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

✍ Scribed by Turkenburg, Johan P.; Christiansen, Lars; Huge-Jensen, Birgitte; Norskov, Leif; Brady, Leo; Brzozowski, Andrzej M.; Derewenda, Zygmunt S.; Dodson, Eleanor; Dodson, Guy; Tolley, Shirley

• Book ID: 109762837
• Publisher: Nature Publishing Group
• Year: 1990
• Tongue: English
• Weight: 341 KB
• Volume: 343
• Category: Article
• ISSN: 0028-0836
• DOI: 10.1038/343767a0

✦ Synopsis

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.