Acceleration of an aldo-keto reductase by minimal loop engineering

Corinna Krump; Michael Vogl; Lothar Brecker; Bernd Nidetzky; Regina Kratzer

doi:10.1093/protein/gzu021

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

Institute of Biotechnology and Biochemical Engineering (6510)

Research output: Contribution to journal › Letter › peer-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 language	English
Pages (from-to)	245-248
Journal	Protein Engineering, Design, and Selection
Volume	27
Issue number	7
DOIs	https://doi.org/10.1093/protein/gzu021
Publication status	Published - 2014

Fields of Expertise

Human- & Biotechnology

Treatment code (Nähere Zuordnung)

Basic - Fundamental (Grundlagenforschung)
Application

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10.1093/protein/gzu021Licence: CC BY 3.0

Cite this

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title = "Acceleration of an aldo-keto reductase by minimal loop engineering",

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).",

author = "Corinna Krump and Michael Vogl and Lothar Brecker and Bernd Nidetzky and Regina Kratzer",

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doi = "10.1093/protein/gzu021",

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journal = "Protein Engineering, Design, and Selection",

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T1 - Acceleration of an aldo-keto reductase by minimal loop engineering

AU - Krump, Corinna

AU - Vogl, Michael

AU - Brecker, Lothar

AU - Nidetzky, Bernd

AU - Kratzer, Regina

PY - 2014

Y1 - 2014

N2 - 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).

AB - 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).

U2 - 10.1093/protein/gzu021

DO - 10.1093/protein/gzu021

M3 - Letter

SN - 1741-0134

VL - 27

SP - 245

EP - 248

JO - Protein Engineering, Design, and Selection

JF - Protein Engineering, Design, and Selection

IS - 7

ER -

Acceleration of an aldo-keto reductase by minimal loop engineering

Abstract

Fields of Expertise

Treatment code (Nähere Zuordnung)

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