A serine protease triad forms the catalytic centre of a triacylglycerol lipase.
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.
Brady
L
L
Department of Chemistry, University of York, Heslington, UK.
Brzozowski
A M
AM
Derewenda
Z S
ZS
Dodson
E
E
Dodson
G
G
Tolley
S
S
Turkenburg
J P
JP
Christiansen
L
L
Huge-Jensen
B
B
Norskov
L
L
D000595:Amino Acid Sequence; D001665:Binding Sites; D004220:Disulfides; D008049:Lipase; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009089:Mucor / Q000201:enzymology*; D010446:Peptide Fragments; D011487:Protein Conformation; D012697:Serine Endopeptidases; D014961:X-Ray Diffraction
D004220:Disulfides; D010446:Peptide Fragments; D008049:Lipase; D012697:Serine Endopeptidases