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Information on EC 1.11.1.6 - catalase and Organism(s) Burkholderia cenocepacia and UniProt Accession Q4F6N6

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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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Burkholderia cenocepacia
UNIPROT: Q4F6N6
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The taxonomic range for the selected organisms is: Burkholderia cenocepacia
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, catalase-phenol oxidase, 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
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 6
both catalase and peroxidase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional catalase-peroxidase KatG
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein
97000
x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 97000, SDS-PAGE of mature enzyme, x * 80000, SDS-PAGE of recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Charalabous, P.; Risk, J.M.; Jenkins, R.; Birss, A.J.; Hart, C.A.; Smalley, J.W.
Characterization of a bifunctional catalase-peroxidase of Burkholderia cenocepacia
FEMS Immunol. Med. Microbiol.
50
37-44
2007
Burkholderia cenocepacia (Q4F6N6), Burkholderia cenocepacia
Manually annotated by BRENDA team