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Literature summary for 1.1.3.B5 extracted from
- A xylenol orange-based screening assay for the substrate specificity of flavin-dependent para-phenol oxidases (2018), Molecules, 23, 164 .
Application
| Application | Comment | Organism |
|---|---|---|
| analysis | development of a screening assay for the substrate specificity of para-phenol oxidases based on the detection of hydrogen peroxide using the ferric-xylenol orange complex method | Rhodococcus jostii |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Rhodococcus jostii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G392F | mutant does not display measurable activity | Rhodococcus jostii |
| I427T | mutant does not display measurable activity | Rhodococcus jostii |
| L381W | mutant does not display measurable activity | Rhodococcus jostii |
| L438C | variant displays lowered activity towards all substrates as compared to wild-type | Rhodococcus jostii |
| M282L | substrate specificity profile is similar to wild-type | Rhodococcus jostii |
| Q425T | display similar activity to the wild-type enzyme with vanillyl alcohol, but no measurable activity towards any other substrate | Rhodococcus jostii |
| V436I | variant displays lowered activity towards vanillyl alcohol and eugenol | Rhodococcus jostii |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.047 | - |
Vanillyl alcohol | His-tagged recombinant enzyme, pH 7.5, 25°C | Rhodococcus jostii |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodococcus jostii | Q0SBK1 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-cyclohexylphenol + O2 | - |
Rhodococcus jostii | ? | - |
? | |
| 4-cyclopentylphenol + O2 | - |
Rhodococcus jostii | 4-(1-cyclopenten-1-yl)phenol | - |
? | |
| eugenol + O2 + H2O | - |
Rhodococcus jostii | coniferyl alcohol + H2O2 | - |
? | |
| additional information | EUGO displays a somewhat narrower substrate specificity than vanillyl-alcohol oxidase, EC 1.1.3.38. Although alcohols and 4-allylphenols are good substrates for the enzyme, 4-alkylphenols and ethers are hardly accepted | Rhodococcus jostii | ? | - |
- |
|
| vanillyl alcohol + O2 | - |
Rhodococcus jostii | vanillin + H2O2 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EUGO | - |
Rhodococcus jostii |
| RHA1_ro03282 | - |
Rhodococcus jostii |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.7 | - |
4-cyclopentylphenol | His-tagged recombinant enzyme, pH 7.5, 25°C | Rhodococcus jostii | |
| 8 | - |
Vanillyl alcohol | His-tagged recombinant enzyme, pH 7.5, 25°C | Rhodococcus jostii | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 170 | - |
Vanillyl alcohol | His-tagged recombinant enzyme, pH 7.5, 25°C | Rhodococcus jostii | |
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Release 2023.1 (January 2023)
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