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Genetic Optimization of the Catalytic Efficiency of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology

Schwizer, Fabian and Köhler, Valentin and Dürrenberger, Marc and Knörr, Livia and Ward, Thomas R.. (2013) Genetic Optimization of the Catalytic Efficiency of Artificial Imine Reductases Based on the Biotin-Streptavidin Technology. ACS Catalysis, 3 (8). pp. 1752-1755.

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Official URL: http://edoc.unibas.ch/dok/A6212073

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Abstract

Artificial metalloenzymes enable the engineering of the reaction microenvironment of the active metal catalyst by modification of the surrounding host protein. We report herein the optimization of an artificial imine reductase (ATHase) based on biotin–streptavidin technology. By introduction of lipophilic amino acid residues around the active site, an 8-fold increase in catalytic efficiency compared with the wild type imine reductase was achieved. Whereas substrate inhibition was encountered for the free cofactor and wild type ATHase, two engineered systems exhibited classical Michaelis–Menten kinetics, even at substrate concentrations of 150 mM with measured rates up to 20 min–1.
Faculties and Departments:05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Schwizer, Fabian and Köhler, Valentin and Dürrenberger, Marc and Ward, Thomas R.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
e-ISSN:2155-5435
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:03 May 2017 07:28
Deposited On:31 Jan 2014 09:51

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