Structure-function correlations of two highly conserved motifs in Saccharomyces cerevisiae squalene epoxidase.

Antimicrobial Agents and Chemotherapy
Christoph RuckenstuhlFriederike Turnowsky

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.

References

Feb 1, 1994·Protein Science : a Publication of the Protein Society·Z S Hendsch, B Tidor
Feb 12, 1998·Protein Science : a Publication of the Protein Society·M H EppinkW J Van Berkel
Sep 10, 2003·Biochemical and Biophysical Research Communications·Vlasta KlobucníkováIvan Hapala
Nov 26, 2003·Antimicrobial Agents and Chemotherapy·Regina LeberFriederike Turnowsky
Mar 12, 2004·Biochemical and Biophysical Research Communications·Hee-Kyoung LeeGlenn D Prestwich
Oct 18, 2006·Antimicrobial Agents and Chemotherapy·Christoph RuckenstuhlFriederike Turnowsky

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Citations

Nov 5, 2011·Biological Chemistry·Agnieszka BelterJan Barciszewski
Jan 15, 2011·Journal of Chemical Information and Modeling·Marcin NowosielskiLeszek Rychlewski

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