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 ACCESSION NO.
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
distal site Asp152 is essential for the catalase activity of catalase-peroxidase, mechanism for hydrogen peroxide oxidation in volving residues Trp122 and Asp152
-
2 H2O2 = O2 + 2 H2O
show the reaction diagram
catalytic mechanism
-
2 H2O2 = O2 + 2 H2O
show the reaction diagram
the catalytically relevant active site residues Trp111, Tyr238, and Met264 are linked by a covalent structure
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
ethanol degradation IV
-
Glyoxylate and dicarboxylate metabolism
-
methanol oxidation to formaldehyde IV
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
Ab-catalase
A5XB38
-
BNC
-
-
-
caperase
-
-
-
-
CAT
-
-
-
-
CAT
Geomyces pannorum
-
-
CAT
Penicillium cyclopium 1
-
-
-
CAT
Penicillium islandicum
-
-
CAT
Penicillium piceum
-
-
CAT
Penicillium piceum F-648
-
-
-
CAT
Sclerotium sp.
-
-
CAT
-
-
CAT-1
Q9C168
-
CAT-A
A3REN3
-
CAT-A
Penicillium piceum
-
-
CAT-P
Penicillium piceum
-
-
CatA
Q6RSH8
monofunctional catalase
catalase
Colwellia sp.
-
-
catalase
Colwellia sp. MH2
-
-
-
catalase
-
-
catalase
A9GRH4
-
catalase
Phaeobacter gallaeciensis BS107
A9GRH4
-
-
catalase
Pibocella sp.
-
-
catalase
Pibocella sp. MH3
-
-
-
catalase
Roseibacterium elongatum OCh 323
-
-
-
catalase
Roseisalinus antarcticus EL-88
-
-
-
catalase
Sulfitobacter sp.
-
-
catalase
Sulfitobacter sp. MH1
-
-
-
catalase
-
-
catalase
Wenxinia marina HY34
-
-
-
catalase
-
-
catalase -peroxidase KatG
-
-
catalase A
Q6RSH8
monofunctional catalase
catalase C
Q6RSH8
a bifunctional catalase-peroxidase
catalase form III
-
-
catalase P
Q6RSH8
monofunctional catalase
catalase P
Paracoccidioides brasiliensis ATCC MYA-826, Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
Q8X220
-
-
catalase-1
Q9C168
-
catalase-A
A3REN3
-
catalase-peroxidase
-
-
-
-
catalase-peroxidase
-
-
catalase-peroxidase
-
-
-
catalase-peroxidase
-
-
catalase-peroxidase
Q939D2
-
catalase-peroxidase
-
-
catalase-peroxidase
-
-
catalase-peroxidase
-
-
catalase-peroxidase
Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803
-
-
-
catalase-peroxidase
-
-
catalase-peroxidase
-
; bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7
catalase-peroxidase
-
bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7
catalase-peroxidase
Q08129
-
catalase-peroxidase
-
-
catalase-peroxidase
-
-
catalase-peroxidase
-
bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7
catalase-peroxidase
-
-
catalase-phenol oxidase
-
bifunctional enzyme, its major activity is the catalase-mediated decomposition of hydrogen peroxide, but it also catalyzes phenol oxidation
catalase/peroxidase
A4QUT2, A4R5S9
-
catalase/peroxidase
Magnaporthe grisea MA 829
A4QUT2, A4R5S9
-
-
CATC
Q6RSH8
a bifunctional catalase-peroxidase
CatP
Q6RSH8
monofunctional catalase
CatP
Paracoccidioides brasiliensis ATCC MYA-826
Q8X220
-
-
CATPO
Scytalidium thermophilum ATCC 16454
-
-
-
CP
Mycobacterium sp. JC1, Mycobacterium sp. JC1 DSM 3803
-
-
-
equilase
-
-
-
-
H2O2:H2O2 oxidoreductase
-
-
H2O2:H2O2 oxidoreductase
-
-
H2O2:H2O2 oxidoreductase
-
-
H2O2:H2O2 oxidoreductase
-
-
haem catalase
L8B3D7
-
haem catalase
Bifidobacterium asteroides JCM 8230
L8B3D7
-
-
HPI-A
-
catalase-peroxidase isoenzyme
HPI-B
-
catalase-peroxidase isoenzyme
HPII
-
monofunctional catalase
HTHP
Q5LLG6
peroxidase and catalase activity
hydrogen peroxide oxidoreductase
-
-
Kat E catalase
-
-
KatA
Helicobacter pylori 26695, Helicobacter pylori Taiwanese TW-34
-
-
-
KatG
A4QUT2, A4R5S9
-
KatG
Magnaporthe grisea MA 829
A4QUT2, A4R5S9
-
-
KatG
-
; bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7
KatG
-
bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7
KatG
-
bifunctional enzyme with activities of EC 1.11.1.6 and EC 1.11.1.7
KatG1
A4R5S9
located intracellularly
KatG1
Magnaporthe grisea MA 829
A4R5S9
located intracellularly
-
KatG2
A4QUT2
located extracellularly
KatG2
Magnaporthe grisea MA 829
A4QUT2
located extracellularly
-
KpA
Klebsiella pneumoniae IFO 14940
-
-
-
manganese catalase
A8CFD3
-
manganese catalase
Q6LA34
-
optidase
-
-
-
-
PktA
Psychrobacter piscatorii T-3
B3FXQ9
-
-
polyethylene glycol-catalase
-
-
-
-
tyrosine-coordinated heme protein
Q5LLG6
-
VktA
Q9FAZ3
-
manganese catalase
Pyrobaculum calidifontis VA1
Q6LA34
-
-
additional information
-
enzyme belongs to the family of monofunctional catalases
CAS REGISTRY NUMBER
COMMENTARY
9001-05-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme expression is induced under phosphate-limiting growth conditions
-
-
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
bifunctional catalase-peroxidase KatG
-
-
Manually annotated by BRENDA team
gene katG, bifunctional enzyme KatG with catalase and peroxidase activities
SwissProt
Manually annotated by BRENDA team
Capra capra
goat
-
-
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
microfungus isolated from soil collected in arctic tundra
-
-
Manually annotated by BRENDA team
isoform CatA
-
-
Manually annotated by BRENDA team
isoform CatB
-
-
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
Geomyces pannorum
microfungus isolated from soil collected in arctic tundra
-
-
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
strain MA 829
UniProt
Manually annotated by BRENDA team
Magnaporthe grisea MA 829
strain MA 829
UniProt
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
; enzyme KatG is a bifunctional
-
-
Manually annotated by BRENDA team
bifunctional catalase-peroxidase KatG
-
-
Manually annotated by BRENDA team
clinical isolates from Malatya, Turkey
-
-
Manually annotated by BRENDA team
enzyme KatG, gene katG
-
-
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
A3REN3
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
Penicillium islandicum
microfungus isolated from soil collected in arctic tundra, 2 strains
-
-
Manually annotated by BRENDA team
Penicillium piceum
strain F-648
-
-
Manually annotated by BRENDA team
Penicillium piceum
strains F-648 and A-3
-
-
Manually annotated by BRENDA team
Penicillium piceum F-648
strain F-648
-
-
Manually annotated by BRENDA team
Phaeobacter gallaeciensis BS107
-
A9GRH4
UniProt
Manually annotated by BRENDA team
isoform Cat1
A9QNB6
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
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
strain PCC 6803
-
-
Manually annotated by BRENDA team
gene katG, KatG is a bifunctional enzyme showing both catalase and peroxidase activities
-
-
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
Q8L2Z7
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
catalase is responsible for the enzymatic destruction/detoxification of hydrogen peroxide, to combat its deleterious effects
physiological function
P08303, -
the catalase activity of CcO is clearly a side reaction
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
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
-
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
-
catalase is an antioxidant enzyme and plays a significant role in the protection against oxidative stress by reducing hydrogen peroxide
physiological function
A3REN3
chaperone-specific enzyme regulation, overview
physiological function
C8XTA9, -
catalase is an important antioxidant protein that protects organisms against various oxidative stresses by eliminating hydrogen peroxide
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
-
the heme-binding pocket contains two highly conserved water molecules on the distal side
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
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
A0S5U0, -
homology modelling, overview
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
C8XTA9, -
conserved catalytic active residues are His71, Asn144, and Tyr354
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
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 ACCESSION NO.
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
-
-
-
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
A4QUT2, A4R5S9, -
-
-
-
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
Magnaporthe grisea MA 829
A4QUT2, A4R5S9
-
-
-
?
2,6-dimethoxyphenol + H2O2
? + H2O
show the reaction diagram
Penicillium simplicissimum, Penicillium simplicissimum CBS 170.90
-
-
-
?
2-dianisidine + tert-butyl hydroperoxide
?
show the reaction diagram
-
peroxidase activity
-
-
?
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
A4QUT2, A4R5S9, -
-
-
-
?
ethanol + H2O2
acetaldehyde + ?
show the reaction diagram
-
no peroxidase activity
-
?
ethanol + H2O2
acetaldehyde + ?
show the reaction diagram
Magnaporthe grisea MA 829
A4QUT2, A4R5S9
-
-
-
?
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
-
-
-
guaiacol + H2O2
?
show the reaction diagram
A4QUT2, A4R5S9, -
-
-
-
?
guaiacol + H2O2
?
show the reaction diagram
Magnaporthe grisea MA 829
A4QUT2, A4R5S9
-
-
-
?
guajacol + H2O2
? + H2O
show the reaction diagram
-
peroxidase activity
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Kloeckera sp.
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Penicillium islandicum
-
-
-
-
?
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
Geomyces pannorum
-
-
-
-
?
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
Q8X220
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Penicillium piceum
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Q939D2
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Mortierella minutissima, Sclerotium sp.
-
-
-
-
?
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
Q08129
-
-
-
?
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
-
also significant peroxidase activity
-
?
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
Q939D2
detoxification enzyme, protection against peroxides
-
-
?
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
Penicillium piceum
-
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
-
catalase activity
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
catalase activity
-
-
?
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
-
it is proposed that binding of substrate H2O2 to Asp141 and Arg108 controls H2O2 access to the heme active site, thereby modulating the catalase reaction
-
-
?
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
Penicillium piceum 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
-
-, 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
-
-
-
-
?
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
?
show the reaction diagram
-
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
-
-
-
-
?
isonazid + H2O2
?
show the reaction diagram
-
-, activation of antituberculosis drug isonazid, catalytic mechanism
-
-
?
isoniazid + H2O2
isonicotinic acid + H2O
show the reaction diagram
-
antituberculosis drug
-
?
isoniazid + NADH
isonicotinic acyl-NADH
show the reaction diagram
-
isoniazid activation
the product is a strong inhibitor of the NADH-dependent enoyl-[acyl carrier protein] reductase InhA and the beta-ketoacyl [acyl carrier protein] synthase
-
?
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
-
-
-
?
NADH + H2O2
NAD+ + H2O
show the reaction diagram
-
-
-
?
NADPH + H2O2
NADP+ + 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
?
show the reaction diagram
Q08129
-
-
-
?
o-dianisidine + H2O2
?
show the reaction diagram
A4QUT2, A4R5S9, -
-
-
-
?
o-dianisidine + H2O2
?
show the reaction diagram
Magnaporthe grisea MA 829
A4QUT2, A4R5S9
-
-
-
?
o-dianisidine + H2O2
? + H2O
show the reaction diagram
-
-
-
?
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-dianisidine + H2O2
? + H2O
show the reaction diagram
-
peroxidase 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
-
?
p-phenylendiamine + H2O2
? + H2O
show the reaction diagram
-
-
-
?
picolinic hydrazide
?
show the reaction diagram
-
analysis of association and dissociation rate constants
-
-
-
pyrogallol + H2O2
?
show the reaction diagram
A4QUT2, A4R5S9, -
-
-
-
?
pyrogallol + H2O2
?
show the reaction diagram
Magnaporthe grisea MA 829
A4QUT2, A4R5S9
-
-
-
?
pyrogallol + H2O2
? + H2O
show the reaction diagram
-
-
-
?
pyrogallol + H2O2
? + H2O
show the reaction diagram
-
-
-
?
pyrogallol + H2O2
? + H2O
show the reaction diagram
-
-
-
?
pyrogallol + H2O2
? + H2O
show the reaction diagram
-
peroxidase activity
-
-
?
reduced cytochrome c + H2O2
oxidized cytochrome c + H2O
show the reaction diagram
-
-
-
?
tert-butyl peroxide + H2O2
?
show the reaction diagram
Q08129
-
-
-
?
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
?
-
-
bifunctional enzyme providing catalase and peroxidase activities, intermediate structure
-
-
-
additional information
?
-
-
bifunctional enzyme showing both catalase and peroxidase activities
-
-
-
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 ACCESSION NO.
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
-
-
-
?
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
Kloeckera sp.
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Penicillium islandicum
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
-
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
Geomyces pannorum
-
-
-
-
?
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
-
-
-
-
?
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
-
also significant peroxidase activity
-
?
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
Q939D2
detoxification enzyme, protection against peroxides
-
-
?
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
Penicillium piceum
-
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
Penicillium piceum 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
-
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
Pyrobaculum calidifontis VA1
Q6LA34
detoxification enzyme
-
-
?
isonazid + H2O2
?
show the reaction diagram
-
activation of antituberculosis drug isonazid, catalytic mechanism
-
-
?
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 ACCESSION NO.
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
-
protoporphyrin IX, 0.98 heme per dimer
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
-
1.2-1.5 hemes per enzyme dimer
heme
-
binding pocket distal side: triad residues P151, D152, and N153 are important for stability, they interact with the binding pocket proximal side residues W341, D402, and H290
heme
-
wild-type and S315T mutant enzyme, determination of Fe2+-binding/interaction structure
heme
-
dependent on, contains 1 protoheme IX group per KatA 54 kDa polypeptide
heme
-
it is proposed that binding of substrate H2O2 to Asp141 and Arg108 controls H2O2 access to the heme active site, thereby modulating the catalase reaction
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
A4QUT2, A4R5S9, -
; oxidoreductase with a predominant five-coordinated high-spin heme b, ferric MagKatG1 exhibits the typical bands of a heme b-containing peroxidase
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
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
CO
-
complexed with the enzyme, structure determination, binding kinetics
Cu2+
-
less than 0.2 g-atom cupper per mol enzyme
Fe
-
dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant
Fe2+
-
enzyme contains heme
Fe2+
-
enzyme contains heme
Fe2+
-
wild-type and S315T mutant enzyme, determination of Fe2+-binding/interaction structure
Fe2+
-
TvC-II, heme-containing
Fe2+
-
heme-containing enzyme
Fe2+
-
enzyme contains a heme modified with a special hydroperoxide group added to ring I
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+
-
activates isoniazid activation, not essential
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%)
NO
-
complexed with the enzyme, structure determination, binding kinetics
Mn2+
-
stimulatory effect at 2 mM
additional information
Penicillium piceum
-
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 ACCESSION NO.
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
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
-
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
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+
Penicillium piceum
-
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
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%
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 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 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
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
-
-
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 ACCESSION NO.
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.063
-
2-dianisidine
-
recombinant mutant D735A, 23C
0.064
-
2-dianisidine
-
recombinant mutant A110V, 23C
0.065
-
2-dianisidine
-
recombinant mutant L634F, 23C
0.078
-
2-dianisidine
-
recombinant mutant L619P, 23C
0.081
-
2-dianisidine
-
recombinant mutant S315N, 23C
0.084
-
2-dianisidine
-
recombinant wild-type enzyme, 23C
0.096
-
2-dianisidine
-
recombinant mutant A139P, 23C
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
2.4
-
H2O2
-
mutant D152S, pH 7.0, 30C
2.4
-
H2O2
-
mutant D152S, pH 7.0, 30C
2.5
-
H2O2
-
mutants D152N and P151A, pH 7.0, 30C
2.5
-
H2O2
-
mutants D152N and P151A, pH 7.0, 30C
3
-
H2O2
-
peroxidase activity, pH 7.0, 25C
3.2
-
H2O2
-
mutant D152W, pH 7.0, 30C
3.2
-
H2O2
-
mutant D152W, pH 7.0, 30C
3.5
-
H2O2
-
wild-type, pH 7.0, 23C
3.7
-
H2O2
-
catalase activity
3.7
-
H2O2
-
isoenzyme HPI
4
-
H2O2
Q0D9C4
mutant L189W/H225T
4.1
-
H2O2
-
wild-type enzyme, pH 7.0, 30C
4.1
-
H2O2
-
wild-type enzyme, pH 7.0, 30C
4.3
-
H2O2
-
mutant W341A, pH 7.0, 30C
4.8
-
H2O2
A4QUT2, A4R5S9, -
at pH 6.0 and 25C; at pH 6.0 and 25C
5.16
-
H2O2
-
pH 6.0, 25C
5.2
-
H2O2
-
mutant Y111A, pH 7.0, 23C
5.9
-
H2O2
-
recombinant wild-type enzyme, 23C
5.9
-
H2O2
-
mutant D402E, pH 7.0, 30C
6.3
-
H2O2
-
mutant W341F, pH 7.0, 30C
6.3
-
H2O2
-
catalase activity, pH 7.0, 30C
6.4
-
H2O2
-
mutant D402N, pH 7.0, 30C
10
-
H2O2
-
isoenzyme HPII, pH 10.5
10.3
-
H2O2
-
recombinant mutant A110V, 23C
10.7
-
H2O2
-
recombinant mutant A139P, 23C
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
14.3
-
H2O2
-
recombinant mutant L634F, 23C
14.8
-
H2O2
-
recombinant mutant D735A, 23C
15
-
H2O2
-
mutant H290Q, pH 7.0, 30C
16.2
-
H2O2
-
pH 7.0, 40C
16.8
-
H2O2
-
recombinant mutant S315N, 23C
17.1
-
H2O2
-
recombinant mutant L619P, 23C
17.2
-
H2O2
Q5LLG6
-
18.2
-
H2O2
-
isoenzyme HPII, pH 6.8
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
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
158.8
-
H2O2
Penicillium piceum
-
catalase from Penicillium piceum strain F-648
170
-
H2O2
-, Q6LA34
pH 7.0, 25C
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
-
steady- and transient-state kinetics
-
additional information
-
additional information
P08303, -
Michaelis-Menten kinetics, overview
-
additional information
-
additional information
-
kinetic modeling, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.86
-
2-dianisidine
-
recombinant mutant S315N, 23C
0.99
-
2-dianisidine
-
recombinant mutants L634F and D735A, 23C
1.06
-
2-dianisidine
-
recombinant mutant L619P, 23C
1.69
-
2-dianisidine
-
recombinant mutant A139P, 23C
3.48
-
2-dianisidine
-
recombinant wild-type enzyme, 23C
4.85
-
2-dianisidine
-
recombinant mutant A110V, 23C
3
-
H2O2
-
mutant H290Q, pH 7.0, 30C
11
-
H2O2
-
presence of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 6.0
16
-
H2O2
-
mutant W341A, pH 7.0, 30C
17
-
H2O2
-
mutant D402N, pH 7.0, 30C
20
-
H2O2
-
mutant D152W, pH 7.0, 30C
20
-
H2O2
-
mutant D152W, pH 7.0, 30C
20
-
H2O2
-
presence of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 5.5
21
-
H2O2
-
mutant D402E, pH 7.0, 30C
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
95
-
H2O2
-
mutant D152N, pH 7.0, 30C
95
-
H2O2
-
mutant D152N, pH 7.0, 30C
151
-
H2O2
-
presence of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 4.0
200
-
H2O2
-
mutant D152S, pH 7.0, 30C
200
-
H2O2
-
mutant D152S, pH 7.0, 30C
200
-
H2O2
-
pH 7.5, 30C
1460
-
H2O2
-
mutant W341F, pH 7.0, 30C
2140
-
H2O2
-
mutant Y111A, pH 7.0, 23C
2500
-
H2O2
-
mutant P151A, pH 7.0, 30C
2500
-
H2O2
-
mutant P151A, pH 7.0, 30C
2750
-
H2O2
-
recombinant mutant D735A, 23C
2990
-
H2O2
-
recombinant mutant S315N, 23C
3000
-
H2O2
-
pH 6.0, 25C
3180
-
H2O2
-
recombinant mutant L619P, 23C
3270
-
H2O2
-
recombinant wild-type enzyme, 23C
3330
-
H2O2
-
recombinant mutant A139P, 23C
3450
-
H2O2
-
recombinant mutant L634F, 23C
3500
-
H2O2
-
wild-type enzyme, pH 7.0, 30C
3500
-
H2O2
-
wild-type enzyme, pH 7.0, 30C
5230
-
H2O2
-
recombinant mutant A110V, 23C
7010
-
H2O2
A4QUT2, A4R5S9, -
at pH 6.0 and 25C; at pH 6.0 and 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
2830000
-
H2O2
Penicillium piceum
-
catalase from Penicillium piceum strain F-648 at the minimum degree of association (0.3 nM)
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
24
-
H2O2
-
pH 7.5, 30C
11283
160
-
H2O2
-
catalase covalently immobilized onto Eupergit C, in 50 mM phosphate buffer pH 7.0, at 25C
11283
21000
-
H2O2
-
free catalase, in 50 mM phosphate buffer pH 7.0, at 25C
11283
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
2e-07
-
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
2.9e-05
-
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
1.4e-05
-
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
0.18
-
-
substrate o-dianisidine, mutant H290Q
0.5
-
-
substrate guajacol, mutant P151A
0.6
-
-
substrate guajacol, wild-type enzyme
0.8
-
-
substrate o-dianisidine, mutant W341A
0.94
-
-
purified enzyme, peroxidase activity, mixed-type
1.5
-
-
about, cell lysates of wild-type Caco-2 cells
1.8
-
-
substrate o-dianisidine, mutant D402N
2.1
-
-
substrate o-dianisidine, mutant D402E
2.4
-
-
substrate o-dianisidine, mutant P151A
2.4
-
-
substrate o-dianisidine, mutant P151A
2.5
-
-
substrate guajacol, mutants D152N and D152S
3.2
-
-
substrate o-dianisidine, wild-type enzyme
3.2
-
-
substrate o-dianisidine, wild-type enzyme
3.5
4.5
-
about, cell lysates of wild-type Y-1 cells
4
-
-
mutant H82N, pH 7.0, 60C
4.1
-
-
substrate guajacol, mutant D152W; substrate pyrogallol, mutant P151A
6
-
-
about, cell lysates of Caco-2 cells recombinantly overexpressing IGFBP-2
6.1
-
-
substrate o-dianisidine, mutant W341F
6.6
-
-
substrate pyrogallol, wild-type enzyme
7.3
-
-
substrate pyrogallol, mutant D152W
7.5
-
-
substrate o-dianisidine, mutant D152N
7.5
-
-
substrate o-dianisidine, mutant D152N
7.6
-
-
substrate o-dianisidine, mutant D152S
7.6
-
-
substrate o-dianisidine, mutant D152S
8
-
-
about, cell lysates of Y-1 cells recombinantly overexpressing IGFBP-2
8.76
-
-
catalase activity after 5 days of cell culture
12.5
-
-
substrate pyrogallol, mutant D152N
13.6
-
-
substrate pyrogallol, mutant D152S
15.2
-
-
peroxidatic activity
21.5
-
-
substrate o-dianisidine, mutant D152W
21.5
-
-
substrate o-dianisidine, mutant D152W
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
560
-
-
-
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
2200
-
Q939D2
purified recombinant enzyme, catalase-specific activity
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
20700
-
-
-
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
-
-
61500
-
O93662
-
75000
-
-
isoenzyme II
91800
-
-
-
109100
-
-
-
120000
-
-, Q9C4N4
half-maximal activity at 30 mM H2O2
121000
-
-
-
145800
-
-
-
160000
-
-
-
199600
-
D7RJ66, -
after 13.8fold purification, pH 7.0, at 20C
222000
-
B3FXQ9
purified native enzyme, pH 7.0, 25C
273800
-
-
-
282000
-
Kloeckera sp.
-
-
395000
-
-
-
500000
-
-
purified enzyme
953000
-
-
-
additional information
-
-
-
additional information
-
Geomyces pannorum
-
activity in vivo, intracellularly and extracellularly
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
-
Penicillium islandicum
-
activity in vivo, intracellularly and extracellularly
additional information
-
Sclerotium sp.
-
activity in vivo
additional information
-
-
isoniazid activation activities of wild-type and mutant enzymes in absence or presence of Mn2+, overview
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
5.5
A4QUT2, A4R5S9, -
also acts as a versatile peroxidase with a pH optimum in the range 5.0-5.5, using both one-electron [2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid), o-dianisidine, pyrogallol, or guaiacol] and two-electron (Br-, I- or ethanol) donors; also acts as a versatile peroxidase with a pH optimum in the range 5.0-5.5, using both one-electron [2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid), o-dianisidine, pyrogallol, or guaiacol] and two-electron (Br-, I- or ethanol) donors
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
-
Q9AQQ9
-
6
-
A4QUT2, A4R5S9, -
;
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
-
-
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
-
Q939D2
assay at
7
-
-
assay at, catalase activity
7
-
-
assay at
7
-
-
catalase activity
7
-
-
assay at, colorimetric method
7
-
-
both catalase and phenol oxidase activities
7
-
A7LP30, -
-
7
-
Penicillium piceum
-
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
-
Penicillium piceum
-
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
-
P08303, -
-
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
-
A5XB38
-
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
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
-
cold-adapted enzyme
20
-
D7RJ66, -
-
22
-
-
assay at room temperature
23
-
Q5LLG6
highest specific activity
23
-
-
assay at room temperature
25
-
-
assay at
25
-
-
assay at
25
-
-
-
25
-
-
free enzyme
25
-
-
assay at
25
-
B3FXQ9
assay at
25
-
A3REN3
-
25
-
-
immobilized enzyme
30
-
Beta vulgaris var. cicla
-
-
30
-
Penicillium piceum
-
assay at
30
-
-
assay at
30
-
-
catalase activity
30
-
-
catalase activity
30
-
A7LP30, -
-
30
-
Penicillium piceum
-
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
-
Q939D2
assay at
37
-
Q8L2Z7
assay at
37
-
-
assay at
40
-
-
peroxidase activity
40
-
-
peroxidase activity
40
-
Q9AQQ9
-
40
-
-
both wild-type and mutant S2W
40
-
-
Eupergit C-immobilized catalase
40
-
P08303, -
assay at
40
-
-
-
50
-
-
catalase activity
60
-
-
peroxidase activity
60
-
-
more than 70% of catalase maximum activity within
90
-
-, Q6LA34
at pH 7.0
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.2
-
-
isoelectric focusing
4.9
-
Penicillium piceum
-
-
4.9
-
-
isoelectric focusing
5
-
-
isoelectric focusing
5.4
-
-
isoelectric focusing
5.7
-
A4QUT2, A4R5S9, -
isoelectric focusing; isoelectric focusing
6
-
Q8X220
isoelectric focusing
6
-
A4QUT2, A4R5S9, -
calculated from amino acid sequence; calculated from amino acid sequence
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 ACCESSION NO.
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
-
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
-
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
-, 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
-
-
-
Manually annotated by BRENDA team
Kloeckera sp. 2201
-
methanol grown
-
Manually annotated by BRENDA team
Penicillium simplicissimum CBS 170.90
-
-
-
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
-, Q8X182
isoform Cat-1 mainly present; 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
Penicillium piceum
-
-
Manually annotated by BRENDA team
Penicillium piceum 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
-
pentylenetetrazol-induced epileptic seizure is accompanied by significantly reduced catalase activity
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
-
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
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
-
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
P04040
fetal liver
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
-, Q8X182
isoform Cat-3 mainly present; isoform Cat-3 mainly present
Manually annotated by BRENDA team
-
inducible by nitrate containing growth medium
Manually annotated by BRENDA team
-
activity in vivo, intracellularly
Manually annotated by BRENDA team
Geomyces pannorum
-
-
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
-
activity in vivo, intracellularly and extracellularly
Manually annotated by BRENDA team
-
activity in vivo with different growth temperatures and pH, intracellularly and extracellularly
Manually annotated by BRENDA team
Penicillium islandicum
-
activity in vivo, intracellularly and extracellularly
Manually annotated by BRENDA team
Sclerotium sp.
-
activity in vivo
Manually annotated by BRENDA team
Paracoccidioides brasiliensis Pb01 ATCC-MYA-826
-
-
-
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
-
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
-, 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
-
germination tests and seed moisture content determination
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
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
A7LP30, -
present in all tissues examined
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; 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
-
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
-
constitutive epression, tissue expression analysis, overview
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
-, 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
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
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
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
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 ACCESSION NO.
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
-
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
-
catalase and bifunctional catalase-peroxidase
Manually annotated by BRENDA team
Bifidobacterium asteroides JCM 8230
-
-
-
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
A9LSF7, A9QNB5, A9QNB6, -
-
Manually annotated by BRENDA team
-, Q8X182
isoform Cat-3 secreted; isoform Cat-3 secreted
-
Manually annotated by BRENDA team
-
enzyme is secreted to the medium
-
Manually annotated by BRENDA team
Penicillium piceum
-
-
-
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
A4QUT2, A4R5S9, -
-
-
Manually annotated by BRENDA team
Bacillus sp. 13, Magnaporthe grisea MA 829
-
-
-
-
Manually annotated by BRENDA team
Penicillium cyclopium 1
-
enzyme is secreted to the medium
-
-
Manually annotated by BRENDA team
Penicillium piceum 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 islandicum, Sclerotium sp.
-
-
Manually annotated by BRENDA team
Magnaporthe grisea MA 829
-
-
-
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
-
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
Beta vulgaris var. cicla
-
-
Manually annotated by BRENDA team
Kloeckera sp.
-
-
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
-
peroxisomal matrix
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)
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
48000
-
-
and 59000, gel filtration
54000
-
Q5LLG6
gel filtration
59000
-
-
and 48000, gel filtration
80000
-
-, Q8X182
;
83170
-
A4QUT2, A4R5S9, -
theoretical molar mass of monomeric KatG1 with one heme b and a His6-tag
84000
-
Q6RSH8
calculated from amino acid sequence
110000
-
-, L8B3D7
about, gel filtration
145000
-
Colwellia sp.
-
native polyacrylamide gel electrophoresis
150000
-
-
native PAGE
150000
-
-
gel filtration
154000
-
-, Q6LA34
gel filtration
160000
-
-
gel filtration
160000
-
A4QUT2, A4R5S9, -
dimeric KatG1, SDS-PAGE
170000
-
-
catalase-peroxidase
170000
-
Pibocella sp.
-
native polyacrylamide gel electrophoresis
175000
-
-
gel filtration
178000
-
-
gel filtration
180000
-
A4QUT2, A4R5S9, -
homodimer, gel filtration; homodimer, gel filtration
183000
-
-
gel filtration
185000
-
Sulfitobacter sp.
-
native polyacrylamide gel electrophoresis
189000
-
-
gel filtration
190000
-
O93662
gel filtration
200000
-
-
gel filtration
204000
-
-
gel filtration
210000
-
-
ultracentrifugation
220000
-
Capra capra
-
gel filtration
223000
-
-
gel filtration
225000
-
-
sucrose density gradient centrifugation
227300
-
-
TvC-II, gel filtration
228000
-
-
gel filtration
230000
-
-
gel filtration
230000
-
-
gel filtration
230000
-
Cucurbita sp.
-
sucrose density gradient centrifugation
230000
-
-
gel filtration
230000
-
D7RJ66, -
gel filtration
234000
-
A3REN3
native enzyme, gel filtration
235000
-
Beta vulgaris var. cicla
-
gel filtration
236000
-
-
gel filtration
240000
-
-
gel filtration
240000
-
Kloeckera sp.
-
gel filtration
240000
-
Q9AQQ9
PAGE