Issue 20, 2011
From the journal:

Chemical Communications

Structure-guided redesign of d-fructose-6-phosphatealdolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation†

Mariana Gutierrez,a   Teodor Parella,b   Jesús Joglar,a   Jordi Bujonsa  and  Pere Clapés*a  

* Corresponding authors

a Instituto de Química Avanzada de Cataluña-CSIC, Jordi Girona 18-26, 08034 Barcelona, Spain
E-mail: pere.clapes@iqac.csic.es
Fax: +34 93 2045904
Tel: +34 93 4006112

b Servei de Ressonància Magnètica Nuclear, Dept of Chemistry, Universitat Autònoma de Barcelona, Bellaterra, Spain

Abstract

Structure-guided re-design of the acceptor binding site of D-fructose-6-phosphate aldolase from E. coli leads to the construction of FSA A129S/A165G double mutant with an activity between 5- to >900-fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives.

Graphical abstract: Structure-guided redesign of d-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation

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Article information

DOI
https://doi.org/10.1039/C1CC11069A
Article type
Communication
Submitted
23 Feb 2011
Accepted
31 Mar 2011
First published
18 Apr 2011

Chem. Commun., 2011,47, 5762-5764

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Structure-guided redesign of D-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation

M. Gutierrez, T. Parella, J. Joglar, J. Bujons and P. Clapés, Chem. Commun., 2011, 47, 5762 DOI: 10.1039/C1CC11069A

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