Structure-function relationships in naturally occurring mutants of pancreatic lipase

From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic lipases, 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 proper...

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Bibliographic Details
Published inProtein engineering Vol. 7; no. 4; p. 563
Main Authors Carrière, F, Thirstrup, K, Boel, E, Verger, R, Thim, L
Format Journal Article
LanguageEnglish
Published England 01.04.1994
Subjects
Amino Acid Sequence
Animals
Aspergillus oryzae - genetics
Colipases - metabolism
Enzyme Activation
Guinea Pigs
Humans
Lipase - chemistry
Lipase - genetics
Lipase - metabolism
Lipase - ultrastructure
Models, Biological
Models, Molecular
Molecular Sequence Data
Mutation
Phospholipases - analysis
Recombinant Proteins - chemistry
Rodentia
Structure-Activity Relationship
Triglycerides - metabolism
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Summary:From primary structure comparison, the pancreatic lipase family is now divided into three subgroups: classical pancreatic lipases, 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 lipases. Both enzymes display a high phospholipase activity and are not interfacially activated using a short chain triglyceride as substrate. Their activity towards insoluble triglycerides is inhibited by micellar concentrations of bile salts and is not restored by addition of colipase. These atypical kinetic properties are discussed in the light of amino acid sequence comparison between RP2 and classical pancreatic lipases, based on the closed and open conformations of the 3-D structure of human pancreatic lipase.
ISSN:0269-2139
DOI:10.1093/protein/7.4.563