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Information on EC 1.11.1.6 - catalase and Organism(s) Proteus mirabilis and UniProt Accession P42321

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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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This record set is specific for:
Proteus mirabilis
UNIPROT: P42321
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Word Map
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The taxonomic range for the selected organisms is: Proteus mirabilis
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
-
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
-
-
-
?
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
heme
-
heme b
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
3-amino-1H-1,2,4-triazole
-
-
hydroxylamine
-
-
NaCN
-
50% inhibition at 80 mM
additional information
-
detailed comparison of inhibitors
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
537
H2O2
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CATA_PROMI
484
0
55614
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison with catalase from Aliivibrio salmonicida LFI1238. In Aliivibrio salmonicida, the major channel leading to the catalytically essential heme group, is locally more flexible and slightly wider, explaining its enhanced catalytic efficiency. Compared with Proteus mirabilis, the four C-terminal alpha-helices of Aliivibrio salmonicida LFI1238 catalase are displaced in the structures, explaining the reduced thermal stability
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
half-life: 14 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity, chromatography techniques
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Riise, E.K.; Lorentzen, M.S.; Helland, R.; Smalas, A.O.; Leiros, H.K.; Willassen, N.P.
The first structure of a cold-active catalase from Vibrio salmonicida at 1.96 A reveals structural aspects of cold adaptation
Acta Crystallogr. Sect. D
63
135-148
2007
Proteus mirabilis (P42321), Proteus mirabilis, Aliivibrio salmonicida LFI1238 (Q3LSM1)
Manually annotated by BRENDA team