Journal ArticleDOI
A serine protease triad forms the catalytic centre of a triacylglycerol lipase.
Leo Brady,Andrzej M. Brzozowski,Andrzej M. Brzozowski,Zygmunt S. Derewenda,Eleanor J. Dodson,Guy Dodson,S.P. Tolley,Johan P. Turkenburg,Lars Christiansen,Birgitte Huge-Jensen,Leif Norskov,Lars Thim,Ulrich Menge +12 more
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TLDR
The X-ray structure of the Mucor miehei triglyceride lipase is reported and the atomic model obtained reveals a Ser .. His .. Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.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.read more
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Molecular Dynamic Simulation of the Porcine Pancreatic Lipase in Non-aqueous Organic Solvents.
Zi-Shi Chen,Yi-Da Wu,Jin-Heng Hao,Yu-Jia Liu,Kang-Ping He,Wen-Hao Jiang,Mei-Jie Xiong,Yong-Si Lv,Shi-Lin Cao,Jie Zhu +9 more
TL;DR: DMSO acts as a better solvent, in which the PPL can be loose and extended, and retains its native backbone in DMSO compared to PRG and EtOH, and the molecular docking results showed that PPL in D MSO exhibited the highest enzyme-substrate affinity.
Journal ArticleDOI
A novel fusidic acid resistance gene from Streptomyces lividans 66 encodes a highly specific esterase.
TL;DR: Purified FusH cleaved equally well an acetyl, a thioacetyl or a formyl group from the 16 beta-position of fusidic acid and its derivatives, however, a propionyl group at the 16 Beta-position was attacked with difficulty and a 16 alpha-acetyl group was not hydrolysed at all, indicating that FUSH is a highly specific esterase.
Journal ArticleDOI
Cleavage of BSA by a dipeptide seryl-histidine
TL;DR: A dipeptide seryl-histidine (Ser-His) was found to have the protein cleavage activity and might provide clues to the possible roles of short oligopeptides in the origins of modern enzymes.
Journal ArticleDOI
Non-lipolytic and lipolytic sequence-related carboxylesterases: A comparative study of the structure–function relationships of rabbit liver esterase 1 and bovine pancreatic bile-salt-activated lipase
TL;DR: Inhibition studies and manual docking of a bulky ester molecule as vinyl laurate in the catalytic pocket of rLE and bBAL show that the inability of the esterase to hydrolyse large water-insoluble esters is not due to steric hindrance.
Journal ArticleDOI
Gene cloning, sequencing, and expression of an esterase from Acinetobacter lwoffii I6C-1.
Hye Eun Kim,In Soo Lee,Joo-Hwan Kim,Kyu Woong Hahn,Ul Jae Park,Hyon Soo Han,Kyeong Ryang Park +6 more
TL;DR: The EstA sequence was similar to that of the carboxylesterase from Acinetobacter calcoaceticus, Archaeoglobus fulgidus, and Mycobacterium tuberculosis, which contained the conserved motif G-X1-S-X2-G carrying the active-site serine of hydrolytic enzyme.
References
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Journal ArticleDOI
Human lipoprotein lipase complementary DNA sequence
TL;DR: Analysis of the sequence indicates that human lipoprotein lipase, hepaticlipase, and pancreatic lipase are members of a gene family that acts to hydrolyze triglycerides, providing free fatty acids for cells and affecting the maturation of circulating lipoproteins.