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

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

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          Abstract

          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.

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