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Literature summary for 1.1.1.80 extracted from

  • Morra, S.; Pordea, A.
    Biocatalyst-artificial metalloenzyme cascade based on alcohol dehydrogenase (2018), Chem. Sci., 9, 7447-7454 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene adh Thermoanaerobacter brockii

Protein Variants

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

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

Organism UniProt Comment Textmining
Thermoanaerobacter brockii P14941
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
NADP-dependent isopropanol dehydrogenase UniProt Thermoanaerobacter brockii
TBADH
-
Thermoanaerobacter brockii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
assay at Thermoanaerobacter brockii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Thermoanaerobacter brockii

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Thermoanaerobacter brockii
NADPH
-
Thermoanaerobacter brockii

General Information

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