Structure of human pancreatic lipase

@article{Winkler1990StructureOH,
  title={Structure of human pancreatic lipase},
  author={Fritz K. Winkler and Allan D'arcy and Willi Hunziker},
  journal={Nature},
  year={1990},
  volume={343},
  pages={771-774}
}
PANCREATIC lipase (triacylglycerol acyl hydrolase) fulfills a key function in dietary fat absorption by hydrolysing triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids. We have determined the three-dimensional structure of the human enzyme, a single-chain glycoprotein of 449 amino acids, by X-ray crystallography and established its primary structure by sequencing complementary DNA clones. Enzymatic activity is lost after chemical modification of Ser 152 in… Expand
An inactive pancreatic lipase-related protein is activated into a triglyceride-lipase by mutagenesis based on the 3-D structure.
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The biochemical, histochemical and clinical studies as well as the 3-D structures obtained will be a great help for a better understanding of the structure-function relationships of digestive lipases. Expand
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Identification of the active‐site serine in human pancreatic lipase by chemical modification with tetrahydrolipstatin
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The results obtained for human pancreatic lipase corroborate the inhibition mechanism of THL found on the porcine enzyme, and are in full agreement with the identification of the Ser‐152…His‐263…Asp‐176 catalytic triad in the X‐ray structure of human pancreatIC lipase. Expand
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Structural organisation of human bile-salt-activated lipase probed by limited proteolysis and expression of a recombinant truncated variant.
  • K. Loomes
  • Biology, Medicine
  • European journal of biochemistry
  • 1995
Bile-salt-activated lipase belongs to the cholinesterase alpha/beta-hydrolase-fold family of proteins. Here, we have investigated the structural organisation of the human isoform by mapping trypticExpand
Structure of the pancreatic lipase–procolipase complex
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The structure of procolipase is described, which essentially consists of three 'fingers' and is topologically comparable to snake toxins and may form the interfacial binding site of pancreatic lipase. Expand
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