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Information on EC 1.11.1.6 - catalase and Organism(s) Homo sapiens and UniProt Accession P04040

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.6 catalase
IUBMB 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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Homo sapiens
UNIPROT: P04040
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
2
=
+
2
2
=
+
2
Synonyms
catalase, cat-1, catalase a, manganese catalase, polyethylene glycol-catalase, catalase-1, cat-a, catpo, catalase p, catalase-phenol oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
caperase
-
-
-
-
catalase-peroxidase
-
-
-
-
equilase
-
-
-
-
H2O2:H2O2 oxidoreductase
-
-
optidase
-
-
-
-
polyethylene glycol-catalase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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 hide
9001-05-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
show the reaction diagram
-
-
-
?
ethanol + H2O2
acetaldehyde + ?
show the reaction diagram
formic acid + H2O2
?
show the reaction diagram
-
-
-
?
H2O2
O2 + H2O
show the reaction diagram
methanol + H2O2
formaldehyde + ?
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
H2O2
O2 + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one
-
-
2-mercaptoethanol
-
-
3-Amino-1,2,4-triazole
3-amino-1H-1,2,4-triazole
acetic acid
-
in vitro inhibitor
ascorbate
-
in vitro inhibitor
azide
-
very strong inhibitor of erythrocytic CAT but a relatively weak CAT inhibitor in human hemolysates
BrCN
-
acting in vitro
CAS 1609
-
-
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
ethanol
-
in vitro inhibitor
F-
-
in vitro inhibitor
formic acid
-
in vitro inhibitor
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
glycerol trinitrate
-
-
H2O2
-
rapid inactivation above 0.1 M
hydroxylamine
isosorbide dinitrate
-
-
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
methanol
-
in vitro inhibitor
NaCN
-
50% inhibition at 20 mM
nitrite
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
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
-
-
pyocyanin
-
may decrease cellular catalase activity via both transcriptional regulation and direct inactivation of the enzyme
S-nitrosoglutathione
-
-
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
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
progesterone receptor isoform B
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80
H2O2
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
3-Amino-1,2,4-triazole
Homo sapiens
-
erythrocytic CAT, at 25°C, pH not specified in the publication
0.0000002 - 0.009
azide
0.009 - 0.75
nitrite
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.5
-
about, cell lysates of wild-type Caco-2 cells
273800
-
-
6
-
about, cell lysates of Caco-2 cells recombinantly overexpressing IGFBP-2
77.5
-
about, cell lysates of wild-type and recombinantly IGFBP-2-overexpressing 293 cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7.5
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 37
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
catalase activity is significantly higher in patients with renal cell carcinoma than in controls
Manually annotated by BRENDA team
fetal liver
Manually annotated by BRENDA team
-
epithelial cell
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
-
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
-
293 cell
Manually annotated by BRENDA team
-
overexpression of hepatitis C virus non-structural proteins increases catalase activity
Manually annotated by BRENDA team
-
clone T-47DN5
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
erythrocytes
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
-
mainly in liver and kidney
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CATA_HUMAN
527
0
59756
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
x * 60000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 60000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
half-life: 12 s
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C, intact erythrocytes or concentrated hemolysates, 6 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
expressed in in MCF-7, Caco-2, and Hct-116 cells, catalase overexpression is associated with increased sensitivity to tisse necrosis facor-alpha
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
progesterone (0.1 mM) induces catalase activities in T47-D cells, Org2058 (0.1 mM) induces catalase activities in T47-D cells and HBE cells after 48 h of treatment, norethisterone acetate (0.001 mM) induces catalase activities in T47-D cells, tibolone (0.001 mM) induces catalase activities in T47-D cells and HBE cells after 48 h of treatment
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
catalase activity is significantly higher in patients with renal cell carcinoma than in controls. The marker catalase might be potentially important as an additional biochemical tool for diagnosing renal cell carcinoma
medicine
design and production of a bifunctional protein with mitochondrial superoxide dismutase and catalase activities plus cell penetrating peptide from HIV-1 Tat to enable cellular internalization. Coexpression of catalase-superoxide dismutase and superoxide dismutase -Tat fusion genes allows simultaneous self-assembly of the protein sequences. The protein complex is expected to contain one tetrameric structure of catalase, four tetrameric structures of superoxide dismutase and twelve units of Tat. The complex shows cellular internalization and superior protection against paraquat-induced cell death
synthesis
method for large-scale expression and purification of recombinant catalase in Pichia pastoris
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Aebi, H.E.
Catalase in vitro
Methods Enzymol.
105
121-126
1984
Homo sapiens
Manually annotated by BRENDA team
Aebi, H.E.
Catalase. Hydrogen-peroxide:hydrogen-peroxide oxidoreductase E.C. 1.11.1.6
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
3
373-386
1983
Homo sapiens
-
Manually annotated by BRENDA team
Switala, J.; Loewen, P.C.
Diversity of properties among catalases
Arch. Biochem. Biophys.
401
145-154
2002
Aspergillus niger, Bacteroides fragilis, Bordetella pertussis, Bos taurus, Saccharomyces cerevisiae, Brucella abortus, Escherichia coli, Helicobacter pylori, Homo sapiens, Listeria seeligeri, Micrococcus luteus, Proteus mirabilis, Pseudomonas aeruginosa, Pseudomonas syringae, Serratia marcescens, Xanthomonas campestris
Manually annotated by BRENDA team
Hoeflich, A.; Fettscher, O.; Preta, G.; Lahm, H.; Kolb, H.J.; Wolf, E.; Weber, M.M.
Increased activity of catalase in tumor cells overexpressing IGFBP-2
Horm. Metab. Res.
35
816-821
2003
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
O'Malley, Y.Q.; Reszka, K.J.; Rasmussen, G.T.; Abdalla, M.Y.; Denning, G.M.; Britigan, B.E.
The Pseudomonas secretory product pyocyanin inhibits catalase activity in human lung epithelial cells
Am. J. Physiol.
285
L1077-1086
2003
Homo sapiens
Manually annotated by BRENDA team
Ahamed, M.; Verma, S.; Kumar, A.; Siddiqui, M.K.J.
Delta-aminolevulinic acid dehydratase inhibition and oxidative stress in relation to blood lead among urban adolescents
Hum. Exp. Toxicol.
25
547-553
2006
Homo sapiens
Manually annotated by BRENDA team
Abraham, S.; Soundararajan, C.C.; Vivekanandhan, S.; Behari, M.
Erythrocyte antioxidant enzymes in Parkinsons disease
Indian J. Med. Res.
121
111-115
2005
Homo sapiens
Manually annotated by BRENDA team
Abdalla, M.Y.; Ahmad, I.M.; Spitz, D.R.; Schmidt, W.N.; Britigan, R.E.
Hepatitis C virus-core and non structural proteins lead to different effects on cellular antioxidant defenses
J. Med. Virol.
76
489-497
2005
Homo sapiens
Manually annotated by BRENDA team
Arican, O.; Kurutas, B.; Sasmaz, S.
Oxidative stress in patients with acne vulgaris
Mediators Inflamm.
2005
380-384
2005
Homo sapiens
Manually annotated by BRENDA team
Arima, Y.; Nishigori, C.; Takeuchi, T.; Oka, S.; Morimoto, K.; Utani, A.; Miyachi, Y.
4-Nitroquinoline 1-oxide forms 8-hydroxydeoxyguanosine in human fibroblasts through reactive oxygen species
Toxicol. SCi.
91
382-392
2006
Homo sapiens
Manually annotated by BRENDA team
Herve-Grepinet, V.; Veillard, F.; Godat, E.; Heuze-Vourch, N.; Lecaille, F.; Lalmanach, G.
Extracellular catalase activity protects cysteine cathepsins from inactivation by hydrogen peroxide
FEBS Lett.
582
1307-1312
2008
Homo sapiens
Manually annotated by BRENDA team
Shi, X.L.; Feng, M.Q.; Shi, J.; Shi, Z.H.; Zhong, J.; Zhou, P.
High-level expression and purification of recombinant human catalase in Pichia pastoris
Protein Expr. Purif.
54
24-29
2007
Homo sapiens (P04040), Homo sapiens
Manually annotated by BRENDA team
Azevedo-Martins, A.; Curi, R.
Fatty acids decrease catalase activity in human leukaemia cell lines
Cell Biochem. Funct.
26
87-94
2008
Homo sapiens
Manually annotated by BRENDA team
Luepertz, R.; Chovolou, Y.; Kampoetter, A.; Waetjen, W.; Kahl, R.
Catalase overexpression impairs TNF-alpha induced NF-kappaB activation and sensitizes MCF-7 cells against TNF-alpha
J. Cell. Biochem.
103
1497-1511
2008
Homo sapiens
Manually annotated by BRENDA team
Petit, E.; Courtin, A.; Kloosterboer, H.J.; Rostene, W.; Forgez, P.; Gompel, A.
Progestins induce catalase activities in breast cancer cells through PRB isoform: correlation with cell growth inhibition
J. Steroid Biochem. Mol. Biol.
115
153-160
2009
Homo sapiens
Manually annotated by BRENDA team
Coe, E.; Schimmer, A.D.
Catalase activity and arsenic sensitivity in acute leukemia
Leuk. Lymphoma
49
1976-1981
2008
Homo sapiens
Manually annotated by BRENDA team
Boehmer, A.; Jordan, J.; Tsikas, D.
High-performance liquid chromatography ultraviolet assay for human erythrocytic catalase activity by measuring glutathione as o-phthalaldehyde derivative
Anal. Biochem.
410
296-303
2011
Homo sapiens
Manually annotated by BRENDA team
Luangwattananun, P.; Yainoy, S.; Eiamphungporn, W.; Songtawee, N.; Buelow, L.; Ayudhya, C.I.; Prachayasittikul, V.
Engineering of a novel tri-functional enzyme with MnSOD, catalase and cell-permeable activities
Int. J. Biol. Macromol.
85
451-459
2016
Homo sapiens (P04040)
Manually annotated by BRENDA team
Pirincci, N.; Kaya, T.Y.; Kaba, M.; Ozan, T.; Gecit, I.; Oezveren, H.; Eren, H.; Ceylan, K.
Serum adenosine deaminase, catalase, and carbonic anhydrase activities in patients with renal cell carcinoma
Redox Rep.
22
252-256
2017
Homo sapiens (P04040), Homo sapiens
Manually annotated by BRENDA team