title: Structure-function correlations of two highly conserved motifs in Saccharomyces cerevisiae squalene epoxidase.
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.
authors.affiliation: Institute of Molecular Biosciences, Karl-Franzens-Universität Graz, Humboldtstrasse 50, A-8010 Graz, Austria.
authors.forename: Christoph
authors.initials: C
authors.lastname: Ruckenstuhl
authors.forename: Andrea
authors.initials: A
authors.lastname: Poschenel
authors.forename: Reinhard
authors.initials: R
authors.lastname: Possert
authors.forename: Pravas Kumar
authors.initials: PK
authors.lastname: Baral
authors.forename: Karl
authors.initials: K
authors.lastname: Gruber
authors.forename: Friederike
authors.initials: F
authors.lastname: Turnowsky
mesh_terms: D000499:Allylamine / Q000494:pharmacology; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D017124:Conserved Sequence; D008958:Models, Molecular; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D050603:Squalene Monooxygenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D000499:Allylamine; D050603:Squalene Monooxygenase