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American Society for Microbiology, Antimicrobial Agents and Chemotherapy, 4(52), p. 1496-1499, 2008

DOI: 10.1128/aac.01282-07

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

Journal article published in 2008 by Christoph Ruckenstuhl, Andrea Poschenel, Reinhard Possert, Pravas Kumar Baral, Karl Gruber ORCID, Friederike Turnowsky
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

ABSTRACT 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.