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

Type
Label
  • Insight into the Stereospecificity of Short-Chain Thermus thermophilus Alcohol Dehydrogenase Showing pro-S Hydride Transfer and Prelog Enantioselectivity (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Alternative label
  • Pennacchio, A; Giordano, A; Esposito, L; Langella, E.; Rossi, M.; Raia C.A (2010)
    Insight into the Stereospecificity of Short-Chain Thermus thermophilus Alcohol Dehydrogenase Showing pro-S Hydride Transfer and Prelog Enantioselectivity
    in Protein and peptide letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Pennacchio, A; Giordano, A; Esposito, L; Langella, E.; Rossi, M.; Raia C.A (literal)
Pagina inizio
  • 437 (literal)
Pagina fine
  • 443 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 17 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biochimica delle Proteine, CNR, Via P. Castellino 111, I-80131, Naples, Italy Istituto di Chimica Biomolecolare, CNR, Comprensorio Olivetti, Edificio 70, Via Campi Flegrei 34, I-80078 Pozzuoli (Naples) Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134, Naples, Italy (literal)
Titolo
  • Insight into the Stereospecificity of Short-Chain Thermus thermophilus Alcohol Dehydrogenase Showing pro-S Hydride Transfer and Prelog Enantioselectivity (literal)
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 (1)H-NMR spectroscopy. The enzyme transfers the pro-S hydrogen of [4R-(2)H]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-(2)H]NADH with high yield was also set up by enzymatic oxidation of 2-propanol-d(8) catalyzed by Bacillus stearothermophilus alcohol dehydrogenase. (literal)
Prodotto di
Autore CNR

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
data.CNR.it