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Structure of human pancreatic lipase.

Nature (1990-02-22)
F K Winkler, A D'Arcy, W Hunziker
ABSTRACT

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 the porcine enzyme, indicating that this residue is essential in catalysis, but other data are more consistent with a function in interfacial recognition. Our structural results are evidence that Ser 152 is the nucleophilic residue essential for catalysis. It is located in the larger N-terminal domain at the C-terminal edge of a doubly wound parallel beta-sheet and is part of an Asp-His-Ser triad, which is chemically analogous to, but structurally different from, that in the serine proteases. This putative hydrolytic site is covered by a surface loop and is therefore inaccessible to solvent. Interfacial activation, a characteristic property of lipolytic enzymes acting on water-insoluble substrates at water-lipid interfaces, probably involves a reorientation of this flap, not only in pancreatic lipases but also in the homologous hepatic and lipoprotein lipases.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Lipase from Rhizopus oryzae, powder (fine), ~10 U/mg
Sigma-Aldrich
Lipase from Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
Sigma-Aldrich
Lipase from Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
Sigma-Aldrich
Lipase from Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
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Lipase from Candida rugosa, Type VII, ≥700 unit/mg solid
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Lipase from wheat germ, Type I, lyophilized powder, 5-15 units/mg solid
Sigma-Aldrich
Lipase from porcine pancreas, Type II, ≥125 units/mg protein (using olive oil (30 min incubation)), 30-90 units/mg protein (using triacetin)
Sigma-Aldrich
Lipase from porcine pancreas, Type VI-S, ≥20,000 units/mg protein, lyophilized powder
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Lipase acrylic resin, ≥5,000 U/g, recombinant, expressed in Aspergillus niger
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Lipase from Aspergillus oryzae, ≥20,000 U/g
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Lipase from Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
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Lipase from Candida rugosa, lyophilized, powder (fine), 15-25 U/mg
Sigma-Aldrich
Lipase from Rhizopus niveus, powder (fine), ≥1.5 U/mg
Sigma-Aldrich
Lipase from Candida rugosa, powder, yellow-brown, ≥2 U/mg
Sigma-Aldrich
Lipase from Mucor miehei, powder, slightly brown, ~1 U/mg
Sigma-Aldrich
Lipase from Candida sp., recombinant, expressed in Aspergillus niger
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Lipase B Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~9 U/mg
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Lipase A Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~2 U/mg
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Lipase from Pseudomonas cepacia, powder, light beige, ≥30 U/mg
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Lipase immobilized from Candida antarctica, beads, slightly brown, >2 U/mg
Sigma-Aldrich
Lipase from Mucor javanicus, lyophilized powder, ≥300 units/mg solid (using olive oil)
Sigma-Aldrich
Lipase from Aspergillus niger, powder (fine), ~200 U/g