A serine protease triad forms the catalytic centre of a triacylglycerol lipase

Nature. 1990 Feb 22;343(6260):767-70. doi: 10.1038/343767a0.


True lipases attach triacylglycerols and act at an oil-water interface; they constitute a ubiquitous group of enzymes catalysing a wide variety of reactions, many with industrial potential. But so far the three-dimensional structure has not been reported for any lipase. Here we report the X-ray structure of the Mucor miehei triglyceride lipase and describe the atomic model obtained at 3.1 A resolution and refined to 1.9 A resolution. It reveals a Ser..His..Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Disulfides
  • Lipase*
  • Molecular Sequence Data
  • Molecular Structure
  • Mucor / enzymology*
  • Peptide Fragments
  • Protein Conformation
  • Serine Endopeptidases*
  • X-Ray Diffraction


  • Disulfides
  • Peptide Fragments
  • Lipase
  • Serine Endopeptidases