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Literature summary for 1.11.1.24 extracted from

  • Jeong, W.; Cha, M.K.; Kim, I.H.
    Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family (2000), J. Biol. Chem., 275, 2924-2930 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
C45S mutation results in a complete loss of thiol peroxidase activity Escherichia coli
C50S mutant enzyme show about 55% of wild-type activity with H2O2 as substrate Escherichia coli
C99S mutant enzyme show about 95% of wild-type activity with H2O2 as substrate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.117
-
linoleic acid hydroperoxide pH 7.0, 37°C Escherichia coli
0.374
-
tert-butyl hydroperoxide pH 7.0, 37°C Escherichia coli
0.478
-
H2O2 pH 7.0, 37°C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
thioredoxin + linoleic acid hydroperoxide Escherichia coli the enzyme defends against oxidative stress through decomposition of hydroperoxide thioredoxin disulfide + H2O + linoleic acid
-
?
thioredoxin + linoleic acid hydroperoxide Escherichia coli K12 the enzyme defends against oxidative stress through decomposition of hydroperoxide thioredoxin disulfide + H2O + linoleic acid
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AE52
-
-
Escherichia coli K12 P0AE52
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
thioredoxin + H2O2 the Vmax/Km value is about 5fold lower than the Vmax/Km value linoleic acid hydroperoxide Escherichia coli thioredoxin disulfide + 2 H2O
-
?
thioredoxin + H2O2 the Vmax/Km value is about 5fold lower than the Vmax/Km value linoleic acid hydroperoxide Escherichia coli K12 thioredoxin disulfide + 2 H2O
-
?
thioredoxin + linoleic acid hydroperoxide
-
Escherichia coli thioredoxin disulfide + H2O + linoleic acid
-
?
thioredoxin + linoleic acid hydroperoxide the enzyme defends against oxidative stress through decomposition of hydroperoxide Escherichia coli thioredoxin disulfide + H2O + linoleic acid
-
?
thioredoxin + linoleic acid hydroperoxide
-
Escherichia coli K12 thioredoxin disulfide + H2O + linoleic acid
-
?
thioredoxin + linoleic acid hydroperoxide the enzyme defends against oxidative stress through decomposition of hydroperoxide Escherichia coli K12 thioredoxin disulfide + H2O + linoleic acid
-
?
thioredoxin + tert-butyl hydroperoxide the Vmax/Km value is about 14fold lower than the Vmax/Km value linoleic acid hydroperoxide Escherichia coli thioredoxin disulfide + H2O + tert-butyl alcohol
-
?
thioredoxin + tert-butyl hydroperoxide the Vmax/Km value is about 14fold lower than the Vmax/Km value linoleic acid hydroperoxide Escherichia coli K12 thioredoxin disulfide + H2O + tert-butyl alcohol
-
?

Subunits

Subunits Comment Organism
monomer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
bacterioferritin comigratory protein
-
Escherichia coli
BCP
-
Escherichia coli

Expression

Organism Comment Expression
Escherichia coli the expression level gradually elevates during exponential growth until mid-log phase growth beyond which the expression level is decreased down
Escherichia coli the expression level gradually elevates during exponential growth until mid-log phase growth. The enzyme (BCP) is induced 3fold by the oxidative stress given by changing the growth conditions from the anaerobic to aerobic culture up

General Information

General Information Comment Organism
malfunction Bcp null mutant grows more slowly than its wild type in aerobic culture and shows the hypersensitivity toward various oxidants such as H2O2, tert-butyl hydroperoxide, and linoleic acid hydroperoxide Escherichia coli
physiological function the enzyme defends against oxidative stress through decomposition of hydroperoxide Escherichia coli