An inactive pancreatic lipase-related protein is activated into a triglyceride-ligase by mutagenesis based on the 3-D structure

Chemistry and Physics of Lipids

Volumn 93, Issue 1-2, 1998, Pages 103-114

  Bezzine, Sofiane ^b   Roussel, Alain ^a   De Caro, Josiane ^b   Gastinel, Louis ^a   De Caro, Alain ^b   Carrière, Frédéric ^b   Leydier, Sabine ^a   Verger, Robert ^b   Cambillau, Christian ^a  

^a Centre National de la Recherche Scientifique   (France)

^b Centre National de la Recherche Scientifique   (France)

Author keywords

Glycerides; Pancreatic juice; Pancreatic lipase; X ray structure

Indexed keywords

ALANINE; COLIPASE; PANCREAS ENZYME; TAURODEOXYCHOLIC ACID; TRIACYLGLYCEROL LIPASE; TRIOCTANOIN; VALINE;

AMINO ACID SUBSTITUTION; CONFERENCE PAPER; DOG; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME STRUCTURE; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; DOGS; ENZYME ACTIVATION; KINETICS; LIPASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION; PANCREATIC JUICE; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; TRIGLYCERIDES;

CANIS FAMILIARIS; INSECTA;

EID: 0032103823     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-3084(98)00034-6     Document Type: Conference Paper

References (35)

1. Andersson L., Carrière F., Lowe M.E., Nilsson A., Verger R. Pancreatic lipase-related protein 2 but the classical pancreatic lipase hydrolyzes galactolipids. Biochim. Biophys. Acta. 1302:1996;236-240.
2. Borgström B., Erlanson-Albertson C. Pancreatic juice colipase: physiological importance. Biochim. Biophys. Acta. 242:1971;509-513.
3. Bourne Y., Martinez C., Kerfelec B., Lombardo D., Chapus C., Cambillau C. Horse pancreatic lipase-the crystal structure refined at 2.3 Å resolution. J. Mol. Biol. 238:1994;709-732.
4. Brünger, A.T., 1992, X-PLOR version 3.1. manual, New Haven, CT, Yale University Press.
5. Brzozowski A.M., Derewenda U., Derewenda Z.S., Dodson G.G., Lawson D.M., Turkenburg J.P., Bjorkling F., Huge-Jensen B., Patkar S.A., Thim L. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature. 351:1991;491-494.
6. Carrière F., Thirstrup K., Boel E., Verger R., Thim L. Structure-function relationships in naturally occurring mutants of pancreatic lipase. Protein Eng. 7:1994;563-569.
7. Carrière F., Thirstrup K., Hjorth S., Ferrato F., Nielsen P.F., Withers-Martinez C., Cambillau C., Boel E., Thim L., Verger R. Pancreatic lipase structure - function relationships by domain exchange. Biochemistry. 36:1997;239-248.
8. Cudrey C., van Tilbeurgh H., Gargouri Y., Verger R. Inactivation of pancreatic lipases by amphiphilic reagents 5-(Dodecyldithio)-2-nitrobenzoic acid and tetrahydrolipstatin. Dependence upon partitioning between micellar and oil phases. Biochemistry. 32:1993;13800-13808.
9. Egloff, M.-P., 1995, Etudes cristallographiques du système lipase pancréatique humaine-colipase et d'une protéine de transport d'acides gras: Thèse de Docteur-Ingénieur thesis, Ph.D. thesis, Université de Paris-Sud.
10. Egloff M.-P., Marguet F., Buono G., Verger R., Cambillau C., van Tilbeurgh H. The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Biochemistry. 34:1995;2751-2762.
11. Giller T., Buchwald P., Blum-Kaelin D., Hunziker W. Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J. Biol. Chem. 267:1992;16509-16516.
12. Grusby M.J., Nabavi N., Wong H., Dick R.F., Bluestone J.A., Schotz M.C., Glimcher L.H. Cloning of an interleukin-4 inducible gene from cytotoxic T lymphocytes and its identification as a lipase. Cell. 60:1990;451-459.
13. Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C., Fontecilla-Camps J.C. Lipase activation by nonionic detergents: the crystal structure of the porcine lipase-colipase tetraethylene glycol monooctyl ether complex. J. Biol. Chem. 271:1996;18007-18016.
14. Higuchi, R., 1992. Principles and applications for DNA amplification. In: PCR Technology.
15. Hjorth A., Carrière F., Cudrey C., Wöldike H., Boel E., Lawson D.M., Ferrato F., Cambillau C., Dodson G.G., Thim L., Verger R. A structural domain (the lid) found in pancreatic lipases is absent in the guinea pig (phospho)lipase. Biochemistry. 32:1993;4702-4707.
16. Jennens M.L., Lowe M.E. Rat GP-3 is a pancreatic lipase with kinetic properties that differ from colipase-dependent pancreatic lipase. J. Lipid Res. 36:1995;2374-2382.
17. Kerfelec B., La Forge K.S., Puigserver A., Scheele G. Primary structures of canine pancreatic lipase and phospholipase A2 messengers RNAs. Pancreas. 1:1986;430-437.
18. Laskowski R.A., MacArthur M.W., Moss D.S., Thorton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:1993;283-291.
19. Mathews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
20. Maylié M.F., Charles M., Gache C., Desnuelle P. Isolation and partial identification of a pancreatic colipase. Biochim. Biophys. Acta. 229:1971;286-289.
21. Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50:1994;157-163.
22. Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J., Sussman J.L., Verschueren K.H.G., Goldman A. The α/β hydrolase fold. Protein Eng. 5:1992;197-211.
23. Otwinovsky, Z., 1993, DENZO: an oscillation data processing program for macromolecular crystallography, New Haven, CT, Yale University Press.
24. Payne M., Sims H., Jennens M., Lowe M. Rat pancreatic lipase and two related proteins: enzymatic properties and mRNA expression during development. Am. J. Physiol. 266:1994;G914-G921.
25. Roussel, A., Cambillau, C., 1991, Turbo-Frodo. In: Graphics, S. (Ed.), Silicon Graphics Geometry Partners Directory, Mountain View, CA, USA, Silicon Graphics, 86.
26. Sarda L., Desnuelle P. Action de la lipase pancréatique sur les esters en émulsion. Biochim. Biophys. Acta. 30:1958;513-521.
27. Thirstrup K., Carrière F., Hjorth S., Rasmussen P.B., Wöldike H., Nielsen P.F., Thim L. One-step purification and characterization of human pancreatic lipase expressed in insect cells. FEBS Lett. 327:1993;79-84.
28. Thirstrup K., Verger R., Carrière F. Evidence for a pancreatic lipase subfamily with new kinetic properties. Biochemistry. 33:1994;2748-2756.
29. Thirstrup K., Carrière F., Hjorth S.A., Rasmussen P.B., Nielsen P.F., Ladefoged C., Thim L., Boel E. Cloning and expression in insect cells of two pancreatic lipases and a procolipase from Myocastor coypus. Eur. J. Biochem. 227:1995;186-193.
30. van Tilbeurgh H., Sarda L., Verger R., Cambillau C. Structure of the pancreatic lipase-procolipase complex. Nature. 359:1992;159-162.
31. van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., Cambillau C. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 362:1993;814-820.
32. Wagner A.C.C., Wishart M.J., Mulders S.M., Blevins P.M., Andrews P.C., Lowe A.W., Williams J.A. GP-3, a newly characterized glycoprotein on the inner surface of the zymogen granule membrane, undergoes regulated secretion. J. Biol. Chem. 269:1994;9099-9104.
33. Winkler F.K., d'Arcy A., Hunziker W. Structure of human pancreatic lipase. Nature. 343:1990;771-774.
34. Wishart M.J., Andrews P.C., Nichols R., Blevins G.T. Jr., Logsdon C.D., Williams J.A. Identification and cloning of GP-3 from rat pancreatic acinar zymogen granules as a glycosylated membrane-associated lipase. J. Biol. Chem. 268:1993;10303-10311.
35. Withers-Martinez C., Carrière F., Verger R., Bourgeois D., Cambillau C. A pancreatic lipase with a phospholipase A1 activity: crystal structure of a chimeric pancreatic lipase-related protein 2 from guinea pig. Structure. 4:1996;1363-1374.