Any feedback?
Literature summary for 1.14.13.92 extracted from
- Towards practical biocatalytic Baeyer-Villiger reactions: applying a thermostable enzyme in the gram-scale synthesis of optically active lactones in a two-liquid-phase system (2005), Beilstein J. Org. Chem., 1, 10.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the thermally stable phenylacetone monooxygenase and engineered mutants can be used as a practical catalysts for enantioselective Baeyer-Villiger oxidations of several ketones on a preparative scale under in vitro conditions, overview | Thermobifida fusca |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | engineering of three highly stereoselective mutants of the thermally stable phenylacetone monooxygenase as practical catalysts for enantioselective Baeyer-Villiger oxidations of several ketones on a preparative scale under in vitro conditions, optimization of the method including a coupled cofactor-regeneration system, reaction mechanism, overview | Thermobifida fusca |
General Stability
| General Stability | Organism |
|---|---|
| detergents stabilize the enzyme, best by Tween-20 at 0.1% v/v | Thermobifida fusca |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| 2-pentanol | as a sacrificial substrate | Thermobifida fusca |
| cyclohexane | stabilizes the enzyme, best organic solvent, inactivation of the enzyme within 5 min | Thermobifida fusca |
| isopropanol | the most effective stoichiometric sacrificial electron donor, optimal at 5% v/v | Thermobifida fusca |
| methyl tert-butyl ether | stabilizes the enzyme, inactivation of the enzyme within below 5 min | Thermobifida fusca |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermobifida fusca | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
catalytic efficiency of wild-type and mutant PAMO in in vitro catalysis with two-liquid phases, overview | Thermobifida fusca |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| rac-bicyclo [3.2.0]hept-2-en-6-one + NADPH + O2 | activity and stereoselectivity of wild-type and mutant enzymes, overview | Thermobifida fusca | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PAMO | - |
Thermobifida fusca |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
assay at | Thermobifida fusca |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Thermobifida fusca |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | - |
Thermobifida fusca | |
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
