Insight into the Stereospecificity of Short-Chain Thermus thermophilus Alcohol Dehydrogenase Showing pro-S Hydride Transfer and Prelog Enantioselectivity

Title: Insight into the Stereospecificity of Short-Chain Thermus thermophilus Alcohol Dehydrogenase Showing pro-S Hydride Transfer and Prelog Enantioselectivity

Volume: 17 Issue: 4

Author(s): Angela Pennacchio, Assunta Giordano, Luciana Esposito, Emma Langella, Mose Rossi and Carlo A. Raia

Affiliation:

Keywords: Cofactor stereospecificity, Prelog rule, enantioselectivity, short-chain dehydrogenase/reductase, Thermus thermophilus, Bacillus stearothermophilus

Abstract: The stereochemistry of the hydride transfer in reactions catalyzed by NAD(H)-dependent alcohol dehydrogenase from Thermus thermophilus HB27 was determined by means of 1H-NMR spectroscopy. The enzyme transfers the pro-S hydrogen of [4R-2H]NADH and exhibits Prelog specificity. Enzyme-substrate docking calculations provided structural details about the enantioselectivity of this thermophilic enzyme. These results give additional insights into the diverse active site architectures of the largely versatile short-chain dehydrogenase superfamily enzymes. A feasible protocol for the synthesis of [4R-2H]NADH with high yield was also set up by enzymatic oxidation of 2-propanol-d8 catalyzed by Bacillus stearothermophilus alcohol dehydrogenase.

Cite this article as:

Pennacchio Angela, Giordano Assunta, Esposito Luciana, Langella Emma, Rossi Mose and Raia A. Carlo, Insight into the Stereospecificity of Short-Chain Thermus thermophilus Alcohol Dehydrogenase Showing pro-S Hydride Transfer and Prelog Enantioselectivity, Protein & Peptide Letters 2010; 17 (4) . https://dx.doi.org/10.2174/092986610790963564

DOI https://dx.doi.org/10.2174/092986610790963564	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305