Acceleration of an aldo-keto reductase by minimal loop engineering

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...

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Detalles Bibliográficos
Autores principales: Krump, C., Vogl, M., Brecker, L., Nidetzky, B., Kratzer, R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Short Communication
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4064709/
https://www.ncbi.nlm.nih.gov/pubmed/24951537
http://dx.doi.org/10.1093/protein/gzu021
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author Krump, C.
Vogl, M.
Brecker, L.
Nidetzky, B.
Kratzer, R.
author_facet Krump, C.
Vogl, M.
Brecker, L.
Nidetzky, B.
Kratzer, R.
author_sort Krump, C.
collection PubMed
description 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)).
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spelling pubmed-40647092014-07-01 Acceleration of an aldo-keto reductase by minimal loop engineering Krump, C. Vogl, M. Brecker, L. Nidetzky, B. Kratzer, R. Protein Eng Des Sel Short Communication 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)). Oxford University Press 2014-07 /pmc/articles/PMC4064709/ /pubmed/24951537 http://dx.doi.org/10.1093/protein/gzu021 Text en © The Author 2014. Published by Oxford University Press. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Short Communication
Krump, C.
Vogl, M.
Brecker, L.
Nidetzky, B.
Kratzer, R.
Acceleration of an aldo-keto reductase by minimal loop engineering
title Acceleration of an aldo-keto reductase by minimal loop engineering
title_full Acceleration of an aldo-keto reductase by minimal loop engineering
title_fullStr Acceleration of an aldo-keto reductase by minimal loop engineering
title_full_unstemmed Acceleration of an aldo-keto reductase by minimal loop engineering
title_short Acceleration of an aldo-keto reductase by minimal loop engineering
title_sort acceleration of an aldo-keto reductase by minimal loop engineering
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4064709/
https://www.ncbi.nlm.nih.gov/pubmed/24951537
http://dx.doi.org/10.1093/protein/gzu021
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