Reversal of Regioselectivity in Zinc‐Dependent Medium‐Chain Alcohol Dehydrogenase from Rhodococcus erythropolis toward Octanone Derivatives
 
Yazarlar (7)
Gaurao V Dhoke Rheinisch-Westfälische Technische Hochschule Aachen, Almanya
Dr. Öğr. Üyesi Yunus ENSARİ Kafkas Üniversitesi, Türkiye
Dinc Yasat Hacibaloglu Rheinisch-Westfälische Technische Hochschule Aachen, Almanya
Anna Gärtner Rheinisch-Westfälische Technische Hochschule Aachen, Almanya
Anna Joelle Ruff Rheinisch-Westfälische Technische Hochschule Aachen, Almanya
Marco Bocola Rheinisch-Westfälische Technische Hochschule Aachen, Almanya
Mehdi D Davari Rheinisch-Westfälische Technische Hochschule Aachen, Almanya
Makale Türü Açık Erişim Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale)
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