Structure–function relationships in naturally occurring mutants of pancreatic lipase

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Abstract
From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic Upases, pancreatic lipase-related proteins 1 (RPI) and pancreatic lipase-related proteins 2 (RP2). Among the RP2 subfamily, the guinea-pig and coypu enzymes share kinetic properties which differ from those of classical pancreatic Upases. Both enzymes display a high phospholipase activity and are not interfaciaUy activated using a short chain triglyceride as substrate. Their activity towards insoluble triglycerides is inhibited by mkeUar concentrations of bile salts and is not restored by addition of coUpase. These atypical kinetic properties are discussed in the light of amino acid sequence comparison between RP2 and classical pancreatic Upases, based on the closed and open conformations of the 3-D structure of human pancreatic Upase.

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