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Antimicrobial Agents and Chemotherapy, April 2008, p. 1496-1499, Vol. 52, No. 4
0066-4804/08/$08.00+0     doi:10.1128/AAC.01282-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Structure-Function Correlations of Two Highly Conserved Motifs in Saccharomyces cerevisiae Squalene Epoxidase{triangledown}

Christoph Ruckenstuhl,1 Andrea Poschenel,1 Reinhard Possert,1 Pravas Kumar Baral,2 Karl Gruber,2 and Friederike Turnowsky1*

Institute of Molecular Biosciences, Karl-Franzens-Universität Graz, Graz, Austria,1 Institute of Chemistry, Karl-Franzens-Universität Graz, Graz, Austria2

Received 4 October 2007/ Returned for modification 10 November 2007/ Accepted 10 January 2008

Saccharomyces cerevisiae squalene epoxidase contains two highly conserved motifs, 1 and 2, of unknown function. Amino acid substitutions in both regions reduce enzyme activity and/or alter allylamine sensitivity. In the homology model, these motifs flank the flavin adenine dinucleotide cofactor and form part of the interface between cofactor and substrate binding domains.

* Corresponding author. Mailing address: Institute of Molecular Biosciences, Karl-Franzens-Universität Graz, Humboldtstrasse 50, A-8010 Graz, Austria. Phone: 43 316 380 5629. Fax: 43 316 380 9898. E-mail: friederike.turnowsky{at}uni-graz.at

{triangledown} Published ahead of print on 22 January 2008.

Antimicrobial Agents and Chemotherapy, April 2008, p. 1496-1499, Vol. 52, No. 4
0066-4804/08/$08.00+0     doi:10.1128/AAC.01282-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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