| Makale Türü |
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| Dergi Adı | Chembiochem | ||
| Dergi ISSN | 1439-4227 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI | ||
| Makale Dili | İngilizce | Basım Tarihi | 10-2020 |
| Cilt / Sayı / Sayfa | 21 / 20 / 2957–2965 | DOI | 10.1002/cbic.202000247 |
| Makale Linki | https://onlinelibrary.wiley.com/doi/abs/10.1002/cbic.202000247 | ||
| Özet |
| The zinc‐dependent medium‐chain alcohol dehydrogenase from Rhodococcus erythropolis (ReADH) is one of the most versatile biocatalysts for the stereoselective reduction of ketones to chiral alcohols. Despite its known broad substrate scope, ReADH only accepts carbonyl substrates with either a methyl or an ethyl group adjacent to the carbonyl moiety; this limits its use in the synthesis of the chiral alcohols that serve as a building blocks for pharmaceuticals. Protein engineering to expand the substrate scope of ReADH toward bulky substitutions next to carbonyl group (ethyl 2‐oxo‐4‐phenylbutyrate) opens up new routes in the synthesis of ethyl‐2‐hydroxy‐4‐phenylbutanoate, an important intermediate for anti‐hypertension drugs like enalaprilat and lisinopril. We have performed computer‐aided engineering of ReADH toward ethyl 2‐oxo‐4‐phenylbutyrate and octanone derivatives. W296, which is located in … |
| Anahtar Kelimeler |
| alcohol dehydrogenases | homology modeling | molecular docking | protein engineering | Rhodococcus erythropolis |
| Atıf Sayıları | |
| Google Scholar | 8 |
| Web of Science | 7 |
| Scopus | 7 |
| Dergi Adı | CHEMBIOCHEM |
| Yayıncı | John Wiley and Sons Inc |
| Açık Erişim | Hayır |
| ISSN | 1439-4227 |
| E-ISSN | 1439-7633 |
| CiteScore | 5,2 |
| SJR | 0,844 |
| SNIP | 0,650 |