Acceleration of an aldo-keto reductase by minimal loop engineering

Corinna Krump, Michael Vogl, Lothar Brecker, Bernd Nidetzky*, Regina Kratzer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Aldo-keto reductases tighten coenzyme binding by forming a hydrogen bond across the pyrophosphate group of NAD(P)(H). Mutation of the hydrogen bonding anchor Lys24 in Candida tenuis xylose reductase prevents fastening of the “safety belt” around NAD(H). The loosened NAD(H) binding leads to increased turnover numbers (kcat) for reductions of bulky-bulky ketones at constant substrate and coenzyme affinities (i.e. Km Ketone, Km NADH).
Original languageEnglish
Pages (from-to)245-248
JournalProtein Engineering, Design, and Selection
Volume27
Issue number7
DOIs
Publication statusPublished - 2014

Fields of Expertise

  • Human- & Biotechnology

Treatment code (Nähere Zuordnung)

  • Basic - Fundamental (Grundlagenforschung)
  • Application

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