Cloned (Comment) | Organism |
---|---|
gene adh | Thermoanaerobacter brockii |
Protein Variants | Comment | Organism |
---|---|---|
additional information | replacement of the zinc from Thermoanaerobacter brockii alcohol dehydrogenase (TbADH) with Rh(III) catalysts possessing nitrogen donor ligands, by covalent conjugation to the active site cysteine, to create artificial metalloenzymes for NADP+ reduction. TbADH is used as protein scaffold for both alcohol synthesis and the recycling of the cofactor, by combination of the chemically modified species with the non-modified recombinant enzyme. Stability studies reveal that the incorporation of the catalysts into the TbADH pocket provides a shielding environment for the metal catalyst, resulting in increased stability of both the recycling catalyst and the ADH. The reduction of a representative ketone using this modified alcohol dehydrogenase-artificial formate dehydrogenase cascade yields better conversions than in the presence of free metal catalyst | Thermoanaerobacter brockii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | replacement of the zinc from Thermoanaerobacter brockii alcohol dehydrogenase (TbADH) with Rh(III) catalysts possessing nitrogen donor ligands, by covalent conjugation to the active site cysteine, to create artificial metalloenzymes for NADP+ reduction. Compatibility between bioconjugated Rh catalysts and TbADH, overview. Formate dehydrogenase activity of artificial brominated metalloenzymes is observed | Thermoanaerobacter brockii | |
Zn2+ | required, analysis of the zion ion bound in the crystal structure of TbADH complexed to NADP+ (PDB ID 1YKF) | Thermoanaerobacter brockii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermoanaerobacter brockii | P14941 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-butanone + NADPH + H+ | - |
Thermoanaerobacter brockii | 2-butanol + NADP+ | - |
r | |
4-phenyl-2-butanone + NADPH + H+ | - |
Thermoanaerobacter brockii | 4-phenyl-2-butanol + NADP+ | - |
r |
Synonyms | Comment | Organism |
---|---|---|
NADP-dependent isopropanol dehydrogenase | UniProt | Thermoanaerobacter brockii |
TBADH | - |
Thermoanaerobacter brockii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
assay at | Thermoanaerobacter brockii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Thermoanaerobacter brockii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Thermoanaerobacter brockii | |
NADPH | - |
Thermoanaerobacter brockii |
General Information | Comment | Organism |
---|---|---|
additional information | replacment of the zinc from Thermoanaerobacter brockii alcohol dehydrogenase (TbADH) with Rh(III) catalysts possessing nitrogen donor ligands, by covalent conjugation to the active site cysteine, to create artificial metalloenzymes for NADP+ reduction. TbADH is used as protein scaffold for both alcohol synthesis and the recycling of the cofactor, by combination of the chemically modified species with the non-modified recombinant enzyme. Stability studies reveal that the incorporation of the catalysts into the TbADH pocket provides a shielding environment for the metal catalyst, resulting in increased stability of both the recycling catalyst and the ADH. The reduction of a representative ketone using this modified alcohol dehydrogenase-artificial formate dehydrogenase cascade yields better conversions than in the presence of free metal catalyst. Active site residues are H59 and D150, engineering of TbADH for the covalent binding of small molecules into the active site. Reduction of a model ketone using a native-artificial enzyme cascade with the same alcohol dehydrogenase scaffold, modeling, overview | Thermoanaerobacter brockii |