Q5LLG6
-
18.2
H2O2
-
isoenzyme HPII, pH 6.8
19.2
H2O2
-
-
21.8
H2O2
-
pH 7.0, 25C
24
H2O2
-
in 20 mM Tris-HCl buffer (pH 9.0), at 30C
25
H2O2
Kloeckera sp.
-
catalase activity
27
H2O2
-
catalase activity, pH 7.0, 25C
27.73
H2O2
-
pH 7.0, 25C, free enzyme
28.6
H2O2
-
free catalase, in 50 mM phosphate buffer pH 7.0, at 25C
30.4
H2O2
-
25C, pH 7.2
31.42
H2O2
-
pH 7.0, 25C, immobilized enzyme
33.3
H2O2
-
free enzyme
35.5
H2O2
-
pH 8.0, 70C
36
H2O2
-
isoenzyme II
41.5
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0), at 4C
42
H2O2
-
wild-type
43.6
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0), at 25C
50
H2O2
Beta vulgaris var. cicla
-
-
52.5
H2O2
Q9AQQ9
-
61
H2O2
-
pH and temperature not specified in the publication
64
H2O2
-
-
65.8
H2O2
-
mutant S2W
70
H2O2
Capra capra
-
-
75
H2O2
Q8L2Z7
pH 7.0, 37C
75
H2O2
B3FXQ9
pH 7.0, 25C
78
H2O2
D7RJ66
in 50 mM NaH2PO4-Na2HPO4 buffer (pH 7.0) at 20C
80
H2O2
-
-
93
H2O2
-
-
95.9
H2O2
-
catalase covalently immobilized onto Eupergit C, in 50 mM phosphate buffer pH 7.0, at 25C
100
H2O2
A3REN3
pH 7.0, 25C
111
H2O2
-
-
152
H2O2
-
-
158.8
H2O2
-
catalase from Penicillium piceum strain F-648
170
H2O2
Q6LA34
pH 7.0, 25C
174
H2O2
-
-
465
H2O2
-
-
537
H2O2
-
-
1722
H2O2
-
enzyme immobilized on florisil
0.048
o-Dianisidine
-
peroxidase activity, pH 4.5, 30C
83
methanol
Kloeckera sp.
-
peroxidase activity
additional information
additional information
-
stopped-flow kinetics, 25C, pH 7.0
-
additional information
additional information
P08303
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetic modeling, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11
H2O2
-
presence of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 6.0
20
H2O2
-
presence of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 5.5
24
H2O2
-
presence of o-dianisidine, pH 4.0
27
H2O2
-
presence of pyrogallol, pH 4.0
37
H2O2
-
presence of o-dianisidine, pH 4.5
44
H2O2
-
presence of pyrogallol, pH 4.5
55
H2O2
-
presence of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 5.0
56
H2O2
-
presence of pyrogallol, pH 5.0
58
H2O2
-
presence of o-dianisidine, pH 5.0
64
H2O2
-
presence of pyrogallol, pH 5.5
69
H2O2
-
presence of o-dianisidine, pH 5.5; presence of pyrogallol, pH 6.0
71
H2O2
-
presence of o-dianisidine, pH 6.0
92
H2O2
-
presence of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 4.5
151
H2O2
-
presence of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 4.0
200
H2O2
-
pH 7.5, 30C
2140
H2O2
-
mutant Y111A, pH 7.0, 23C
3000
H2O2
-
pH 6.0, 25C
11000
H2O2
-
wild-type, pH 7.0, 23C
16300
H2O2
-
-
18000
H2O2
-
catalase activity, pH 7.0, 22C
26000
H2O2
-
peroxidase activity, pH 7.0, 22C
29000
H2O2
Q6LA34
pH 7.0, 25C, per subunit
62800
H2O2
-
pH and temperature not specified in the publication
80000
H2O2
A3REN3
pH 7.0, 25C
125000
H2O2
Q8X182
isoform Cat-2
149000
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0), at 4C
175000
H2O2
-
in 50 mM potassium phosphate buffer (pH 7.0), at 25C
217000
H2O2
Capra capra
-
-
255000
H2O2
Q8L2Z7
pH 7.0, 37C
360000
H2O2
-
pH 8.0, 70C
850000
H2O2
-
-
2830000
H2O2
-
catalase from Penicillium piceum strain F-648 at the minimum degree of association (0.3 nM)
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24
H2O2
-
pH 7.5, 30C
22
160
H2O2
-
catalase covalently immobilized onto Eupergit C, in 50 mM phosphate buffer pH 7.0, at 25C
22
21000
H2O2
-
free catalase, in 50 mM phosphate buffer pH 7.0, at 25C
22
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
3-Amino-1,2,4-triazole
Q8L2Z7
pH 7.0, 37C
0.053
4-aminoantipyrine
-
catalase activity, pH 8.5, 30C
0.55
formaldehyde
Capra capra
-
non-competitive inhibition
1.6
indole acetic acid
Capra capra
-
non-competitive inhibition
6.7
L-cysteine
Capra capra
-
non-competitive inhibition
0.001
NaN3
Q8L2Z7
pH 7.0, 37C
0.0017
NaN3
Capra capra
-
non-competitive inhibition
0.14
Phenol
-
catalase activity, pH 8.5, 30C
1.5
L-tryptophan
Capra capra
-
non-competitive inhibition
additional information
additional information
-
estimated kinetic parameters for catalase inactivation in various media, kinetic model of inactivation, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00122
(+)-catechin
-
pH 7.0, 23C
0.049
(-)-epigallocatechin
-
pH 7.0, 23C
20
3-Amino-1,2,4-triazole
-
erythrocytic CAT, at 25C, pH not specified in the publication
80
3-amino-1H-1,2,4-triazole
O93662
IC50: 80 mM
0.0166
apigenin
-
pH 7.0, 23C
0.033
Astragalin
-
pH 7.0, 23C
0.0000002
azide
-
erytrocyctic CAT, at 25C, pH not specified in the publication
0.0004
azide
-
pH 7.0, 25C
0.0015
azide
Q8X220
in 50 mM sodium phosphate buffer, pH 7.8, at 37C
0.0017
azide
-
-
0.009
azide
-
hemolysate CAT, at 25C, pH not specified in the publication
0.01
azide
-
first isoform, 25C, pH 4.5
0.01
azide
-
isoenzyme with optimum at pH 4.5
0.075
azide
-
second isoform, 25C, pH 6.5
0.075
azide
-
isoenzyme with optimum at pH 6.5
1
azide
-
third isoform, 25C, pH 10.0
1
azide
-
isoenzyme with optimum at pH 10.0
2
beta-mercaptoethanol
-
-
0.056
catechol
-
pH 7.0, 23C
0.0088
cyanide
-
pH 7.0, 25C
0.2
cyanide
-
second isoform, 25C, pH 6.5
0.2
cyanide
-
isoenzyme with optimum at pH 6.5
2
cyanide
-
third isoform, 25C, pH 10.0
2
cyanide
-
isoenzyme with optimum at pH 10.0
12
cyanide
-
first isoform, 25C, pH 4.5
12
cyanide
-
isoenzyme with optimum at pH 4.5
0.000029
Epicatechin gallate
-
pH 7.0, 23C
0.00033
epigallocatechin gallate
-
pH 7.0, 23C
0.02
galangin
-
pH 7.0, 23C
0.046
gallic acid
-
pH 7.0, 23C
0.0003
hydroxylamine
-
-
0.002
hydroxylamine
Q8X220
in 50 mM sodium phosphate buffer, pH 7.8, at 37C
0.0044
hydroxylamine
-
pH 7.0, 25C
0.0744
kaempferol
-
pH 7.0, 23C
0.005
KCN
O93662
IC50: 0.005 mM
0.168
KCN
Q8X182
isoform Cat-2, IC50: 0.146 mM, catalase activity, IC50: 0.168 mM, peroxidase activity
0.0116
luteolin
-
pH 7.0, 23C
0.000014
myricetin
-
pH 7.0, 23C
0.001
NaN3
O93662
IC50: 0.001 mM
0.009
nitrite
-
erythrocytic CAT, at 25C, pH not specified in the publication
0.75
nitrite
-
hemolysate CAT, at 25C, pH not specified in the publication
0.0018
pyrogallol
-
pH 7.0, 23C
0.045
quercetin
-
pH 7.0, 23C
0.036
rutin
-
pH 7.0, 23C
0.345
Sodium azide
-
pH 7.0, 23C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.004
-
peroxidase activity after 5 days of cell culture
0.016
-
peroxidase activity after 10 days of cell culture
0.086
-
peroxidase activity after 5 days of cell culture in presence of 0.1 mM paraquat
0.164
-
peroxidase activity after 10 days of cell culture in presence of 0.1 mM paraquat
0.94
-
purified enzyme, peroxidase activity, mixed-type
1.5
-
about, cell lysates of wild-type Caco-2 cells
3.5 - 4.5
-
about, cell lysates of wild-type Y-1 cells
4
-
mutant H82N, pH 7.0, 60C
6
-
about, cell lysates of Caco-2 cells recombinantly overexpressing IGFBP-2
8
-
about, cell lysates of Y-1 cells recombinantly overexpressing IGFBP-2
8.76
-
catalase activity after 5 days of cell culture
15.2
-
peroxidatic activity
43.2
-
catalase activity
65
-
mutant V123F, pH 7.0, 60C
74.14
-
catalase activity after 10 days of cell culture
77.5
-
about, cell lysates of wild-type and recombinantly IGFBP-2-overexpressing 293 cells
82
-
purified recombinant His-tagged enzyme expressed in Bacillus subtilis
104.3
-
peroxidase activity
117
-
partially purified TvC-I
130
Q8X182
isoform Cat-2, peroxidase activity with 3,3-diaminobenzidine
139
-
catalase activity after 5 days of cell culture in presence of 0.1 mM paraquat
234.8
-
catalase activity after 10 days of cell culture in presence of 0.1 mM paraquat
316
-
crude extract, at 30C
366.6
Q8X220
crude extract, in 50 mM sodium phosphate buffer, pH 7.8, at 37C
444.4
-
60C, pH 7.0
470
Q8X182
isoform Cat-2, peroxidase activity with ascorbate
955
Q8L2Z7
recombinant enzyme
1017
-
-
1134
Q8X220
after 3.1fold purification, in 50 mM sodium phosphate buffer, pH 7.8, at 37C
1145
-
purified enzyme, catalase activity
1300
Q8X182
isoform Cat-2, peroxidase activity with guaiacol
1486
-
catalatic activity
1600
Q8X182
isoform Cat-2, peroxidase activity with o-dianisidine
3667
A8CFD3
25C, pH 8.0
4000
-
isoenzyme I
5320
-
purified enzyme
6400
L8B3D7
purified enzyme, pH 6,5, 37C
8000
-
isoenzyme II
8870
-
native wild-type enzyme, pH 7.0, 60C
14490
D7RJ66
crude extract, pH 7.0, at 20C
18710
-
recombinant wild-type enzyme, pH 7.0, 60C
19700
B3FXQ9
native enzyme, cell extract, pH 7.0, 25C
23500
Q6LA34
91fold purified enzyme, at 70C
25700
-
purified native enzyme, pH 7.0, 40C
30000
A5XB38
37C, pH 5.0
34600
Q9AQQ9
-
35000
-
after 110.7fold purification, at 30C
38330
Capra capra
-
-
39960
-
pH 7.0, 25C
53400
P04040
-
55000
-
purified enzyme, catalase activity, mixed-type
55000
-
purified TvC-II
56950
Beta vulgaris var. cicla
-
-
75000
-
isoenzyme II
91800
-
-
120000
Q9C4N4
half-maximal activity at 30 mM H2O2
121000
-
-
199600
D7RJ66
after 13.8fold purification, pH 7.0, at 20C
222000
B3FXQ9
purified native enzyme, pH 7.0, 25C
273800
-
-
282000
Kloeckera sp.
-
-
500000
-
purified enzyme
953000
-
-
additional information
-
-
additional information
-
activity in vivo, intracellularly
additional information
-
activity in vivo, intracellularly and extracellularly
additional information
-
activity in vivo with different growth temperatures, intracellularly and extracellularly
additional information
-
activity in vivo, intracellularly and extracellularly
additional information
Sclerotium sp.
-
activity in vivo
additional information
-
activity in vivo, intracellularly and extracellularly
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
enzyme activity at pH 7.0, 23C, in nonionic micellar and reverse micellar systems, formed by mixing of Brij 30, Brij 35, cyclohexane, decaline, dodecane, n-heptane or isooctane, and water, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
peroxidase activity
4.5
-
optimum of first isoform
4.5
-
there are three isoenzymes with pH-optima at 4.5, 6.5, and 10.0
4.75
Q8X182
isoform Cat-2, peroxidase activity
5 - 10
B3FXQ9
broad optimum
5
-
aasay at, peroxidase activity
5.2 - 7.8
Capra capra
-
-
5.5 - 10
-
no sharp optimum
5.5 - 6
Q4F6N6
both catalase and peroxidase activity
6 - 10
A3REN3
broad optimum
6 - 8
Beta vulgaris var. cicla
-
-
6 - 9
Q8L2Z7
broad optimum
6.25
Q8X182
isoform Cat-2, catalase activity
6.4
-
catalase-peroxidase enzyme
6.5
-
optimal activity below pH 6.5
6.5
-
catalase activity
6.5
-
peroxidatic activity
6.5
-
optimum of second isoform
6.5
-
there are three isoenzymes with pH-optima at 4.5, 6.5, and 10.0
6.5
-
assay at
6.8 - 7.5
-
-
6.8
-
isoenzyme HPII, first pH-optimum
6.8
-
assay at, native PAGE
7 - 10
-
peroxidase and catalase activities
7 - 9
-
three isoforms
7 - 9
D7RJ66
-
7
Capra capra
-
-
7
-
sharp optimum
7
-
optimum for the extracellular enzyme
7
-
assay at, catalase activity
7
-
catalase activity
7
-
assay at, colorimetric method
7
-
both catalase and phenol oxidase activities
7
-
in 10 mM phosphate buffered saline
7
-
Eupergit C-immobilized enzyme
7
-
free enzyme and immobilized enzyme on nanoparticles
7
-
assay at
7
-
assay at
7.2
Kloeckera sp.
-
-
7.4
-
assay at
7.4
P00432
assay at
7.5
-
peroxidase activity
7.5
-
catalatic activity
7.5
-
free and immobilized catalase onto controlled pore glass
7.5
-
free enzyme
7.5
-
immobilized enzyme
7.5
-
assay at
8 - 10.5
-
isoenzyme II
8
-
isoenzyme I
8
-
both wild-type and mutant S2W
9.5
Q6LA34
in glycine-NaOH buffer, at 70C
10
-
optimum of third isoform
10
-
there are three isoenzymes with pH-optima at 4.5, 6.5, and 10.0
10.5
-
isoenzyme HPII, second pH-optimum
10.5
Q5LLG6
highest specific activity
additional information
-
the apparent pH optimum is the intersection of the optimum for binding, 7.0, and the optimum for activity, 5.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
-
pH-profile, TvC-I
3 - 11
-
about 40% of maximal activity at pH 3 and at pH 10
3 - 11
A3REN3
activity range
3 - 12
B3FXQ9
activity range, 53.4% of maximal activity at pH 4.0, 18.4% at pH 3.0
4 - 10
-
activity within
4 - 10
-
pH-profile, TvC-II
4 - 12
Q8X220
the purified CatP is stable and yields similar activity from pH 4.0 to 12.0
4 - 13
-
isoform Cat-2
4 - 6
-
peroxidase activity
4.5 - 10.5
A5XB38
above 90% of maximum activity
5 - 10
P08303
activit range
5 - 11
-
more than 50% of maximum activity within
5 - 11
D7RJ66
-
5 - 12
-
isoforms Cat-1, Cat-3
5 - 8
Q9AQQ9
-
5 - 9
Kloeckera sp.
-
activity within
5 - 9
-
more than 60% of catalase maximum activity within
5 - 9
-
activity range, free enzyme and immobilized enzyme on nanoparticles
5.5 - 8.5
Q4F6N6
-
6 - 11
-
-
6 - 7.5
-
the activity of Eupergit C-immobilized catalase remains almost constant for pH values 6.0-7.5 whereas this is not case for the free catalase
6 - 8
-
catalase activity
6 - 8
-
more than 80% of catalase maximum activity within
6 - 8.5
Capra capra
-
activity within
6 - 9
Q8L2Z7
rapid drop of activity below pH 6.0 and above pH 9.0
6.5 - 10
-
high activity within
8 - 10
A8CFD3
60 min, 30C, no loss of activity
additional information
Q4F6N6
no catalytic activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
-
cold-adapted enzyme
22
-
assay at room temperature
23
Q5LLG6
highest specific activity
23
-
assay at room temperature
25
-
assay at
25
-
free enzyme
25
-
assay at
25
B3FXQ9
assay at
25
A3REN3
-
25
-
immobilized enzyme
30 - 37
A5XB38
-
30
Beta vulgaris var. cicla
-
-
30
-
assay at
30
-
catalase activity
30
-
catalase activity
30
-
in 10 mM phosphate buffered saline
30
-
assay at
35
-
immobilized catalase onto controlled pore glass
35
-
free enzyme and immobilized enzyme on nanoparticles
37
Q8L2Z7
assay at
37
-
assay at
40
-
peroxidase activity
40
-
peroxidase activity
40
-
both wild-type and mutant S2W
40
-
Eupergit C-immobilized catalase
40
P08303
assay at
50
-
catalase activity
60
-
peroxidase activity
60
-
more than 70% of catalase maximum activity within
90
Q6LA34
at pH 7.0
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 37
-
activity within
0 - 37
-
-
0
D7RJ66
the enzyme has 78% activity at 0C
10 - 40
A3REN3
activity range
15 - 75
-
activity range, free enzyme and immobilized enzyme on nanoparticles
20 - 80
-
20C: about 75% of maximal activity, 80C: about 65% of maximal activity
25 - 35
-
high relative activity in the temperature range of 25-35C
30 - 100
Q6LA34
range of significant activity
30 - 60
-
activity in presence of ethanol-1,2-diol, overview
30 - 94
-
inactive at 20C
37 - 70
A5XB38
slight decrease in activity compared to temperature optimum
60
-
45% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
-
isoelectric focusing
4.9
-
isoelectric focusing
5
-
isoelectric focusing
5.4
-
isoelectric focusing
6
Q8X220
isoelectric focusing
6.1
Q6RSH8
calculated from amino acid sequence
6.2
Q8X220
isoelectric focusing
6.4
A9LSF7, A9QNB5, A9QNB6
calculated
6.5
A9LSF7, A9QNB5, A9QNB6
calculated
6.9
-
sequence calculation
6.9
C8XTA9
sequence calculation
8.7
A9LSF7, A9QNB5, A9QNB6
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
epithelial cell
Manually annotated by BRENDA team
A5XB38
constitutive expression for the first 3 h post injection of H2O2
Manually annotated by BRENDA team
-
Y-1 cell, increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
Manually annotated by BRENDA team
-
catalase activity increases with increasing blood lead level
Manually annotated by BRENDA team
-
catalase level is statistically decreased in patients with acne vulgaris compared to healthy ones
Manually annotated by BRENDA team
-
adrenocortical tumor cell, increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
Manually annotated by BRENDA team
-
colon tumor cell, increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
Manually annotated by BRENDA team
Q9C4N4
only present if growth medium is supplemented with hemin
Manually annotated by BRENDA team
-
KatB inducible by H2O2
Manually annotated by BRENDA team
-
inducible by H2O2, heat-shock, ethanol and stationary-phase conditions
Manually annotated by BRENDA team
-
inducible at low salt concentrations
Manually annotated by BRENDA team
Kloeckera sp.
-
methanol grown
Manually annotated by BRENDA team
Bacillus firmus OF4, Penicillium simplicissimum CBS 170.90
-
-
-
Manually annotated by BRENDA team
Kloeckera sp. 2201
-
methanol grown
-
Manually annotated by BRENDA team
-
Caco-2 cell, increased activity of catalase in tumor cells recombinantly overexpressing IGFBP-2 probably mediated through IGF-independent mechanisms
Manually annotated by BRENDA team
-
isoform Cat-1 mainly present
Manually annotated by BRENDA team
-
the catalase activity in striatum is significantly decreased in the lesioned group as compared to sham group and pretreatment with Withania somnifera reverses its activity significantly and dose dependently in the lesioned goup pretretaed with 100 mg/kg 200 mg/ml or 300 mg/kg body weight extracts of Withania somnifera orally as compared to lesioned group
Manually annotated by BRENDA team
Cucurbita sp.
-
-
Manually annotated by BRENDA team
-
heme in the growth medium is absolutely required for enzyme expression
Manually annotated by BRENDA team
-
0.5% v/v methanol in the cell culture medium
Manually annotated by BRENDA team
Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803
-
0.5% v/v methanol in the cell culture medium
-
Manually annotated by BRENDA team
Talaromyces piceae F-648
-
-
-
Manually annotated by BRENDA team
A9LSF7, A9QNB5, A9QNB6
expression is highest 46 h after cyst germination
Manually annotated by BRENDA team
A5XB38
constitutive expression for the first 3 h post injection of H2O2
Manually annotated by BRENDA team
-
from seeds
Manually annotated by BRENDA team
-
activities of catalase activity shows similar behavior after the exhaustive exercise bout, with a maximum activity at 3 h after the exercise. Activity tends to fall at 4 h after the exercise in comparison with 3 h
Manually annotated by BRENDA team
-
catalase activity increases with increasing blood lead level
Manually annotated by BRENDA team
-
enzyme activity is significantly lower in patients with Parkinsons disease compared to the control
Manually annotated by BRENDA team
-
pentylenetetrazol-induced epileptic seizure is accompanied by significantly reduced catalase activity
Manually annotated by BRENDA team
-
56 genotypes
Manually annotated by BRENDA team
A5XB38
constitutive expression for the first 3 h post injection of H2O2
Manually annotated by BRENDA team
A5XB38
constitutive expression for the first 3 h post injection of H2O2
Manually annotated by BRENDA team
-
diabetic animals treated with BioGHK incorporated collagen (Peptide Incorporated Collagen) show significant higher levels of catalase due to the ability of GHK to attract macrophages and cytokines towards the wound environment
Manually annotated by BRENDA team
-
activity increased significantly in the diazinon treated group compared with the control group
Manually annotated by BRENDA team
A5XB38
constitutive expression for the first 3 h post injection of H2O2
Manually annotated by BRENDA team
-
overexpression of hepatitis C virus non-structural proteins increases catalase activity
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
catalase activity is decreased dramatically after forebrain ischemia insult, no significant difference in catalase activity between control group and sham-operated group and curcumin-treted group
Manually annotated by BRENDA team
A9LSF7, A9QNB5, A9QNB6
highest expression
Manually annotated by BRENDA team
A7LP30
marked up-regulation of expression in larvae in which H2O2 is overloaded and after wounding through injection
Manually annotated by BRENDA team
-
fifth instar larval stage
Manually annotated by BRENDA team
Beta vulgaris var. cicla
-
-
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
activity continouosly increases from day 20 til day 70 after sowing
Manually annotated by BRENDA team
-
activity drastically diminishes from 7 to 17 days after sowing
Manually annotated by BRENDA team
O81336
stability of enzyme is increased in a light-dependent manner both in C3- and in crassulacean acid metabolism-induced plants, without changes in the level of leaf transcript
Manually annotated by BRENDA team
Capra capra
-
-
Manually annotated by BRENDA team
P04040
fetal liver
Manually annotated by BRENDA team
-
activity is increased by 1.13fold at 4 h after exposure to 50 cGy whole body gamma-irradiation and remains elevated at almost the same level up to 12 h after exposure
Manually annotated by BRENDA team
-
in azathioprine-treated rats a significant decrease in catalase activity is observed 24 h post-treatment. This inhibition is significantly released with pre-treatment with Hibiscus sabdariffa, Rosmarinus officinalisor Salvia officinalis
Manually annotated by BRENDA team
Mus musculus BALB/c
-
activity is increased by 1.13fold at 4 h after exposure to 50 cGy whole body gamma-irradiation and remains elevated at almost the same level up to 12 h after exposure
-
Manually annotated by BRENDA team
Capra capra
-
-
Manually annotated by BRENDA team
-
activity remains unaltered after exposure to 50 cGy whole body gamma-irradiation
Manually annotated by BRENDA team
Mus musculus BALB/c
-
activity remains unaltered after exposure to 50 cGy whole body gamma-irradiation
-
Manually annotated by BRENDA team
A5XB38
constitutive expression for the first 3 h post injection of H2O2
Manually annotated by BRENDA team
-
telomerase-deficient MEF cells have lower catalase activity
Manually annotated by BRENDA team
-
isoform Cat-3 mainly present
Manually annotated by BRENDA team
-
inducible by nitrate containing growth medium
Manually annotated by BRENDA team
Sclerotium sp.
-
activity in vivo
Manually annotated by BRENDA team
-
activity in vivo with different growth temperatures and pH, intracellularly and extracellularly
Manually annotated by BRENDA team
-
activity in vivo, intracellularly
Manually annotated by BRENDA team
-
activity in vivo, intracellularly and extracellularly
Manually annotated by BRENDA team
Penicillium cyclopium 1
-
activity in vivo with different growth temperatures and pH, intracellularly and extracellularly
-
Manually annotated by BRENDA team
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
-
-
-
Manually annotated by BRENDA team
-
retinal. mRNA transcript for catalase in normal (5.5 mM) glucose medium or high (22 mM) glucose medium after 1, 3, or 5 days of stimulation. The pattern of relative expression of the pericyte catalase transcript at day 1 is essentially unchanged at 3 and 5 days with only a slightly higher value (10%) in high glucose medium, which is statistically significantly increased after 1 (p = 0.037), 3 (p = 0.037), and 5 (p = 0.025) days
Manually annotated by BRENDA team
-
N2 fixing root nodules, transcription of katA from OxyR-dependent promoter
Manually annotated by BRENDA team
-
activity is kept at a high and stable value
Manually annotated by BRENDA team
-
from seeds
Manually annotated by BRENDA team
-
developing, expression and activity increase in non hydrated seeds and during desiccation on the mother plant and after artificial drying on the flowerhead
Manually annotated by BRENDA team
-
catalase activity is reduced significantly by lesioning, extract of Ginkgo biloba dose-dependently restores the activity
Manually annotated by BRENDA team
-
clone T-47DN5
Manually annotated by BRENDA team
-
no change in catalase activity after treatment with nicotinamide
Manually annotated by BRENDA team
Rattus norvegicus Wistar
-
no change in catalase activity after treatment with nicotinamide
-
Manually annotated by BRENDA team
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
-
-
-
Manually annotated by BRENDA team
-
mouse small mesenteric artery
Manually annotated by BRENDA team
additional information
-
catalase and bifunctional catalase-peroxidase are growth regulated and expressed mainly during the stationary phase, growth pattern analysis
Manually annotated by BRENDA team
additional information
-
germination tests and seed moisture content determination
Manually annotated by BRENDA team
additional information
Q6LA34
high enzyme activity when the strain VA1 is grown under aerobic conditions, and decreased activity under anaerobic growth
Manually annotated by BRENDA team
additional information
A7LP30
present in all tissues examined
Manually annotated by BRENDA team
additional information
Q8X220
the protein and expression level are reduced during the mycelial saprobic phase compared to the yeast phase of infection
Manually annotated by BRENDA team
additional information
A9LSF7, A9QNB5, A9QNB6
expression in all developmental stages except for 3-h germinated cysts. Highest expression occurs in sporulating hyphae and the least in 3-h germinated cysts
Manually annotated by BRENDA team
additional information
A9LSF7, A9QNB5, A9QNB6
major catalase in all developmental stages, with the highest expression occurring in sporulating hyphae and the lowest in 3-h germinated cysts. In planta, activity increases dramatically about 8 h after host inocculation
Manually annotated by BRENDA team
additional information
-
biofilm cultures
Manually annotated by BRENDA team
additional information
L8B3D7
catalase activity absolutely depends on exposure to O2 and occurs in cells grown in medium containing a heme source, these cells show higher viability on exposure to H2O2, growth optimum 37C
Manually annotated by BRENDA team
additional information
-
changes in the level of catalase activity in the three tissues of fat body, midgut and haemolymph of the five selected bivoltine breeds and their 9 quantitative traits, namely larval weight, cocoon weight, shell weight, shell ratio, filament length, filament weight, denier, renditta and effective rearing rate, and correlation between them under high temperature conditions, overview
Manually annotated by BRENDA team
additional information
-
constitutive epression, tissue expression analysis, overview
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
C8XTA9
tissue quantitative real-time RT-PCR expression analysis, overview. Expression level of catalase transcripts both in haemocytes and hepatopancreas changes rapidly and dynamically after Vibrio alginolyticus challenging in the intermoult stage
Manually annotated by BRENDA team
additional information
-
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
-
Manually annotated by BRENDA team
additional information
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
-
the protein and expression level are reduced during the mycelial saprobic phase compared to the yeast phase of infection
-
Manually annotated by BRENDA team
additional information
Bifidobacterium asteroides JCM 8230
-
catalase activity absolutely depends on exposure to O2 and occurs in cells grown in medium containing a heme source, these cells show higher viability on exposure to H2O2, growth optimum 37C
-
Manually annotated by BRENDA team
additional information
Pyrobaculum calidifontis VA1
-
high enzyme activity when the strain VA1 is grown under aerobic conditions, and decreased activity under anaerobic growth
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q9FAZ3
high level of H2O2 tolerance of strain S-1T even in presence of 100 mM H2O2 is attributable to its cell surface catalase activity
Manually annotated by BRENDA team
-
20% of the total activity
Manually annotated by BRENDA team
-
catalase and bifunctional catalase-peroxidase
Manually annotated by BRENDA team
-
enzyme is produced in the cytoplasm and transported into the periplasm by a Sec-independent enzyme transport, the enzyme contains no signal peptide at the N-terminus
Manually annotated by BRENDA team
-
enzyme is produced in the cytoplasm and transported into the periplasm by a Sec-independent enzyme transport, the enzyme contains no signal peptide at the N-terminus
-
Manually annotated by BRENDA team
Bifidobacterium asteroides JCM 8230
-
-
-
Manually annotated by BRENDA team
-
isoform Cat-3 secreted
-
Manually annotated by BRENDA team
-
constitutive, basal level of catalase activity. Inhibition of extracellular catalase activity by 3-amino-1,2,4-triazole or KCN leads to a striking inactivation of secreted cysteine cathepsins
-
Manually annotated by BRENDA team
Penicillium cyclopium 1
-
enzyme is secreted to the medium
-
-
Manually annotated by BRENDA team
Bacillus sp. 13, Talaromyces piceae F-648
-
-
-
-
Manually annotated by BRENDA team
Cucurbita sp.
-
exclusively localized
Manually annotated by BRENDA team
-
catalase-peroxidase enzyme
Manually annotated by BRENDA team
Penicillium cyclopium 1
-
mainly
-
Manually annotated by BRENDA team
Penicillium simplicissimum CBS 170.90
-
catalase-peroxidase enzyme
-
Manually annotated by BRENDA team
-
mainly in liver and kidney
Manually annotated by BRENDA team
-
enzyme is produced in the cytoplasm and transported into the periplasm by a Sec-independent enzyme transport, the enzyme contains no signal peptide at the N-terminus
-
Manually annotated by BRENDA team
Penicillium simplicissimum CBS 170.90
-
catalase only
-
-
Manually annotated by BRENDA team
-
enzyme is produced in the cytoplasm and transported into the periplasm by a Sec-independent enzyme transport, the enzyme contains no signal peptide at the N-terminus
-
-
Manually annotated by BRENDA team
Kloeckera sp.
-
-
Manually annotated by BRENDA team
Beta vulgaris var. cicla
-
-
Manually annotated by BRENDA team
-
peroxisomal matrix
Manually annotated by BRENDA team
-
mainly in liver and kidney
Manually annotated by BRENDA team
-
80% of the total activity
Manually annotated by BRENDA team
Q8X220
enzyme contains the peroxisome-PTS-1-targeting signal
Manually annotated by BRENDA team
-
main localization
Manually annotated by BRENDA team
Kloeckera sp. 2201
-
-
-
Manually annotated by BRENDA team
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
-
enzyme contains the peroxisome-PTS-1-targeting signal
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aliivibrio salmonicida (strain LFI1238)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Enterococcus faecalis (strain ATCC 700802 / V583)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
-
and 59000, gel filtration
689638
54000
Q5LLG6
gel filtration
699519
59000
-
and 48000, gel filtration
689638
80000
Q8X182
;
439772
84000
Q6RSH8
calculated from amino acid sequence
698069
110000
L8B3D7
about, gel filtration
725909
145000
Colwellia sp.
-
native polyacrylamide gel electrophoresis
700696
150000
-
native PAGE
439782
150000
-
gel filtration
439801
154000
Q6LA34
gel filtration
655845
160000
-
gel filtration
655626
170000
-
catalase-peroxidase
439784
170000
Pibocella sp.
-
native polyacrylamide gel electrophoresis
700696
178000
-
gel filtration
655112
183000
-
gel filtration
689731
185000
Sulfitobacter sp.
-
native polyacrylamide gel electrophoresis
700696
189000
-
gel filtration
688311
190000
O93662
gel filtration
439779
200000
-
gel filtration
656391
204000
-
gel filtration
654896
210000
-
ultracentrifugation
439800
220000
Capra capra
-
gel filtration
439805
223000
-
gel filtration
439773
225000
-
sucrose density gradient centrifugation
439806
227300
-
TvC-II, gel filtration
655372
228000
-
gel filtration
661985
230000
-
gel filtration
439776
230000
-
gel filtration
439778
230000
Cucurbita sp.
-
sucrose density gradient centrifugation
439795
230000
-
gel filtration
697068
230000
D7RJ66
gel filtration
712314
234000
A3REN3
native enzyme, gel filtration
725581
235000
Beta vulgaris var. cicla
-
gel filtration
439775
236000
-
gel filtration
439790
240000
-
gel filtration
439785, 439789
240000
Kloeckera sp.
-
gel filtration
439791
240000
Q9AQQ9
PAGE
685756
244000
Q8X220
gel filtration
712318
247000
B3FXQ9
gel filtration
725159
258000
-
isoenzyme with optimum at pH 10.0, SDS-PAGE
699027
260000
Q9C4N4
gel filtration
439774
280000
-
gel filtration
701415
285000
-
isoenzyme with optimum at pH 6.5, SDS-PAGE
699027
308000
-
isoenzyme with optimum at pH 4.5, SDS-PAGE
699027
318000
-
gel filtration
675328
320000
-
sedimentation equilibrium analysis, gel filtration
439803
320000
-
PAGE
684646
320000
O81336
-
689650
320000
-
-
712524
320000
-
-
723832
337000
-
sedimentation equillibrium analysis
439802
339000
Capra capra
-
gel filtration
439788
360000
-
native electrophoresis
439777
385000
-
sedimentation equilibrium analysis
439799
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q0D9C4
x * 54000, SDS-PAGE
?
-
x * 42000, SDS-PAGE
?
P04040
x * 60000, SDS-PAGE
?
A7LP30
x * 56000, SDS-PAGE
?
-
x * 57000, SDS-PAGE
?
Q8X220
x * 61000, SDS-PAGE
?
-
x * 84000, isoenzyme I, x * 60000, isoenzyme II, x * 80000, isoenzyme III, SDS-PAGE
?
-
x * 66.6, calculation from deduced amino acid sequence
?
-
x * 54000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 83200, SDS-PAGE
?
A8CFD3
x * 33000, calculated including the putative signal peptide, x * 33000, SDS-PAGE of recombinant inactive form
?
A5XB38
x * 56000, calculated, x * 98.5, SDS-PAGE of fusion protein with maltose binding protein
?
A9LSF7, A9QNB5, A9QNB6
x * 57700, calculated
?
A9LSF7, A9QNB5, A9QNB6
x * 57900, calculated
?
A9LSF7, A9QNB5, A9QNB6
x * 58400, calculated
?
Q4F6N6
x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein
?
A0S5U0
x * 57440, sequence calculation
?
-
x * 58000, recombinant isozyme Cat1.4, SDS-PAGE
?
C8XTA9
x * 58500, about, sequence calculation
?
Bacillus firmus OF4
-
x * 84000, isoenzyme I, x * 60000, isoenzyme II, x * 80000, isoenzyme III, SDS-PAGE
-
?
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
-
x * 61000, SDS-PAGE
-
dimer
-
2 * 75000, SDS-PAGE
dimer
-
2 * 80000, SDS-PAGE
dimer
-
1 * 75000 + 1 * 68000, SDS-PAGE
dimer
-
catalase-peroxidase, 2 * 85000, SDS-PAGE
dimer
-
2 * 92000, SDS-PAGE
dimer
Penicillium simplicissimum CBS 170.90
-
catalase-peroxidase, 2 * 85000, SDS-PAGE
-
dimer
Mycobacterium sp. JC1
-
2 * 80000, SDS-PAGE
-
dimer
Klebsiella pneumoniae IFO 14940
-
2 * 92000, SDS-PAGE
-
dimer
Mycobacterium sp. JC1 DSM 3803
-
2 * 80000, SDS-PAGE
-
hexamer
Q5LLG6
ring-like arrangement of six monomers, 6 * 7900 (SDS-PAGE), 6 * 8300 calculated
homodimer
L8B3D7
2 * 55000, SDS-PAGE
homodimer
Bifidobacterium asteroides JCM 8230
-
2 * 55000, SDS-PAGE
-
homotetramer
D7RJ66
4 * 58000, SDS-PAGE
homotetramer
P00432
4 * 60000, SDS-PAGE
homotetramer
B3FXQ9
4 * 59000, SDS-PAGE
homotetramer
-
4 * 80000, SDS-PAGE
homotetramer
-
4 * 72000, SDS-PAGE
homotetramer
Q8X220
4 * 61000, SDS-PAGE
homotetramer
Q9C168
x-ray crystallography
homotetramer
-
4 * 56000, gel filtration
homotetramer
A3REN3
4 * 74000, recombinant His-tagged catalase-A with bound heme cofactor, SDS-PAGE, 4 * 57000-58000, native enzyme
homotetramer
-
4 * 79000, wild-type and mutant enzymes, SDS-PAGE
homotetramer
-
4x * 58860, sequence calculation
homotetramer
Paracoccidioides brasiliensis ATCC MYA-826
-
4 * 61000, SDS-PAGE
-
homotetramer
-
4 * 56000, gel filtration
-
homotetramer
Serratia marcescens SYBC08
-
4 * 58000, SDS-PAGE
-
homotetramer
Psychrobacter piscatorii T-3
-
4 * 59000, SDS-PAGE
-
homotetramer
Scytalidium thermophilum ATCC 16454
-
4 * 79000, wild-type and mutant enzymes, SDS-PAGE
-
oligomer
O81336
x * 79000, + x* 74000, + x * 62000, higher molecular masses of subunits coincide with higher catalytic activity
tetramer
-
4 * 85000, SDS-PAGE
tetramer
Cucurbita sp.
-
4 * 55000, SDS-PAGE
tetramer
Q9AQQ9
4 * 60000, SDS-PAGE
tetramer
Capra capra
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 51000, SDS-PAGE
tetramer
-
4 * 42500, SDS-PAGE
tetramer
-
4 * 59000, SDS-PAGE
tetramer
-
4 * 62000, SDS-PAGE
tetramer
Kloeckera sp.
-
4 * 62000, SDS-PAGE
tetramer
-
4 * 80000, SDS-PAGE
tetramer
-
4 * 54000, SDS-PAGE
tetramer
-
4 * 54000, SDS-PAGE
tetramer
O93662
4 * 54000, SDS-PAGE
tetramer
-
4 * 92000, SDS-PAGE
tetramer
-
4 * 63000, SDS-PAGE
tetramer
-
4 * 79000, SDS-PAGE
tetramer
Beta vulgaris var. cicla
-
4 * 58500, SDS-PAGE
tetramer
-
4 * 84000, SDS-PAGE
tetramer
-
4 * 97000, SDS-PAGE
tetramer
-
4 * 60300, SDS-PAGE
tetramer
-
4 * 60000, SDS-PAGE for all three isoforms
tetramer
Q9C4N4
4 * 57700, MALDI-TOF
tetramer
-
4 * 57300, SDS-PAGE
tetramer
Q6LA34
4 * 33450, amino acid sequence calculation, 4 * 38000, SDS-PAGE
tetramer
-
4 * 62900, TvC-II, SDS-PAGE
tetramer
-
subunit composition of different plants, overview
tetramer
-
4 * 61000, SDS-PAGE, 4 * 54000, calculated
tetramer
-
tetramer in solution
tetramer
Rhodospirillum rubrum S1
-
4 * 79000, SDS-PAGE
-
tetramer
Kloeckera sp. 2201
-
4 * 62000, SDS-PAGE
-
tetramer
-
4 * 51000, SDS-PAGE
-
tetramer
Pyrobaculum calidifontis VA1
-
4 * 33450, amino acid sequence calculation, 4 * 38000, SDS-PAGE
-
monomer
-
1 * 80000, isoforms Cat-1, Cat-3
additional information
-
dehydration induces the synthesis of a 55 kDa subunit via activation of the CATA1 gene
additional information
-
determination and analysis of secondary enzyme structure
additional information
-
enzyme secondary structure analysis
additional information
O81336
sodium dodecylsufate treatment breaks active oligomeric catalse into the less active and putatively dimeric 160000 Da form
additional information
-
catalase form III structure analysis, overview
additional information
-
homology modeling of isozyme Cat1.4
additional information
A0S5U0
homology modelling, overview
additional information
-
determination and analysis of secondary enzyme structure
-
additional information
Talaromyces piceae F-648
-
enzyme secondary structure analysis
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
four different N-linked sugar moieties
glycoprotein
-
-
glycoprotein
-
8.1% mannose, 0.2% glucose, 1.9% glucosamine per weight
additional information
-
enzyme contains an N-terminal signal peptide comprising residues 24-38, clevage site is between residues 23 and 24
glycoprotein
-
-
additional information
-
no signal peptide at the N-terminus
additional information
-
no signal peptide at the N-terminus
-
glycoprotein
-
2-4% carbohydrate content
additional information
Q8X220
enzyme contains the peroxisome-PTS-1-targeting signal
additional information
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
-
enzyme contains the peroxisome-PTS-1-targeting signal
-
additional information
-
overexpression of cyanide-insensitive terminal oxidase leads to failure to produce temperature-inducible catalyse KatC without affecting transcription of katC. Presence of an intact disulfide bond formation system is required for KatC activity, and enzyme is predicted to contain two cysteine resiudes
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diffraction to 1.96 A. Comparison with catalase from Proteus mirabilis. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. The reduced thermal stability of cold-adapted Aliivibrio salmonicida catalase may be explained by a reduced number of ion-pair networks and displacement of the four C-terminal alpha-helices
Q3LSM1
fee enzyme and enzyme complexed with ammonia or NO, hanging drop vapor diffusion method, mixing of 0.004 ml of 12-13 mg/ml protein, containing NH4OH, with an equal volume of the reservoir solution consisting of 45-60 mM magnesium formate, pH 6.7, 2-3 weeks, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.88-1.99 A resolution
P00432
purified catalase form III, sitting drop vapour diffusion method, mixing of 40 mg/ml protein in 0.05 M sodium phosphate, pH 6.8, with reservoir solution containing 12% PEG 4000 and 0.05 M sodium phosphate, pH 6.8, X-ray diffraction structure determination and analysis at 2.69 A resolution
-
metal-bound [FeII/FeII]-ADEec and [FeII/MnII]-ADEec enzyme, sitting drop vapor diffusion, room temperature, X-ray diffraction struccture determination and analysis at 2.63-2.8 A resolution
-
homology modeling using crystal structures of human and bovine catalases
A5XB38
mutant M244A, diffraction to 2.0 A, monoclinic space group C2, presence of a dimer in the asymmetric unit
-
ammonium sulfate precipitation
Kloeckera sp.
-
comparison with catalase from Aliivibrio salmonicida LFI1238. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. Compared with Proteus mirabilis, the four C-terminal alpha-helices of Aliivibrio salmonicida LFI1238 catalase are displaced in the structures, explaining the reduced thermal stability
P42321
hanging drop vapour diffusion method, using 24% (w/v) PEG 2000, 10 mM NaCl, 10 mM CaCl2, and 3% (w/v) 6-aminocaproic acid in 100 mM bis-Tris buffer pH 6.5 at 18C
-
native and recombinant wild-type enzyme and enzyme mutants H82N and V123F, sitting drop vapour diffusion method, mixing of 9.4 mg/ml protein with reservoir solution containing 18% w/v PEG 2000, 0.1 M barium chloride, 0.1 M bis-tris pH 6.8 for the wild-type enzyme, and 6-16% w/v PEG 400, 0.2 M potassium chloride, 0.01 M calcium chloride, 0.05 M sodium cacodylate, pH 5.0-5.6 for the mutant H82N or PEG 4000 instead of PEG 400 for the mutant V123F, X-ray diffraction structure determination and analysis at 2.7 A, 1.4 A, 1.5 A, and 1.9 A resolution, respectively
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
-
TvC-I, half-life: at least 50 h
655372
1 - 3
-
TvC-I, half-life: about 2 h
655372
2
-
and below, TvC-I is rapidly inactivated
655372
3
-
no activity below
439778
3
-
TvC-I, half-life: at least 50 h
655372
3
-
inactivation
661985
3
-
more than 60% of the original activity is retained after treatment at pH 3.0 and 40C for 1h
712524
3.8 - 7.8
Q8X220
approximately 20% activity is observed at pH 3.8 followed by a steady rise of activity as the pH is increased to 7.8 (100% activity)
712318
4 - 10
-
TvC-II is rapidly inactivated below pH 4.0 and above pH 10.0, at pH 6.0-10.0 the half-life is approximately 20 h, at pH 5.0 it is 45 h, at pH 4.0 77 h
655372
4 - 11
-
stable within, enzyme from acatalasemic dog liver has a stability range from pH 6-9
439776
4 - 5
-
residual activity
439778
4
-
inactivation below
439803
4
Capra capra
-
inactivation below
439805
4
-
purified native enzyme, 15 min, inactivation
725606
4.5
B3FXQ9
purified native enzyme, 15 min, 60C, complete inactivation
725159
5 - 10
-
the enzyme is stable in the pH range of 5.0 to 10.0 after 1 h of treatment at 40C
701415
5.2 - 10.7
-
stable within
439773
6 - 10
-
purified native enzyme, stable, best at pH 7.0
725606
6 - 11
-
over 80% remaining activity after 1 h at 30C
654896
6 - 8
Beta vulgaris var. cicla
-
stable for 60 min at 25C, stability in basic media lower than in acidic media
439775
6 - 9
-
maximum stability within, isoform Cat-3
439798
7 - 10
-
maximum stability within, isoform Cat-1
439798
7 - 11
-
maximum stability within, isoform Cat-2
439798
7
-
rapid inactivation below
439806
7
-
24 h, more than 90% of initial activity
684646
8
B3FXQ9
purified native enzyme, 15 min, 60C, most stable at
725159
9
-
optimal stability value
439806
9
-
85% remaining activity after 20 h at 30C
654896
9
-
70C, half-life: 510 h
655112
9
-
immobilized catalase onto controlled pore glass retains 80% of its maximum activity at pH 9.0, while free catalase retains only 40% of its maximum activity at pH 9.0
699601
10
-
70C, half-life: 360 h
655112
11
Capra capra
-
inactivation above
439805
11
B3FXQ9
purified native enzyme, 15 min, 60C, complete inactivation
725159
additional information
Q5LLG6
HTHP is stable under a wide range of pH values
699519
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
-
675328
25 - 70
-
when the extract is incubated at specified temperature (25-70C) 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 70C for pHs of 6.5, 10.0, and 4.5, respectively. After heating at 70C 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.
699027
30 - 60
-
thermoinactivation kinetics in the presence or absence of substrate H2O2, overview
726417
30
-
50% loss of activity in 30 min
439782
30
-
85% remaining peroxidase activity after 20 h at pH 9.0
654896
30
Q8L2Z7
10 min, loss of 20% activity
655297
35 - 40
-
slightly suppressed activity
439778
35 - 50
-
the half-lives of free catalase at 35 and 50C 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
699601
37
-
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
657432
40 - 50
-
the half lives of free catalase at 40 and 50C are 9.0 and 6.7 h, respectively, and correspondingly 29.1 and 4.8 h for Eupergit C-immobilized catalase
712789
40 - 60
-
the enzyme is stable for 24 h at 40C with a half-life of 4 h 60C, at 50C the half life is about 18 h
701415
40
-
inactivation above
439792
40
Q9AQQ9
15 h, incubation below 40C, retains most of its activity. Activity is quickly lost above 40C
685756
40
A5XB38
1 h, 60% residual activity
686832
40
A3REN3
stable up to, a sharp decline in activity above
725581
40
-
purified native enzyme, 15 min, stable
725606
45
-
30% loss of activity in 30 min, enzyme from acatalasemic liver has 70% loss of activity in 30 min
439776
45
-
stable up to
439785
45
-
Cat-1 half-life: 12.5 min, Cat-3 half-life: 18 min, Cat-2 stable
439798
45
-
60 min, 17% decreased activity
654036
50 - 60
-
65% residual activity after 15 min at 50C, 54% residual activity after 30 min at 50C, 43% residual activity after 40 min at 50C, 12% residual activity after 15 min of preincubation at 60C, preincubation at 65C for 10 min results in complete loss of activity
697068
50
Beta vulgaris var. cicla
-
half-life: 30 min
439775
50
-
loss of both catalase-peroxidase activities
439790
50
-
155% activation during transfer from 4C in 5 min
439792
50
-
-
439792
50
-
188% activation during t