Jayne S

References (4)

Title : Crystallization of a proteolyzed form of the horse pancreatic lipase-related protein 2: structural basis for the specific detergent requirement - Mancheno_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_2107
Author(s) : Mancheno JM , Jayne S , Kerfelec B , Chapus C , Crenon I , Hermoso JA
Ref : Acta Crystallographica D Biol Crystallogr , 60 :2107 , 2004
Abstract : Horse pancreatic lipase-related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence-comparison analyses reveal that the three proteins possess the same two-domain organization: an N-terminal catalytic domain and a C-terminal domain, which in PL is involved in colipase binding. Nevertheless, despite the high level of sequence identity found, they exhibit distinct enzymatic properties. The intrinsic sensitivity of the peptide bond between Ser245 and Thr246 within the flap region of PLRP2 to proteolytic cleavage probably complicates PLRP2 crystallization since, as shown here, this proteolyzed form of PLRP2 is only crystallized after specific detergent stabilization of this region. This has been performed by the hanging-drop vapour-diffusion method at 291 K and exclusively in the presence of N,N-dimethyldecylamine-beta-oxide (DDAO). However, most crystals (>95%) are highly twinned and diffract poorly (to approximately 7-5 A resolution). Diffraction-quality trigonal crystals have unit-cell parameters a = b = 128.4, c = 85.8 A and belong to space group P3(2)21. A 2.9 A native data set was collected at ESRF on beamline ID14-2 with an R(merge) of 12.7%. Preliminary structural analysis provides a structural basis for the specific roles of DDAO.
ESTHER : Mancheno_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_2107
PubMedSearch : Mancheno_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_2107
PubMedID: 15502342
Gene_locus related to this paper: horse-2plrp

Title : Activation of horse PLRP2 by bile salts does not require colipase. - Jayne_2002_Biochemistry_41_8422
Author(s) : Jayne S , Kerfelec B , Foglizzo E , Granon S , Hermoso J , Chapus C , Crenon I
Ref : Biochemistry , 41 :8422 , 2002
Abstract : Although structurally similar to pancreatic lipase (PL), the key enzyme of intestinal fat digestion, pancreatic lipase-related protein type 2 (PLRP2) differs from PL in certain functional properties. Notably, PLRP2 has a broader substrate specificity than PL, and unlike that of PL, its activity is not restored by colipase in the presence of bile salts. In the studies presented here, the activation mechanism of horse PLRP2 was studied through active site-directed inhibition experiments, and the results demonstrate fundamental differences with that of PL. The opening of the horse PLRP2 flap occurs as soon as bile salt monomers are present, is accelerated in the presence of micelles, and does not require the presence of colipase. Moreover, in contrast to PL, horse PLRP2 is able to directly interact with a bile salt micelle to form an active binary complex, without the micelle being presented by colipase, as evidenced by molecular sieving experiments. These findings, together with the sensitivity of the horse PLRP2 flap to partial proteolysis, are indicative of a higher flexibility of the flap of horse PLRP2 relative to PL. From these results, it can be concluded that PLRP2 can adopt an active conformation in the intestine, which could be important for the further understanding of the physiological role of PLRP2. Finally, this work emphasizes the essential role of colipase in lipase catalysis at the lipid-water interface in the presence of bile.
ESTHER : Jayne_2002_Biochemistry_41_8422
PubMedSearch : Jayne_2002_Biochemistry_41_8422
PubMedID: 12081491
Gene_locus related to this paper: horse-2plrp

Title : High expression in adult horse of PLRP2 displaying a low phospholipase activity. -
Author(s) : Jayne S , Kerfelec B , Foglizzo E , Chapus C , Crenon I
Ref : Biochimica & Biophysica Acta , 1594 :255 , 2002
PubMedID: 11904221
Gene_locus related to this paper: horse-2plrp

Title : Pancreatic lipase-related protein type 1: a double mutation restores a significant lipase activity - Crenon_1998_Biochem.Biophys.Res.Commun_246_513
Author(s) : Crenon I , Jayne S , Kerfelec B , Hermoso J , Pignol D , Chapus C
Ref : Biochemical & Biophysical Research Communications , 246 :513 , 1998
Abstract : Besides the active pancreatic lipase (PL) which plays a major role in dietary fat digestion, the presence of a pancreatic lipase related protein 1 (PLRP1) displaying a very low lipolytic activity has been reported in vertebrates. It has been suggested that the reduced lipolytic activity of PLRP1 results from specific features of the N-terminal domain of the protein. Therefore, based on sequence comparison between PL and PLRP1 and modelling experiments, several residues located in the vicinity of the active site pocket of both enzymes have been mutated. In this paper, we report that, as regards to PL, two substitutions in positions 179 and 181 in PLRP1 account for the very low lipolytic activity of the protein. Indeed, substituting these residues (V179 and A181) in PLRP1 for those found in PL (A179 and P181), restores a significant lipolytic activity for PLRP1.
ESTHER : Crenon_1998_Biochem.Biophys.Res.Commun_246_513
PubMedSearch : Crenon_1998_Biochem.Biophys.Res.Commun_246_513
PubMedID: 9610393
Gene_locus related to this paper: human-PNLIPRP1