Caenorhabditis elegans

BUTCHER LAB - BIOCHEMISTRY DEPARTMENT

University of Florida

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The nematode C. elegans secretes ascarosides, a class of pheromones worms use to communicate with each other. Previously, the crystal structure of C. elegans Acyl-CoA Oxidase 1.1 (ACOX-1.1) revealed the purified enzyme was bound not only to its FAD cofactor but also to ATP. Prior kinetic studies show that ACOX incubated without ATP or FAD gradually lost its activity. This loss could be blocked by the addition of ATP and FAD, but not FAD alone. Therefore, we studied  the immediate effect of ATP and/or FAD addition on the activity of ACOX-1.1 using an HRP-coupled kinetic assay. To study the key residues involved in the allosteric network, we utilized mutagenesis and performed kinetic assays of the mutant enzyme.