Neutron crystallographic evidence of lipase–colipase complex activation by a micelle dimensional structure of the uncomplexed human enzyme
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چکیده
Institut de Biologie Structurale Jean-Pierre Ebel, CEA-CNRS, of PL in solution. The PL–CL structure (van Tilbeurgh 41 Avenue des Martyrs, 38027 Grenoble Cedex 1, 2Large Scale et al., 1993), in turn, shows that the active site is exposed Structures Group, Institut Laue-Langevin, BP 156, 38042 Grenoble and the flap makes a series of polar contacts with CL. and 3Laboratoire de Bioénergétique et d’Ingénierie des Protéines, Together, these structures have provided a comprehensive UPR 9036 CNRS, BP 71, 13402 Marseille Cedex 9, France
منابع مشابه
Neutron crystallographic evidence of lipase-colipase complex activation by a micelle.
The concept of lipase interfacial activation stems from the finding that the catalytic activity of most lipases depends on the aggregation state of their substrates. It is thought that activation involves the unmasking and structuring of the enzyme's active site through conformational changes requiring the presence of oil-in-water droplets. Here, we present the neutron structure of the activate...
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In the duodenum, pancreatic lipase (PL) develops its activity on triglycerides by binding to the bile-emulsified oil droplets in the presence of its protein cofactor pancreatic colipase (PC). The neutron crystal structure of a PC-PL-micelle complex (Hermoso, J., Pignol, D., Penel, S., Roth, M., Chapus, C., and Fontecilla-Camps, J. C. (1997) EMBO J. 16, 5531-5536) has suggested that the stabiliz...
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The binding of porcine pancreatic lipase and colipase was studied using the techniques of two-phase partition and affinity chromatography. The binding exhibited a pH dependency (maximum = pH 5.8, minimum = pH 8.6), was not significantly effected by the concentrations of NaCl, (0 to 1 M), and was inhibited by bile salts at concentrations above their critical micelle concentration. Below their cr...
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The crystal structure of the ternary porcine lipase-colipase-tetra ethylene glycol monooctyl ether (TGME) complex has been determined at 2.8 A resolution. The crystals belong to the cubic space group F23 with a = 289.1 A and display a strong pseudo-symmetry corresponding to a P23 lattice. Unexpectedly, the crystalline two-domain lipase is found in its open configuration. This indicates that in ...
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A monolayer reaction system employing tripropionin and siliconized glass beads was used to study the effects of taurodeoxycholate and colipase on the catalytic activity, interfacial stability, and interfacial affinity of porcine pancreatic lipase B (EC 3.1.1.3) The stability and catalytic activity of lipase at the bead-water interface are governed by the same two ionizable groups with pKa value...
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تاریخ انتشار 1997