Any feedback?
Literature summary for 1.11.1.18 extracted from
- A useful propionate cofactor enhancing activity for organic solvent-tolerant recombinant metal-free bromoperoxidase (perhydrolase) from Streptomyces aureofaciens (2019), Biochem. Biophys. Res. Commun., 516, 327-332 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 2,2-dimethylpropanoic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| 2-chloropropanoic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| 2-Methylpropanoic acid | acts as a cofactor | Kitasatospora aureofaciens |  |
| 3-chloropropanoic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| acetic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| butanoic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| ethylene glycol | acts as a cofactor, it has a low Log P | Kitasatospora aureofaciens | |
| heptanoic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| hexanoic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| Methoxyacetic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| additional information | the carboxylic acids including hydroxyacetic acid, cyanoacetic acid, bromoacetic acid, chloroacetic acid, dichloroacetic acid, trichloroacetic acid, succinic acid, and malic acid, and amino acids, such as glycine, aspartic acid, glutamic acid, histidine, lysine, and arginine, are inactive as cofactors | Kitasatospora aureofaciens | |
| additional information | the oxidative brominating activity of an organic solvent-tolerant recombinant metal-free bromoperoxidase C-terminally tagged BPO-A1 (rBPO-A1) from Streptomyces aureofaciens depends on various additives. These include carboxylic acids, used as cofactors, and alcohols, used as water-miscible organic solvents. Propanoic acid, 2-methylpropanoic acid, and 1-butanoic acid enhanced rBPO-A1's activity by 13.7, 8.0, and 4.6fold, respectively, compared to that obtained with acetic acid. The decrease in the activity associated with changes from primary to tertiary fatty chains can be attributed to increased steric hindrance. Carboxylic acid binding structure analysis, overview | Kitasatospora aureofaciens | |
| octanoic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| pentanoic acid | acts as a cofactor | Kitasatospora aureofaciens | |
| propanoic acid | acts as a cofactor, it has a high Log D at pH 5.0. The increase in the activity of the enzyme with propanoic acid around 10-50°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br- | Kitasatospora aureofaciens | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene bpo-A1, recombiant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3) | Kitasatospora aureofaciens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| RH + HBr + H2O2 | Kitasatospora aureofaciens | - |
RBr + 2 H2O | - |
? | |
| RH + HBr + H2O2 | Kitasatospora aureofaciens ATCC 10762 | - |
RBr + 2 H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Kitasatospora aureofaciens | P33912 | Streptomyces aureofaciens | - |
| Kitasatospora aureofaciens ATCC 10762 | P33912 | Streptomyces aureofaciens | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombiant His-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by ammonium sulfate fractionation and nickel affinity chromatography followed by desalting gel filtration | Kitasatospora aureofaciens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2.6 | - |
wild-type enzyme, pH 5.0, 25°C, substrates monochlorodimedone and HBr in presence of 1-butanoic acid | Kitasatospora aureofaciens |
| 18.1 | - |
wild-type enzyme, pH 5.0, 25°C, substrates monochlorodimedone and HBr in presence of acetic acid | Kitasatospora aureofaciens |
| 145.8 | - |
wild-type enzyme, pH 5.0, 25°C, substrates monochlorodimedone and HBr in presence of 2-methylpropanoic acid | Kitasatospora aureofaciens |
| 248.6 | - |
wild-type enzyme, pH 5.0, 25°C, substrates monochlorodimedone and HBr in presence of propanoic acid | Kitasatospora aureofaciens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| cyclohexene + HBr + H2O2 | - |
Kitasatospora aureofaciens | ? + 2 H2O | - |
? | |
| cyclohexene + HBr + H2O2 | - |
Kitasatospora aureofaciens ATCC 10762 | ? + 2 H2O | - |
? | |
| indene + HBr + H2O2 | - |
Kitasatospora aureofaciens | ? + 2 H2O | - |
? | |
| indene + HBr + H2O2 | - |
Kitasatospora aureofaciens ATCC 10762 | ? + 2 H2O | - |
? | |
| monochlorodimedone + HBr + H2O2 | the monochlorodimedone stable enol form exists as an enolic anion without the ketoic isomer at reaction pH 5.0 | Kitasatospora aureofaciens | monobromomonochlorodimenone + 2 H2O | - |
? | |
| monochlorodimedone + HBr + H2O2 | the monochlorodimedone stable enol form exists as an enolic anion without the ketoic isomer at reaction pH 5.0 | Kitasatospora aureofaciens ATCC 10762 | monobromomonochlorodimenone + 2 H2O | - |
? | |
| additional information | positional specificity of oxidative hydroxybromination for olefins, using rBPO-A1 and PA in the presence of methanol, is higher compared to a non-enzymatic reaction using peracetic acid. The oxidative bromination step, occurring after the enzymatic peroxidation step, is suggested to be pseudoenzymatic. Non-enzymatic oxidative bromination's influence can be disregarded under acidic condition of pH 6.0 or lower because generation of a strongly brominating active species is not the rate-limiting step under acidic conditions | Kitasatospora aureofaciens | ? | - |
- |
|
| additional information | positional specificity of oxidative hydroxybromination for olefins, using rBPO-A1 and PA in the presence of methanol, is higher compared to a non-enzymatic reaction using peracetic acid. The oxidative bromination step, occurring after the enzymatic peroxidation step, is suggested to be pseudoenzymatic. Non-enzymatic oxidative bromination's influence can be disregarded under acidic condition of pH 6.0 or lower because generation of a strongly brominating active species is not the rate-limiting step under acidic conditions | Kitasatospora aureofaciens ATCC 10762 | ? | - |
- |
|
| nerol + HBr + H2O2 | - |
Kitasatospora aureofaciens | ? + 2 H2O | - |
? | |
| RH + HBr + H2O2 | - |
Kitasatospora aureofaciens | RBr + 2 H2O | - |
? | |
| RH + HBr + H2O2 | - |
Kitasatospora aureofaciens ATCC 10762 | RBr + 2 H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| BPO-A1 | - |
Kitasatospora aureofaciens |
| bpoA1 | UniProt | Kitasatospora aureofaciens |
| bromoperoxidase | - |
Kitasatospora aureofaciens |
| metal-free bromoperoxidase | - |
Kitasatospora aureofaciens |
| perhydrolase | - |
Kitasatospora aureofaciens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
recombinant enzyme | Kitasatospora aureofaciens |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 80 | reaction activity in the presence of recombinant BPO-A1 peaks at 60°C whereas peak in the non-enzymatic activity of H2O2 is not observed in temperature range of 10-70°C. The increase in the activity of the enzyme with propanoic acid around 10-50°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br-. The active species is heat-labile. The significant decrease in activity around 65-70°C is attributed to decomposition of the active species | Kitasatospora aureofaciens |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 10 | 80 | reaction activity in the presence of recombinant BPO-A1 peaks at 60°C whereas peak in the non-enzymatic activity of H2O2 is not observed in temperature range of 10-70°C. The increase in the activity of the enzyme with propanoic acid around 10-50°C is due to the peroxidation step because high activity in the nonenzymatic oxidative bromination step is maintained at low temperature, which suppresses the decomposition of the active species generated by the reaction between peracid and Br-. The active species is heat-labile. The significant decrease in activity around 65-70°C is attributed to decomposition of the active species. The native BPO-A1 possesses high stability up to 80°C. Recombinant BPO-A1 possesses high peroxidating activity at high temperatures | Kitasatospora aureofaciens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
assay at | Kitasatospora aureofaciens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | a non-heme enzyme | Kitasatospora aureofaciens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
