User menu

A proposed architecture for lecithin cholesterol acyl transferase (LCAT): Identification of the catalytic triad and molecular modeling

Bibliographic reference Peelman, F ; Vinaimont, N ; Verhee, A ; Vanloo, B ; Verschelde, JL ; et. al. A proposed architecture for lecithin cholesterol acyl transferase (LCAT): Identification of the catalytic triad and molecular modeling. In: Protein Science, Vol. 7, no. 3, p. 587-599 (1998)
Permanent URL
  1. Alexandrov, Fast protein fold recognition via sequence structure alignment and contact capacity potentials, 53 (1996)
  2. Altschul Stephen F., Gish Warren, Miller Webb, Myers Eugene W., Lipman David J., Basic local alignment search tool, 10.1016/s0022-2836(05)80360-2
  3. Bonelli, J Lipid Res, 33, 1863 (1992)
  4. Cygler Miroslaw, Schrag Joseph D., Sussman Joel L., Harel Michal, Silman Israel, Gentry Mary K., Doctor Bhupendra P., Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins, 10.1002/pro.5560020309
  5. Egloff Marie-Pierre, Marguet Frank, Buono Gerard, Verger Robert, Cambillau Christian, van Tilbeurgh Herman, The 2.46 .ANG. Resolution Structure of the Pancreatic Lipase-Colipase Complex Inhibited by a C11 Alkyl Phosphonate, 10.1021/bi00009a003
  6. Fischer Daniel, Eisenberg David, Protein fold recognition using sequence-derived predictions, 10.1002/pro.5560050516
  7. Francone Omar L., Evangelista Lolita, Fielding Christopher J., Lecithin-cholesterol acyltransferase: effects of mutagenesis at N-linked oligosaccharide attachment sites on acyl acceptor specificity, 10.1016/0005-2760(93)90110-u
  8. Francone, J Lipid Res, 37, 1609 (1996)
  9. Francone Omar L., Fielding Christopher J., Structure-function relationships in human lecithin:cholesterol acyltransferase. Site-directed mutagenesis at serine residues 181 and 216, 10.1021/bi00106a002
  10. Geourjon C., Deléage G., SOPM: a self-optimized method for protein secondary structure prediction, 10.1093/protein/7.2.157
  11. Ghosh Debashis, Wawrzak Zdzislaw, Pletnev Vladimir Z, Li Naiyin, Kaiser Rudolf, Pangborn Walter, Jörnvall Hans, Erman Mary, Duax William L, Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase, 10.1016/s0969-2126(01)00158-7
  12. Glomset, J Lipid Res, 9, 155 (1968)
  13. Hansson M., Gough S.P., Brody S.S., Structure prediction and fold recognition for the ferrochelatase family of proteins, 10.1002/(sici)1097-0134(199704)27:4<517::aid-prot5>;2-7
  14. Hengstschläger-Ottnad Elke, Kuchler Karl, Schneider Wolfgang J., Chicken Lecithin-Cholesterol Acyltransferase : MOLECULAR CHARACTERIZATION REVEALS UNUSUAL STRUCTURE AND EXPRESSION PATTERN, 10.1074/jbc.270.44.26139
  15. Hide, J Lipid Res, 33, 167 (1992)
  16. Higgins Desmond G., Sharp Paul M., CLUSTAL: a package for performing multiple sequence alignment on a microcomputer, 10.1016/0378-1119(88)90330-7
  17. Hoeg Jeffrey M., Vaisman Boris L., Demosky Stephen J., Meyn Susan M., Talley Glenda D., Hoyt Robert F., Feldman Sanford, Bérard Annie M., Sakai Nao, Wood Douglas, Brousseau Margaret E., Marcovina Santica, Brewer H. Bryan, Santamarina-Fojo Silvia, Lecithin:Cholesterol Acyltransferase Overexpression Generates Hyperalpha-lipoproteinemia and a Nonatherogenic Lipoprotein Pattern in Transgenic Rabbits, 10.1074/jbc.271.8.4396
  18. Hubbard Tim, Tramontano Anna, Update on protein structure prediction: results of the 1995 IRBM workshop, 10.1016/s1359-0278(96)00028-4
  19. Jauhiainen, J Biol Chem, 261, 7032 (1986)
  20. Jauhiainen Matti, Dolphin Peter J., Human Plasma Lecithin:Cholesterol Acyltransferase (LCAT) On the role of essential carboxyl groups in catalysis, Hypercholesterolemia, Hypocholesterolemia, Hypertriglyceridemia, in Vivo Kinetics (1990) ISBN:9781468459067 p.71-75, 10.1007/978-1-4684-5904-3_8
  21. Jauhiainen Matti, Ridgway Neale D., Dolphin Peter J., Aromatic boronic acids as probes of the catalytic site of human plasma lecithin—cholesterol acyltransferase, 10.1016/0005-2760(87)90193-7
  22. Jauhiainen, J Biol Chem, 263, 6525 (1988)
  23. Jonas Ana, Lecithin-cholesterol acyltransferase in the metabolism of high-density lipoproteins, 10.1016/0005-2760(91)90062-m
  24. Jones David T., Miller Robert T., Thornton Janet M., Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing, 10.1002/prot.340230312
  25. Jones D. T., Taylort W. R., Thornton J. M., A new approach to protein fold recognition, 10.1038/358086a0
  26. Karmin O, Hill John S., Pritchard P.Haydn, Role of N-linked glycosylation of lecithin: cholesterol acyltransferase in lipoprotein substrate specificity, 10.1016/0005-2760(94)00183-y
  27. Kitabatake Katsuaki, Piran Uri, Kamio Yoshiyuki, Doi Yukio, Nishida Toshiro, Purification of human plasma lecithin:cholesterol acyltransferase and its specificity towards the acyl acceptor, 10.1016/0005-2760(79)90181-4
  28. Kuivenhoven, J Lipid Res, 38, 191 (1997)
  29. Lee Young-Phil, Adimoolam Shanthi, Liu Ming, Subbaiah Papasani V, Glenn Kevin, Jonas Ana, Analysis of human lecithin–cholesterol acyltransferase activity by carboxyl-terminal truncation, 10.1016/s0005-2760(96)00149-x
  30. Lhose, J Lipid Res, 38, 892 (1997)
  31. Longhi Sonia, Knoops-Mouthuy Edith, Cambillau Christian, Mannesse Maurice, Verheij Hubertus M., De Haas Gerard H., Egmond Maarten, Crystal structure of cutinase covalently inhibited by a triglyceride analogue, 10.1002/pro.5560060202
  32. Martinelle Mats, Holmquist Mats, Clausen Ib Groth, Patkar Shamkant, Svendsen Allan, Hult Karl, The role of Glu87 and Trp89 in the lid of Humicola lanuginosa lipase, 10.1093/protein/9.6.519
  33. Mehta Perdeep K., Heringa Jaap, Argos Patrick, A simple and fast approach to prediction of protein secondary structure from multiply aligned sequences with accuracy above 70%, 10.1002/pro.5560041208
  34. Norin Martin, Haeffner Fredrik, Achour Adnane, Norin Torbjörn, Hult Karl, Computer modeling of substrate binding to lipases fromRhizomucor miehei, Humicola lanuginosa, andCandida rugosa, 10.1002/pro.5560030915
  35. Ollis David L., Cheah Eong, Cygler Miroslaw, Dijkstra Bauke, Frolow Felix, Franken Sybille M., Harel Michal, Remington S. Jamse, Silman Israel, Schrag Joseph, Sussman Joel L., Verschueren Koen H.G., Goldman Adrian, The α/β hydrolase fold, 10.1093/protein/5.3.197
  36. Osuna Joel, Soberon Xavier, Morett Enrique, A proposed architecture for the central domain of the bacterial enhancer-binding proteins based on secondary structure prediction and fold recognition, 10.1002/pro.5560060304
  37. Richardson Jane S., The Anatomy and Taxonomy of Protein Structure, Advances in Protein Chemistry Volume 34 (1981) ISBN:9780120342341 p.167-339, 10.1016/s0065-3233(08)60520-3
  38. Rosseneu, Abstract workshop on “Reverse cholesterol transport.”, 10 (1997)
  39. Rost Burkhard, Sander Chris, Prediction of Protein Secondary Structure at Better than 70% Accuracy, 10.1006/jmbi.1993.1413
  40. Seguret-Mace S., Latta-Mahieu M., Castro G., Luc G., Fruchart J.-C., Rubin E., Denefle P., Duverger N., Potential Gene Therapy for Lecithin-Cholesterol Acyltransferase (LCAT) Deficient and Hypoalphalipoproteinemic Patients With Adenovirus-Mediated Transfer of Human LCAT Gene, 10.1161/01.cir.94.9.2177
  41. Solovyev, Comput Appl Biosci, 10, 661 (1994)
  42. Sorci-Thomas, J Biol Chem, 265, 2665 (1990)
  43. Vanloo Berlinda, Taveirne Josée, Baert Johan, Lorent Geneviève, Lins Laurence, Ruyschaert Jean-Marie, Rosseneu Maryvonne, LCAT activation properties of apo A-I CNBr fragments and conversion of discoidal complexes into spherical particles, 10.1016/0005-2760(92)90316-n
  44. van Tilbeurgh Herman, Egloff Marie-Pierre, Martinez Chrislaine, Rugani Nathalie, Verger Robert, Cambillau Christian, Interfacial activation of the lipase–procolipase complex by mixed micelles revealed by X-ray crystallography, 10.1038/362814a0
  45. van Tilbeurgh Herman, Sarda Louis, Verger Robert, Cambillau Christian, Structure of the pancreatic lipase–procolipase complex, 10.1038/359159a0
  46. Vasel Birger, Hecht Hans-Jürgen, Schmid Rolf Dieter, Schomburg Dietmar, 3D-Structures of the lipase from Rhizomucor miehei at different temperatures and computer modelling of a complex of the lipase with trilaurylglycerol, 10.1016/0168-1656(93)90128-a
  47. Vercaemst R., Union A., Rosseneu M., Separation and quantitation of free cholesterol and cholesteryl esters in a macrophage cell line by high-performance liquid chromatography, 10.1016/s0378-4347(00)82655-9
  48. Verhasselt Peter, Aert Rita, Voet Marleen, Volckaert Guido, XIV. Yeast sequencing reports. Twelve open reading frames revealed in the 23·6 kb segment flanking the centromere on theSaccharomyces cerevisiae chromosome XIV right arm, 10.1002/yea.320101013
  49. Wang Jingchuan, Gebre Abraham K., Anderson Richard A., Parks John S., Amino Acid Residue 149 of Lecithin:Cholesterol Acyltransferase Determines Phospholipase A2and Transacylase Fatty Acyl Specificity, 10.1074/jbc.272.1.280
  50. Wilmot C.M., Thornton J.M., Analysis and prediction of the different types of β-turn in proteins, 10.1016/0022-2836(88)90103-9
  51. Winkler F. K., D'Arcy A., Hunziker W., Structure of human pancreatic lipase, 10.1038/343771a0
  52. Yang, J Biol Chem, 262, 3086 (1987)