Structure-Function Correlations of Two Highly Conserved Motifs inSaccharomyces cerevisiaeSqualene Epoxidase
Copyright policy )Structure-Function Correlations of Two Highly Conserved Motifs inSaccharomyces cerevisiaeSqualene Epoxidase
ABSTRACTSaccharomyces cerevisiaesqualene 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.
- University of Graz Austria
Models, Molecular, Structure-Activity Relationship, Saccharomyces cerevisiae Proteins, Squalene Monooxygenase, Amino Acid Motifs, Amino Acid Sequence, Saccharomyces cerevisiae, Conserved Sequence, Allylamine
Models, Molecular, Structure-Activity Relationship, Saccharomyces cerevisiae Proteins, Squalene Monooxygenase, Amino Acid Motifs, Amino Acid Sequence, Saccharomyces cerevisiae, Conserved Sequence, Allylamine
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