Issue 46, 2010
From the journal:

Chemical Communications

Computational design of orthogonal nucleoside kinases†‡

Lingfeng Liu,a   Paul Murphy,b   David Bakerbc  and  Stefan Lutz*a  

* Corresponding authors

a Department of Chemistry, Emory University, Atlanta, USA
E-mail: sal2@emory.edu
Fax: +1 404-727-6586
Tel: +1 404-712-2170

b Department of Biochemistry, University of Washington, Seattle, USA

c Howard Hughes Medical Institute, Seattle, USA

Abstract

We report the computational enzyme design of an orthogonal nucleoside analog kinase for 3′-deoxythymidine. The best kinase variant shows an 8500-fold change in substrate specificity, resulting from a 4.6-fold gain in catalytic efficiency for the nucleoside analog and a 2000-fold decline for the native substrate thymidine.

Graphical abstract: Computational design of orthogonal nucleoside kinases

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Article information

DOI
https://doi.org/10.1039/C0CC02961K
Article type
Communication
Submitted
01 Pha 2010
Accepted
29 Leo 2010
First published
19 Mph 2010

Chem. Commun., 2010,46, 8803-8805

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Computational design of orthogonal nucleoside kinases

L. Liu, P. Murphy, D. Baker and S. Lutz, Chem. Commun., 2010, 46, 8803 DOI: 10.1039/C0CC02961K

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