Abstract
The consensus sequence of the third histidine box of a range of Delta(5), Delta(6), Delta(8) and sphingolipid desaturases differs from that of the membrane-bound non-fusion Delta(12) and Delta(15) desaturases in the presence of glutamine instead of histidine. We have used site-directed mutagenesis to determine the importance of glutamine and other residues of the third histidine box and created a chimaeric enzyme to determine the ability of the Cyt b(5) fusion domain from the plant sphingolipid desaturase to substitute for the endogenous domain of the Delta(6) desaturase.
MeSH terms
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Amino Acid Substitution
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Arabidopsis / enzymology
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Asteraceae / enzymology*
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Cytochromes b5 / chemistry
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Cytochromes b5 / metabolism
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Fatty Acid Desaturases / chemistry*
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Fatty Acid Desaturases / genetics
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Fatty Acid Desaturases / metabolism*
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Histidine / metabolism
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Linoleoyl-CoA Desaturase
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Mutagenesis, Site-Directed
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae
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Vegetables / enzymology
Substances
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Recombinant Fusion Proteins
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Recombinant Proteins
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Histidine
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Cytochromes b5
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Fatty Acid Desaturases
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Linoleoyl-CoA Desaturase
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delta-8 fatty acid desaturase