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 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 propert...

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Bibliographic Details
Published in:Protein engineering 1994-04, Vol.7 (4), p.563-569
Main Authors: CarriÈre, Frédéric, Thirstrup, Kenneth, Boel, Esper, Verger, Robert, Thim, Lars
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Aspergillus oryzae - genetics
Biological and medical sciences
Colipases - metabolism
coypu
Enzyme Activation
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
guinea pig
Guinea Pigs
Humans
Hydrolases
interfacial activation
lid domain
Lipase - chemistry
Lipase - genetics
Lipase - metabolism
Lipase - ultrastructure
Models, Biological
Models, Molecular
Molecular Sequence Data
Mutation
phospholipase activity
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 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.
ISSN:1741-0126
0269-2139
1741-0134
1460-213X
DOI:10.1093/protein/7.4.563