Crystal structure of the catalytic domain of human bile salt activated lipase

Protein Sci. 2000 Sep;9(9):1783-90. doi: 10.1110/ps.9.9.1783.


Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a variety of lipids in the small intestine. A distinct property of BAL is its dependency on bile salts in hydrolyzing substrates of long acyl chains or bulky alcoholic motifs. A crystal structure of the catalytic domain of human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has been determined at 2.3 A resolution. The crystal form belongs to space group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein shows an alpha/beta hydrolase fold. In the absence of bound bile salt molecules, the protein possesses a preformed catalytic triad and a functional oxyanion hole. Several surface loops around the active site are mobile, including two loops potentially involved in substrate binding (residues 115-125 and 270-285).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bile Acids and Salts / metabolism*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Enzyme Activation
  • Humans
  • Lipase / chemistry*
  • Lipase / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid


  • Bile Acids and Salts
  • Lipase

Associated data

  • PDB/1F6W