Structure-function correlations of two highly conserved motifs in Saccharomyces cerevisiae squalene epoxidase.
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.
Ruckenstuhl
Christoph
C
Institute of Molecular Biosciences, Karl-Franzens-Universität Graz, Humboldtstrasse 50, A-8010 Graz, Austria.
Poschenel
Andrea
A
Possert
Reinhard
R
Baral
Pravas Kumar
PK
Gruber
Karl
K
Turnowsky
Friederike
F
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
D029701:Saccharomyces cerevisiae Proteins; D000499:Allylamine; D050603:Squalene Monooxygenase