Brian Baker, Chemistry and Biochemistry
The purpose of my project was to determine whether the hydrolysis of lysophosphatidylcholine occurs at the sn-1 or the sn-2 position. I found that the rate of acyl migration is about 17 times slower than the hydrolytic rate. Additionally, the hydrolytic rate varies with the source of the enzyme. Both of these findings suggest that migration is not required for hydrolysis; this implies that hydrolysis can occur in the sn-1 position. I attempted to synthesize an analog that would restrict acyl migration thereby allowing hydrolysis only in the sn-1 position, however these attempts failed. I used computer aided molecular modelling to probe the enzyme-substrate interactions and found that lysophosphatidylcholine does fit into the active site of the enzyme with an orientation conducive to hydrolysis.