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Literature summary extracted from
- 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 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.11.1.24 | - |
Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.11.1.24 | C45S | mutation results in a complete loss of thiol peroxidase activity | Escherichia coli |
| 1.11.1.24 | C50S | mutant enzyme show about 55% of wild-type activity with H2O2 as substrate | Escherichia coli |
| 1.11.1.24 | C99S | mutant enzyme show about 95% of wild-type activity with H2O2 as substrate | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.11.1.24 | 0.117 | - |
linoleic acid hydroperoxide | pH 7.0, 37°C | Escherichia coli |  |
| 1.11.1.24 | 0.374 | - |
tert-butyl hydroperoxide | pH 7.0, 37°C | Escherichia coli | |
| 1.11.1.24 | 0.478 | - |
H2O2 | pH 7.0, 37°C | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.24 | thioredoxin + linoleic acid hydroperoxide | Escherichia coli | the enzyme defends against oxidative stress through decomposition of hydroperoxide | thioredoxin disulfide + H2O + linoleic acid | - |
? | |
| 1.11.1.24 | thioredoxin + linoleic acid hydroperoxide | Escherichia coli K12 | the enzyme defends against oxidative stress through decomposition of hydroperoxide | thioredoxin disulfide + H2O + linoleic acid | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.11.1.24 | Escherichia coli | P0AE52 | - |
- |
| 1.11.1.24 | Escherichia coli K12 | P0AE52 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.11.1.24 | - |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.24 | thioredoxin + H2O2 | the Vmax/Km value is about 5fold lower than the Vmax/Km value linoleic acid hydroperoxide | Escherichia coli | thioredoxin disulfide + 2 H2O | - |
? | |
| 1.11.1.24 | 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 | - |
? | |
| 1.11.1.24 | thioredoxin + linoleic acid hydroperoxide | - |
Escherichia coli | thioredoxin disulfide + H2O + linoleic acid | - |
? | |
| 1.11.1.24 | thioredoxin + linoleic acid hydroperoxide | the enzyme defends against oxidative stress through decomposition of hydroperoxide | Escherichia coli | thioredoxin disulfide + H2O + linoleic acid | - |
? | |
| 1.11.1.24 | thioredoxin + linoleic acid hydroperoxide | - |
Escherichia coli K12 | thioredoxin disulfide + H2O + linoleic acid | - |
? | |
| 1.11.1.24 | thioredoxin + linoleic acid hydroperoxide | the enzyme defends against oxidative stress through decomposition of hydroperoxide | Escherichia coli K12 | thioredoxin disulfide + H2O + linoleic acid | - |
? | |
| 1.11.1.24 | 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 | - |
? | |
| 1.11.1.24 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.11.1.24 | monomer | - |
Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.11.1.24 | bacterioferritin comigratory protein | - |
Escherichia coli |
| 1.11.1.24 | BCP | - |
Escherichia coli |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.11.1.24 | Escherichia coli | the expression level gradually elevates during exponential growth until mid-log phase growth beyond which the expression level is decreased | down |
| 1.11.1.24 | 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
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.11.1.24 | 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 |
| 1.11.1.24 | physiological function | the enzyme defends against oxidative stress through decomposition of hydroperoxide | Escherichia coli |
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Release 2023.1 (January 2023)
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