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^*

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biotechnologie und Bioprozesstechnik (6510)

Publikation: Beitrag in einer Fachzeitschrift › Short communication › Begutachtung

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).

Originalsprache	englisch
Seiten (von - bis)	245-248
Fachzeitschrift	Protein Engineering, Design, and Selection
Jahrgang	27
Ausgabenummer	7
DOIs	https://doi.org/10.1093/protein/gzu021
Publikationsstatus	Veröffentlicht - 2014

Fields of Expertise

Human- & Biotechnology

Treatment code (Nähere Zuordnung)

Basic - Fundamental (Grundlagenforschung)
Application

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10.1093/protein/gzu021Lizenz: CC BY 3.0

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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 (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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AU - Vogl, Michael

AU - Brecker, Lothar

AU - Nidetzky, Bernd

AU - Kratzer, Regina

PY - 2014

Y1 - 2014

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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

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Acceleration of an aldo-keto reductase by minimal loop engineering

Abstract

Fields of Expertise

Treatment code (Nähere Zuordnung)

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