possibly takes part in the further metabolic reactions of the fragments formed from the side-chain of the steroid hormone precursor in the adrenals or gonads
enzyme transfers the pro-R hydrogen from the pyridine 4 position of the reduced coenzyme. This stereospecificity is stable over a broad range of temperatures up to 70°C and different concentrations of the coenzyme (catalytic or stoichiometric). NADP+ and its synthetic analogs, 3-acetylpyridine-ADP+ and thio-NADP+, can be used successfully
possibly takes part in the further metabolic reactions of the fragments formed from the side-chain of the steroid hormone precursor in the adrenals or gonads
enzyme transfers the pro-R hydrogen from the pyridine 4 position of the reduced coenzyme. This stereospecificity is stable over a broad range of temperatures up to 70°C and different concentrations of the coenzyme (catalytic or stoichiometric)
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
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
an evolutionary tree is constructed to analyze the evolution of the enzyme illustrates that the isopropanol dehydrogenase from Aspergillus fumigatus Af293 is far from to other dehydrogenases
an evolutionary tree is constructed to analyze the evolution of the enzyme illustrates that the isopropanol dehydrogenase from Aspergillus fumigatus Af293 is far from to other dehydrogenases
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
without any stabilizer, the enzyme at pH 5.6 and 7.0 retains over 25% of its maximum activity after pre-treated in different buffers ranging from pH 5.6-10.0 for 27 h at 4°C
without any stabilizer, the enzyme at pH 5.6 and 7.0 retains over 25% of its maximum activity after pre-treated in different buffers ranging from pH 5.6-10.0 for 27 h at 4°C
the enzyme is an ideal candidate biocatalyst in the construction of coenzyme regeneration system and the enzymatic bioconversion of high value alcohols or other compounds
the enzyme is an ideal candidate biocatalyst in the construction of coenzyme regeneration system and the enzymatic bioconversion of high value alcohols or other compounds