Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.6 extracted from

  • Varnado, C.L.; Hertwig, K.M.; Thomas, R.; Roberts, J.K.; Goodwin, D.C.
    Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7 (2004), Arch. Biochem. Biophys., 421, 166-174.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene katP, expression of wild-type and mutant enzymes in strain XL-1 Blue and as His-tagged proteins in BL21(DE3) Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information stopped-flow kinetics, 25°C, pH 7.0 Escherichia coli
3
-
H2O2 peroxidase activity, pH 7.0, 25°C Escherichia coli
27
-
H2O2 catalase activity, pH 7.0, 25°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme contains heme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene katP
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information enzyme contains an N-terminal signal peptide comprising residues 24-38, clevage site is between residues 23 and 24 Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from strain BL21(DE3) by nickel affinity chromatography Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

Synonyms

Synonyms Comment Organism
catalase-peroxidase
-
Escherichia coli
KatP
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
18000
-
H2O2 catalase activity, pH 7.0, 22°C Escherichia coli
26000
-
H2O2 peroxidase activity, pH 7.0, 22°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
aasay at, peroxidase activity Escherichia coli
7
-
assay at, catalase activity Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
4 6 peroxidase activity Escherichia coli
6 8 catalase activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme
-
Escherichia coli