Abstract
Yeast Erv1p is a ubiquitous FAD-dependent sulfhydryl oxidase, located in the intermembrane space of mitochondria. The dimeric enzyme is essential for survival of the cell. Besides the redox-active CXXC motif close to the FAD, Erv1p harbours two additional cysteine pairs. Site-directed mutagenesis has identified all three cysteine pairs as essential for normal function. The C-terminal cysteine pair is of structural importance as it contributes to the correct arrangement of the FAD-binding fold. Variations in dimer formation and unique colour changes of mutant proteins argue in favour of an interaction between the N-terminal cysteine pair with the redox centre of the partner monomer.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites / physiology
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Color
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Conserved Sequence
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Cysteine* / metabolism
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Dimerization
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Enzyme Activation / physiology
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Flavin-Adenine Dinucleotide / metabolism
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Genetic Complementation Test
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Mitochondrial Proteins / genetics
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Mitochondrial Proteins / metabolism*
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Models, Molecular
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Mutagenesis, Site-Directed
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Oxidation-Reduction
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Oxidoreductases / genetics
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Oxidoreductases / metabolism*
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Oxidoreductases Acting on Sulfur Group Donors
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Protein Structure, Tertiary / physiology
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Saccharomyces cerevisiae
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Serine / metabolism
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Spectrophotometry
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Structure-Activity Relationship
Substances
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Mitochondrial Proteins
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Saccharomyces cerevisiae Proteins
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Flavin-Adenine Dinucleotide
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Serine
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Oxidoreductases
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Oxidoreductases Acting on Sulfur Group Donors
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ERV2 protein, S cerevisiae
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sulfhydryl oxidase
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ERV1 protein, S cerevisiae
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Cysteine