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Information on EC 1.11.1.6 - catalase and Organism(s) Neurospora crassa and UniProt Accession Q8X182

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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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Neurospora crassa
UNIPROT: Q8X182
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The taxonomic range for the selected organisms is: Neurospora crassa
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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2
H2O2
=
O2
+
2
H2O
2
=
+
2
Synonyms
catalase, cat-1, catalase a, manganese catalase, polyethylene glycol-catalase, catalase-1, cat-a, catpo, catalase p, haem catalase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
caperase
-
-
-
-
CAT
-
-
-
-
catalase-peroxidase
-
-
-
-
equilase
-
-
-
-
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
two monofunctional catalases, Cat-1 and Cat-3, one catalase-peroxidase enzyme, Cat-2
-
?
3,3'-diaminobenzidine + H2O2
? + H2O
show the reaction diagram
isoform Cat-2
-
?
ascorbate + H2O2
? + H2O
show the reaction diagram
isoform Cat-2
-
?
H2O2
O2 + H2O
show the reaction diagram
o-dianisidine + H2O2
? + H2O
show the reaction diagram
isoform Cat-2
-
?
o-methoxyphenol + H2O2
? + H2O
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
two monofunctional catalases, Cat-1 and Cat-3, one catalase-peroxidase enzyme, Cat-2
-
?
H2O2
O2 + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
all isoforms have chlorine instead of ferro-protoheme IX at the active site
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
less than 0.2 g-atom cupper per mol enzyme
Iron
-
3.4 g-atom iron per mol enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-amino-1H-1,2,4-triazole
50% inactivation in 1 h
hydroxyl radicals
inactivation of isoform Cat-1
KNO2
-
37% inhibition at 1 mM
KNO3
-
14% inhibition at 1 mM
NaN3
-
98% inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025 - 13
H2O2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
125000
H2O2
isoform Cat-2
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.168
KCN
Neurospora crassa
isoform Cat-2, IC50: 0.146 mM, catalase activity, IC50: 0.168 mM, peroxidase activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130
isoform Cat-2, peroxidase activity with 3,3-diaminobenzidine
1300
isoform Cat-2, peroxidase activity with guaiacol
1600
isoform Cat-2, peroxidase activity with o-dianisidine
470
isoform Cat-2, peroxidase activity with ascorbate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.75
isoform Cat-2, peroxidase activity
6.25
isoform Cat-2, catalase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
activity within
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Cat-2
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoform Cat-1 mainly present
Manually annotated by BRENDA team
isoform Cat-3 mainly present
Manually annotated by BRENDA team
isoform Cat-1 mainly present
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isoform Cat-3 secreted
-
Manually annotated by BRENDA team
isoform Cat-3 secreted
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
320000
-
sedimentation equilibrium analysis, gel filtration
85000
-
4 * 85000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 80000, isoforms Cat-1, Cat-3
homotetramer
x-ray crystallography
monomer
1 * 80000, isoforms Cat-1, Cat-3
tetramer
-
4 * 85000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
2-4% carbohydrate content
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
inactivation below
439803
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
isoform Cat-1, half-life: 70 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
isoform Cat-1, very stable for months, resistant to denaturizing agents such as urea or guanidine-HCl
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidation by singlet oxygen
439772
oxidation by singlet oxygen
439772
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoforms Cat-1, Cat-2, Cat-3
to homogeneity, chromatography techniques
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Peraza, L.; Hansberg, W.
Neurospora crassa catalases, singlet oxygen and cell differentiation
Biol. Chem.
383
569-575
2002
Aspergillus nidulans, Neurospora crassa, Neurospora crassa (Q8X182)
Manually annotated by BRENDA team
Jacob, G.S.; Orme-Johnson, W.H.
Catalase of Neurospora crassa. 1. Induction, purification, and physical properties
Biochemistry
18
2967-2974
1979
Neurospora crassa
Manually annotated by BRENDA team
Jacob, G.S.; Orme-Johnson, W.H.
Catalase of Neurospora crassa. 2. Electron paramagnetic resonance and chemical properties of the prosthetic group
Biochemistry
18
2975-2980
1979
Neurospora crassa
Manually annotated by BRENDA team
Dominguez, L.; Sosa-Peinado, A.; Hansberg, W.
Catalase evolved to concentrate H2O2 at its active site
Arch. Biochem. Biophys.
500
82-91
2010
Neurospora crassa (Q9C168), Neurospora crassa
Manually annotated by BRENDA team