Lipases by Phosphonates and the 3-D Structures of Lipase-inhibitor Complexes

Inhibition of Lipases by Phosphonates and the 3-D Structures of Lipase-Inhibitor Complexes 

Stadler et al. [95] studied the influence of substrate hydrophobicity and steric hindrance by variation of the alkyl and acyl chain length at the sn-2 position of the glycerol backbone. Hydrolysis of these synthetic substrates demonstrated fhat minor structural variations at this sn-2 position of TAG strongly affect fhe stereoselectivity of file lipases tested. These authors concluded that fhe ester carbonyl in the (non-hydrolyzed) sn-2 position of a TAG was responsible for correct positioning of fhe substrate in the binding site of lipases. Taking into consideration the 

2 The 2.45 A Resolution Structure of the Pancreatic/Procolipase Complex Inhibited by a C-n Alkylphosphonate 

3 Crystal Structure of the Open Form of DCL in Complex with a Phosphonate Inhibitor 

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