Brady_1990_Nature_343_767

Reference

Title : A serine protease triad forms the catalytic centre of a triacylglycerol lipase - Brady_1990_Nature_343_767
Author(s) : Brady L , Brzozowski AM , Derewenda ZS , Dodson E , Dodson G , Tolley S , Turkenburg JP , Christiansen L , Huge-Jensen B , Norskov L , Thim L , Menge U
Ref : Nature , 343 :767 , 1990
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.

PubMedSearch : Brady_1990_Nature_343_767
PubMedID: 2304552
Gene_locus related to this paper: rhimi-lipas

Related information

Gene_locus rhimi-lipas
Family Lipase_3
Structure 1TGL    3TGL

Citations formats

Brady L, Brzozowski AM, Derewenda ZS, Dodson E, Dodson G, Tolley S, Turkenburg JP, Christiansen L, Huge-Jensen B, Norskov L, Thim L, Menge U (1990)
A serine protease triad forms the catalytic centre of a triacylglycerol lipase
Nature 343 :767

Brady L, Brzozowski AM, Derewenda ZS, Dodson E, Dodson G, Tolley S, Turkenburg JP, Christiansen L, Huge-Jensen B, Norskov L, Thim L, Menge U (1990)
Nature 343 :767