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Information on EC 1.11.1.6 - catalase and Organism(s) Paracoccidioides brasiliensis and UniProt Accession Q8X220
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1.11.1.6 catalaseIUBMB Comments
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.
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Word Map
- 1.11.1.6
- dismutase
- sod
- malondialdehyde
- gsh
- ascorbate
- necrosis
-
thiobarbituric
- erythrocyte
- wistar
- endothelial
- xanthine
- glutathione-s-transferase
- artery
- cholesterol
- s-transferase
- caspase-3
-
albino
- chlorophyll
- copper
- heme
- creatinine
- myeloperoxidase
- tnf
-
anti-oxidant
- peroxisomal
- gsh-px
-
tbars
- biotechnology
- streptozotocin
- agriculture
-
ache
- analysis
- comet
- hydroperoxide
-
hepatoprotective
-
nephrotoxicity
-
neuroprotective
-
sacrificed
- mannitol
-
defenses
-
h2o2-induced
- urease
- cadmium
-
alt
- industry
-
hepatotoxicity
- degradation
- ischemia
- diagnostics
- gill
-
pro-oxidant
- synthesis
- alpha-tocopherol
- acetylcholinesterase
-
aquatic
- medicine
-
reperfusion
- polyphenols
- energy production
The taxonomic range for the selected organisms is: Paracoccidioides brasiliensis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
catalase, cat-1, catalase a, manganese catalase, polyethylene glycol-catalase, catalase-1, cat-a, catpo, catalase p, catalase-phenol oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
caperase
-
-
-
-
CAT
-
-
-
-
catalase-peroxidase
-
-
-
-
equilase
-
-
-
-
optidase
-
-
-
-
polyethylene glycol-catalase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
9001-05-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
fungal enzyme interacts with the host, enzyme plays a role in the defense of the organism against oxygen-dependent killing mechanisms
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
specific irreversible inhibitor, complete inhibition at 20 mM
azide
irreversible inhibitor, effective at concentrations less than1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
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
additional information
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
-
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
azide
Paracoccidioides brasiliensis
in 50 mM sodium phosphate buffer, pH 7.8, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1134
after 3.1fold purification, in 50 mM sodium phosphate buffer, pH 7.8, at 37°C
366.6
crude extract, in 50 mM sodium phosphate buffer, pH 7.8, at 37°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 12
the purified CatP is stable and yields similar activity from pH 4.0 to 12.0
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the protein and expression level are reduced during the mycelial saprobic phase compared to the yeast phase of infection
additional information
-
the protein and expression level are reduced during the mycelial saprobic phase compared to the yeast phase of infection
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme contains the peroxisome-PTS-1-targeting signal
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q8X220_PARBR
502
0
56885
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme contains the peroxisome-PTS-1-targeting signal
additional information
-
enzyme contains the peroxisome-PTS-1-targeting signal
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8 - 7.8
approximately 20% activity is observed at pH 3.8 followed by a steady rise of activity as the pH is increased to 7.8 (100% activity)
712318
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
CatP is highly resistant to denaturation by guanidine-HCl. The enzyme conserves activity after 48 h exposure to 1 M guanidine-HCl. Guanidine-HCl at 1.5 M for 48 h decreases the catalase P activity to about 60%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PbcatP, DNA and amino acid sequence determination and analysis, expression analysis, phylogenetic analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CatP presents high levels of expression in the yeast parasitic phase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moreira, S.F.; Bailao, A.M.; Barbosa, M.S.; Jesuino, R.S.; Felipe, M.S.; Pereira, M.; de Almeida Soares, C.M.
Monofunctional catalase P of Paracoccidioides brasiliensis: identification, characterization, molecular cloning and expression analysis
Yeast
21
173-182
2004
Paracoccidioides brasiliensis (Q8X220), Paracoccidioides brasiliensis, Paracoccidioides brasiliensis Pb01 ATCC -MYA-826 (Q8X220)
Chagas, R.F.; Bailao, A.M.; Pereira, M.; Winters, M.S.; Smullian, A.G.; Deepe, G.S.; de Almeida Soares, C.M.
The catalases of Paracoccidioides brasiliensis are differentially regulated: protein activity and transcript analysis
Fungal Genet. Biol.
45
1470-1478
2008
Paracoccidioides brasiliensis (Q6RSH8), Paracoccidioides brasiliensis
Chagas, R.F.; Bailao, A.M.; Fernandes, K.F.; Winters, M.S.; Pereira, M.; Soares, C.M.
Purification of Paracoccidioides brasiliensis catalase P: subsequent kinetic and stability studies
J. Biochem.
147
345-351
2010
Paracoccidioides brasiliensis (Q8X220), Paracoccidioides brasiliensis, Paracoccidioides brasiliensis ATCC MYA-826 (Q8X220)
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