Title : Use of Escherichia coli strains containing fad mutations plus a triple plasmid expression system to study the import of myristate, its activation by Saccharomyces cerevisiae acyl-CoA synthetase, and its utilization by S. cerevisiae myristoyl-CoA:protein N-myristoyltransferase.

Pub. Date : 1993 Feb 25

PMID : 8440712






2 Functional Relationships(s)
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1 In addition, S. cerevisiae Faa1p is better able to direct myristoyl-CoA to the bacteria"s phospholipid biosynthetic pathways than FadD, while FadD is more efficient at directing myristoyl-CoA to the genetically engineered protein N-myristoylation pathway. S-tetradecanoyl-coenzyme A long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C
2 In addition, S. cerevisiae Faa1p is better able to direct myristoyl-CoA to the bacteria"s phospholipid biosynthetic pathways than FadD, while FadD is more efficient at directing myristoyl-CoA to the genetically engineered protein N-myristoylation pathway. S-tetradecanoyl-coenzyme A long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C