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Information on EC 1.11.1.21 - catalase-peroxidase and Organism(s) Caulobacter vibrioides and UniProt Accession O31066

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EC Tree
     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.21 catalase-peroxidase
IUBMB Comments
Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
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Caulobacter vibrioides
UNIPROT: O31066
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The taxonomic range for the selected organisms is: Caulobacter vibrioides
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide
donor
+
H2O2
=
oxidized donor
+
2
H2O
+
=
+
2
2
H2O2
=
O2
+
2
H2O
2
=
+
2
Synonyms
catalase-peroxidase, catalase peroxidase, catalase/peroxidase, hydroperoxidase i, katg2, katx2, katg1, fvcp01, fvcp02, fesod a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
catalase-peroxidase
-
-
SYSTEMATIC NAME
IUBMB Comments
donor:hydrogen-peroxide oxidoreductase
Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
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
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
show the reaction diagram
-
-
-
?
H2O2
O2 + 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
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the null katG mutation has little effect on the growth rate in the absence of added H2O2. However, growth inhibition is evident with low levels of exogenous H2O2
physiological function
the catalatic and/or peroxidatic activity of KatG is important in reducing H2O2 concentration to a steady-state level compatible with sustained exponential growth. Catalase-peroxidase clearly plays a critical role in stationary-phase survival
malfunction
-
catalase-peroxidase activity is decreased in a Caulobacter crescentus rho::TN5 mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli DH5alpha cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the katG gene is induced by hydrogen peroxide, KatG activity is constant throughout exponential growth and is induced 50fold in the stationary phase
the KatG catalase activity of the rho mutant strain is drastically decreased
-
transcription of the KatG gene is increased in the rho::Tn5 mutant
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Italiani, V.C.; Braz, V.S.; Xiao, H.; Steinman, H.M.; Marques, M.V.
Catalase-peroxidase activity is decreased in a Caulobacter crescentus rho mutant
FEMS Microbiol. Lett.
303
48-54
2010
Caulobacter vibrioides
Manually annotated by BRENDA team
Steinman, H.M.; Fareed, F.; Weinstein, L.
Catalase-peroxidase of Caulobacter crescentus: function and role in stationary-phase survival
J. Bacteriol.
179
6831-6836
1997
Caulobacter vibrioides (O31066), Caulobacter vibrioides
Manually annotated by BRENDA team