Fig. 7.

Modified serine at residue 114. A: The crystal structure of blocked Ser114 with BMK (blocked structure). The catalytic triad is shown as red sticks. Ligplot showing residues involved in interactions between BMK and _CAlipase. The covalently bound BMK forms hydrogen bonds with Leu38 and Trp115. The methyl and benzene moieties are stabilized predominately by hydrophobic interactions with Val140, Phe176, Phe179, Trp192, and Phe211. B: Ser114 is modified as the fatty acid bound form in open structure by introduction of LPC. Ligplot analysis for bound LPC and _CAlipase is shown. The hydrophobic interactions between Val140, Phe179, and Phe211 are absent due to the lack of methyl and benzyl groups.