Issue 47, 2010
From the journal:

Chemical Communications

The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer†

Vanja Stojković,a   Laura L. Perissinotti,ab   Jeeyeon Lee,c   Stephen J. Benkovicc  and  Amnon Kohen*a  

* Corresponding authors

a Department of Chemistry, The University of Iowa, Iowa City, IA, USA
E-mail: amnon-kohen@uiowa.edu
Fax: +1 319 335 1270
Tel: +1 319 335 0234

b Departamento de Química Inorgánica, Analítica y Química Física/INQUIMAE, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón II, piso 3, C1428EHA Buenos Aires, Argentina

c Department of Chemistry, Pennsylvania State University, University Park, PA, USA

Abstract

Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.

Graphical abstract: The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

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Article information

DOI
https://doi.org/10.1039/C0CC02988B
Article type
Communication
Submitted
02 Aug 2010
Accepted
28 Sep 2010
First published
25 Oct 2010

Chem. Commun., 2010,46, 8974-8976

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The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

V. Stojković, L. L. Perissinotti, J. Lee, S. J. Benkovic and A. Kohen, Chem. Commun., 2010, 46, 8974 DOI: 10.1039/C0CC02988B

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