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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Allylamine / pharmacology
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Amino Acid Motifs
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Amino Acid Sequence
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Conserved Sequence
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Models, Molecular
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Saccharomyces cerevisiae / drug effects
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Squalene Monooxygenase / chemistry*
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Squalene Monooxygenase / genetics
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Squalene Monooxygenase / metabolism*
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Structure-Activity Relationship
Substances
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Saccharomyces cerevisiae Proteins
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Allylamine
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Squalene Monooxygenase