Yarrowia lipolytica dehydrogenase/reductase: An enzyme tolerant for lipophilic compounds and carbohydrate substrates

Kamila Napora, Tanja Wrodnigg, Patrick Kosmus, Martin Thonhofer, Karen Robins, Margit Winkler*

*Korrespondierende/r Autor/-in für diese Arbeit

Publikation: Beitrag in einer FachzeitschriftArtikelBegutachtung

Abstract

Yarrowia lipolytica short chain dehydrogenase/reductase (YlSDR) was expressed in Escherichia coli, purified and characterized in vitro. The substrate scope for YlSDR mediated oxidation was investigated with alcohols and unprotected carbohydrates spectrophotometrically, revealing a preference for secondary compared to primary alcohols. In reduction direction, YlSDR was highly active on ribulose and fructose, suggesting that the enzyme is a mannitol-2-dehydrogenase. In order to explore substrate tolerance especially for space-demanding, lipophilic protecting groups, 5-O-trityl-d-ribitol and 5-O-trityl-α,β-d-ribose were investigated as substrates: YlSDR oxidized 5-O-trityl-d-ribitol and 5-O-trityl-α,β-d-ribose and reduced the latter at the expense of NADP(H).
Originalspracheenglisch
Seiten (von - bis)3393-3395
FachzeitschriftBioorganic & Medicinal Chemistry Letters
Jahrgang23
Ausgabenummer11
DOIs
PublikationsstatusVeröffentlicht - 2013

Fields of Expertise

  • Human- & Biotechnology

Treatment code (Nähere Zuordnung)

  • Basic - Fundamental (Grundlagenforschung)
  • Experimental

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