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Information on EC 1.11.1.6 - catalase and Organism(s) Bos taurus and UniProt Accession P00432
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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: Bos taurus
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
-
-
-
-
CAT
-
-
-
-
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
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
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
nitrite
nitrite effectively reduces inactive catalase compound II to the ferric enzyme. Presence of chloride significantly enhances nitrite-induced catalase inhibition
NO
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
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
Glutaraldehyde
-
the presence of trace amount of glutaraldehyde in immobilization medium causes the catalase activity to decline
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
additional information
-
enzyme inhibition by flavonoids, structure-function relationship, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sodium arsenate
-
CAT activity is activated by 200 mM arsenate up to 120% compared to the control
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
95.9
H2O2
-
catalase covalently immobilized onto Eupergit C, in 50 mM phosphate buffer pH 7.0, at 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
160
H2O2
-
catalase covalently immobilized onto Eupergit C, in 50 mM phosphate buffer pH 7.0, at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
estimated kinetic parameters for catalase inactivation in various media, kinetic model of inactivation, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme activity at pH 7.0, 23°C, in nonionic micellar and reverse micellar systems, formed by mixing of Brij 30, Brij 35, cyclohexane, decaline, dodecane, n-heptane or isooctane, and water, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
439793, 439807, 439808, 657432, 685295, 687061, 699601, 700795, 712789, 723827, 725146, 725750, 726417
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
catalase form III protein and crystal structure analysis, overview
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). CATA_BOVIN
527
0
59915
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
fee enzyme and enzyme complexed with ammonia or NO, hanging drop vapor diffusion method, mixing of 0.004 ml of 12-13 mg/ml protein, containing NH4OH, with an equal volume of the reservoir solution consisting of 45-60 mM magnesium formate, pH 6.7, 2-3 weeks, soaking of crystals in ligand solutions, X-ray diffraction structure determination and analysis at 1.88-1.99 A resolution
purified catalase form III, sitting drop vapour diffusion method, mixing of 40 mg/ml protein in 0.05 M sodium phosphate, pH 6.8, with reservoir solution containing 12% PEG 4000 and 0.05 M sodium phosphate, pH 6.8, X-ray diffraction structure determination and analysis at 2.69 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme immobilization via precipitation with ammonium sulfate and then crosslinking with glutaraldehyde, method development. The immoblized enzyme shows about 50% of free enzyme activity, its thermal and storage stabilities are improved compared to the free catalase and the remaining activity of immobilized CLEA-CAT-BSA enzyme derivative is 50% of its initial activity at the end of 400 consecutive uses in a batch type-reactor
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
immobilized catalase onto controlled pore glass retains 80% of its maximum activity at pH 9.0, while free catalase retains only 40% of its maximum activity at pH 9.0
699601
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
thermoinactivation kinetics in the presence or absence of substrate H2O2, overview
35 - 50
-
the half-lives of free catalase at 35 and 50°C were 9.0 and 6.7 h, respectively and these correspondingly are 70.0 and 9.7 h for immobilized catalase onto controlled pore glass
37
-
enzyme in homogenous aqueous solution: half-life is 19.0 h, enzyme in aqueous solution with Brij 35: half-life is 17.5 h, enzyme in reverse micelles of 0.1 M Brij 30 in n-heptane: half-life is 14.5 h
40 - 50
-
the half lives of free catalase at 40 and 50°C are 9.0 and 6.7 h, respectively, and correspondingly 29.1 and 4.8 h for Eupergit C-immobilized catalase
50
-
enzyme in homogenous aqueous solution: half-life is 35 min, enzyme in aqueous solution with Brij 35: half-life is 12 min, enzyme in reverse micelles of 0.1 M Brij 30 in n-heptane: half-life is 77 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme stability at 23°C, 37°C or 50°C in nonionic micellar and reverse micellar systems, formed by mixing of Brij 30, Brij 35, cyclohexane, decaline, dodecane, n-heptane or isooctane, and water
-
free and immobilized catalases show their maximum activities at 50 mM buffer concentration. When the buffer concentration is increased from 25 to 100 mM, the activity of Eupergit C-immobilized catalase is more affected than the activity of free catalase. At 100 mM buffer concentration, free catalase retains 96.9% of its maximum activity although immobilized catalase retains 80% of its maximum activity
-
polyethylene glycol and glycol stabilize best, 3-7fold increase in enzyme stability at 30°C, pH 7.0
-
propane-1,2,3-triol is protective against thermoinactivation of the enzyme at 43°C, but less at 55°C
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, immobilized enzyme onto controlled pore glass, 77 days, 74% loss of activity
-
5°C, immobilized enzyme onto controlled pore glass, 77 days, 23% loss of activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
energy production
combination oflaccase and catalase in construction of H2O2-O2 based biocathode for applications in glucose biofuel cells. The deposited enzymes laccase and catalase by means of alternating current electrophoretic deposition (AC-EPD) do not inhibit each other and carry out about 90% of the catalytic reduction process of O2-H2O2
synthesis
synthesis
-
covalent immobilization of catalase on florisil via glutaraldehyde. Optimal immobilization is at pH 6.0, 10°C, leading to a vmax of immobilized enzyme of 20 mM H2O2 per min and mg protein and a 50fold increase in Km value. the immobilized enzyme retains 40% of initial activtiy after 50 uses and is more stable than free enzyme
synthesis
glutathione-mediated superoxide generation in an aqueous solution is increased by presence of catalase. The catalase-exaggerated extracellular superoxide generation may give a harmful effect to living cells
synthesis
improvement of thermal stability, resistance to protease degradation, and resistance to ascorbate inhibition, while retaining enzyme structure and activity, by conjugation to poly(acrylic acid). 55-80% and 90-100% activity is retained for all samples synthesized at pH 5.0 and pH 7.0, respectively, Km or Vmax values do not differ significantly from those of the free enzyme. Conjugates synthesized at pH 7.0 are thermally stable up to 85-90°C, and retain 40-90% of their original activities after storing for 10 weeks at 8°C
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sichak, S.P.; Dounce, A.L.
Analysis of the peroxidatic mode of action of catalase
Arch. Biochem. Biophys.
249
286-295
1986
Bos taurus
Schonbaum, G.R.; Chance, B.
Catalase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
363-408
1976
Bos taurus, Equus caballus, Micrococcus luteus
-
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
Gebicka, L.; Jurgas-Grudzinska, M.
Activity and stability of catalase in nonionic micellar and reverse micellar systems
Z. Naturforsch. C
59
887-891
2004
Bos taurus
Agardh, C.D.; Hultberg, B.; Nayak, R.C.; Farthing-Nayak, P.; Agardh, E.
Bovine retinal pericytes are resistant to glucose-induced oxidative stress in vitro
Antioxid. Redox Signal.
7
1486-1493
2005
Bos taurus
Titov, V.Y.; Petrenko, Y.M.; Vanin, A.F.
Mechanism of inhibition of catalase by nitro and nitroso compounds
Biochemistry
73
92-96
2008
Bos taurus
Ozyilmaz, G.; Tukel, S.S.; Alptekin, O.
Kinetic properties and storage stability of catalase immobilized on to florisil
Indian J. Biochem. Biophys.
44
38-43
2007
Bos taurus
Alptekin, O.; Tuekel, S.; Yildirim, D.; Alagoez, D.
Characterization and properties of catalase immobilized onto controlled pore glass and its application in batch and plug-flow type reactors
J. Mol. Catal. B
58
124-131
2009
Bos taurus
-
Kertulis-Tartar, G.M.; Rathinasabapathi, B.; Ma, L.Q.
Characterization of glutathione reductase and catalase in the fronds of two Pteris ferns upon arsenic exposure
Plant Physiol. Biochem.
47
960-965
2009
Bos taurus, Pteris vittata, Pteris ensiformis
Alptekin, O.; Tuekel, S.; Yildirim, D.; Alagoez, D.
Immobilization of catalase onto Eupergit C and its characterization
J. Mol. Catal. B
64
177-183
2010
Bos taurus
-
Foroughi, L.M.; Kang, Y.N.; Matzger, A.J.
Sixty years from discovery to solution: crystal structure of bovine liver catalase form III
Acta Crystallogr. Sect. D
67
756-762
2011
Bos taurus
Purwar, N.; McGarry, J.M.; Kostera, J.; Pacheco, A.A.; Schmidt, M.
Interaction of nitric oxide with catalase: structural and kinetic analysis
Biochemistry
50
4491-4503
2011
Bos taurus (P00432), Bos taurus
Krych, J.; Gebicka, L.
Catalase is inhibited by flavonoids
Int. J. Biol. Macromol.
58
148-153
2013
Bos taurus
Tuekel, S.; Huerrem, F.; Yildirim, D.; Alptekin, A.
Preparation of crosslinked enzyme aggregates (CLEA) of catalase and its characterization
J. Mol. Catal. B
97
252-257
2013
Bos taurus
-
Cantemir, A.; Raducan, A.; Puiu, M.; Oancea, D.
Kinetics of thermal inactivation of catalase in the presence of additives
Process Biochem.
48
471-477
2013
Bos taurus
-
Riccardi, C.M.; Cole, K.S.; Benson, K.R.; Ward, J.R.; Bassett, K.M.; Zhang, Y.; Zore, O.V.; Stromer, B.; Kasi, R.M.; Kumar, C.V.
Toward "stable-on-the-table" enzymes improving key properties of catalase by covalent conjugation with poly(acrylic acid)
Bioconjug. Chem.
25
1501-1510
2014
Bos taurus (P00432)
Ueno, M.; Sekine-Suzuki, E.; Nyui, M.; Nakanishi, I.; Matsumoto, K.I.
Amplification of glutathione-mediated oxidative stress by catalase in an aqueous solution at hyperthermal temperatures
J. Clin. Biochem. Nutr.
60
93-99
2017
Bos taurus (P00432)
Krych-Madej, J.; Gebicka, L.
Interactions of nitrite with catalase Enzyme activity and reaction kinetics studies
J. Inorg. Biochem.
171
10-17
2017
Bos taurus (P00432)
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