Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Krump, C; Vogl, M; Brecker, L; Nidetzky, B; Kratzer, R.
Acceleration of an aldo-keto reductase by minimal loop engineering.
Protein Eng Des Sel. 2014; 27(7):245-248
Doi: 10.1093/protein/gzu021
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- Führende Autor*innen der Med Uni Graz
- Krump Corinna
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- 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 (k(cat)) for reductions of bulky-bulky ketones at constant substrate and coenzyme affinities (i.e. K(m Ketone), K(m NADH)). © The Author 2014. Published by Oxford University Press.
- Find related publications in this database (using NLM MeSH Indexing)
- Aldehyde Reductase - chemistry
- Aldehyde Reductase - genetics
- Aldehyde Reductase - metabolism
- Aldo-Keto Reductases -
- Candida - enzymology
- Hydrogen Bonding -
- Kinetics -
- Models, Molecular -
- Mutation -
- NAD - metabolism
- Protein Conformation -
- Protein Engineering -
- Find related publications in this database (Keywords)
- Aldo-keto reductase
- chiral ethyl mandelates
- enzyme engineering
- saturation transfer difference NMR