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Volumn 105, Issue 10, 2003, Pages 590-600

The role of pancreatic lipase C2-like domain in enzyme interaction with a lipid-water interface

Author keywords

C2 domain; Interfacial enzymology; Lipase; Lipidomics; Lipolysis; Protein lipid interactions

Indexed keywords

COLIPASE; LIPID; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; PERFORIN; PHOSPHATIDYLINOSITIDE; PHOSPHOLIPASE A2; PHOSPHOLIPASE C; PHOSPHOLIPID; POLYPEPTIDE; PROTEIN KINASE C; SYNAPTOTAGMIN; TRIACYLGLYCEROL LIPASE; TRIOCTANOIN; WATER;

EID: 0242266580     PISSN: 14387697     EISSN: None     Source Type: Journal    
DOI: 10.1002/ejlt.200300809     Document Type: Conference Paper
Times cited : (4)

References (48)
  • 1
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase
    • F. K. Winkler, A. d'Arcy, W. Hunziker: Structure of human pancreatic lipase. Nature 343 (1990) 771-774.
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.K.1    D'Arcy, A.2    Hunziker, W.3
  • 2
    • 0026687923 scopus 로고
    • Structure of the pancreatic lipase-procolipase complex
    • H. van Tilbeurgh, L. Sarda, R. Verger, C. Cambillau: Structure of the pancreatic lipase-procolipase complex. Nature 359 (1992) 159-162.
    • (1992) Nature , vol.359 , pp. 159-162
    • Van Tilbeurgh, H.1    Sarda, L.2    Verger, R.3    Cambillau, C.4
  • 3
    • 0033609039 scopus 로고    scopus 로고
    • Human pancreatic lipase: Colipase dependence and interfacial binding of lid domain mutants
    • S. Bezzine, F. Ferrato, M. G. Ivanova, V. Lopez, R. Verger, F. Carriere: Human pancreatic lipase: colipase dependence and interfacial binding of lid domain mutants. Biochemistry 38 (1999) 5499-5510.
    • (1999) Biochemistry , vol.38 , pp. 5499-5510
    • Bezzine, S.1    Ferrato, F.2    Ivanova, M.G.3    Lopez, V.4    Verger, R.5    Carriere, F.6
  • 4
    • 0027200087 scopus 로고
    • Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-Ray crystallography
    • H. van Tilbeurgh, M.-P. Egloff, C. Martinez, N. Rugani, R. Verger, C. Cambillau: Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-Ray crystallography. Nature 362 (1993) 814-820.
    • (1993) Nature , vol.362 , pp. 814-820
    • Van Tilbeurgh, H.1    Egloff, M.-P.2    Martinez, C.3    Rugani, N.4    Verger, R.5    Cambillau, C.6
  • 5
    • 0029161231 scopus 로고
    • The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate
    • M.-P. Egloff, F. Marguet, G. Buono, R. Verger, C. Cambillau, H. van Tilbeurgh: The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Biochemistry 34 (1995) 2751-2762.
    • (1995) Biochemistry , vol.34 , pp. 2751-2762
    • Egloff, M.-P.1    Marguet, F.2    Buono, G.3    Verger, R.4    Cambillau, C.5    Van Tilbeurgh, H.6
  • 6
    • 0037137122 scopus 로고    scopus 로고
    • The beta 5′ loop of the pancreatic lipase C2-like domain plays a critical role in the lipase-lipid interactions
    • H. Chahinian, S. Bezzine, F. Ferrato, M. G. Ivanova, B. Perez, M. E. Lowe, F. Carriere: The beta 5′ loop of the pancreatic lipase C2-like domain plays a critical role in the lipase-lipid interactions. Biochemistry 41 (2002) 13725-13735.
    • (2002) Biochemistry , vol.41 , pp. 13725-13735
    • Chahinian, H.1    Bezzine, S.2    Ferrato, F.3    Ivanova, M.G.4    Perez, B.5    Lowe, M.E.6    Carriere, F.7
  • 7
    • 0345563250 scopus 로고    scopus 로고
    • Human pancreatic lipase: An exposed hydrophobic loop from the C-terminal domain may contribute to interfacial binding
    • S. Bezzine, F. Carrière, J. De Caro, R. Verger, A. De Caro: Human pancreatic lipase: An exposed hydrophobic loop from the C-terminal domain may contribute to interfacial binding. Biochemistry 37 (1998) 11846-11855.
    • (1998) Biochemistry , vol.37 , pp. 11846-11855
    • Bezzine, S.1    Carrière, F.2    De Caro, J.3    Verger, R.4    De Caro, A.5
  • 8
    • 0034236239 scopus 로고    scopus 로고
    • The C-terminal domain of pancreatic lipase: Functional and structural analogies with c2 domains
    • H. Chahinian, B. Sias, F. Carriere: The C-terminal domain of pancreatic lipase: functional and structural analogies with c2 domains. Curr. Protein. Pept. Sci. 1 (2000) 91-103.
    • (2000) Curr. Protein. Pept. Sci. , vol.1 , pp. 91-103
    • Chahinian, H.1    Sias, B.2    Carriere, F.3
  • 10
    • 0033546322 scopus 로고    scopus 로고
    • Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest
    • A. Roussel, S. Canaan, M. P. Egloff, M. Riviere, L. Dupuis, R. Verger, C. Cambillau: Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J. Biol. Chem. 274 (1999) 16995-17002.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16995-17002
    • Roussel, A.1    Canaan, S.2    Egloff, M.P.3    Riviere, M.4    Dupuis, L.5    Verger, R.6    Cambillau, C.7
  • 11
    • 0027435346 scopus 로고
    • The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
    • M. E. M. Noble, A. Cleasby, L. N. Johnson, M. R. Egmond, L. G. J. Frenken: The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett. 331 (1993) 123-128.
    • (1993) FEBS Lett. , vol.331 , pp. 123-128
    • Noble, M.E.M.1    Cleasby, A.2    Johnson, L.N.3    Egmond, M.R.4    Frenken, L.G.J.5
  • 12
    • 0026432669 scopus 로고
    • Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum
    • J. D. Schrag, Y. Li, S. Wu, M. Cygler: Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature 351 (1991) 761-764.
    • (1991) Nature , vol.351 , pp. 761-764
    • Schrag, J.D.1    Li, Y.2    Wu, S.3    Cygler, M.4
  • 13
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
    • C. Martinez, P. de Geus, M. Lauwereys, G. Matthyssens, C. Cambillau: Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356 (1992) 615-618.
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    De Geus, P.2    Lauwereys, M.3    Matthyssens, G.4    Cambillau, C.5
  • 15
    • 0028129833 scopus 로고
    • Lipoprotein lipase. Molecular model based on the pancreatic lipase x- Ray structure: Consequences for heparin binding and catalysis
    • H. van Tilbeurgh, A. Roussel, J. M. Lalouel, C. Cambillau: Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis. J. Biol. Chem. 269 (1994) 4626-4633.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4626-4633
    • Van Tilbeurgh, H.1    Roussel, A.2    Lalouel, J.M.3    Cambillau, C.4
  • 18
    • 0031019017 scopus 로고    scopus 로고
    • Serine phospholipid-specific phospholipase a that is secreted from activated platelets. A new member of the lipase family
    • T. Sato, J. Aoki, Y. Nagai, N. Dohmae, K. Takio, T. Doi, H. Arai, K. Inoue: Serine phospholipid-specific phospholipase A that is secreted from activated platelets. A new member of the lipase family. J. Biol. Chem. 272 (1997) 2192-2198.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2192-2198
    • Sato, T.1    Aoki, J.2    Nagai, Y.3    Dohmae, N.4    Takio, K.5    Doi, T.6    Arai, H.7    Inoue, K.8
  • 19
    • 0033574428 scopus 로고    scopus 로고
    • An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans
    • Y. Nagai, J. Aoki, T. Sato, K. Amano, Y. Matsuda, H. Arai, K. Inoue: An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans. J. Biol. Chem. 274 (1999) 11053-11059.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11053-11059
    • Nagai, Y.1    Aoki, J.2    Sato, T.3    Amano, K.4    Matsuda, Y.5    Arai, H.6    Inoue, K.7
  • 23
    • 0026665148 scopus 로고
    • Mapping of the epitope on lipoprotein lipase recognized by a monoclonal antibody (5D2) which inhibits lipase activity
    • M. S. Liu, Y. Ma, M. R. Hayden, J. D. Brunzell: Mapping of the epitope on lipoprotein lipase recognized by a monoclonal antibody (5D2) which inhibits lipase activity. Biochim. Biophys. Acta 1128 (1992) 113-115.
    • (1992) Biochim. Biophys. Acta , vol.1128 , pp. 113-115
    • Liu, M.S.1    Ma, Y.2    Hayden, M.R.3    Brunzell, J.D.4
  • 24
    • 0031030859 scopus 로고    scopus 로고
    • Mutation of tryptophan residues in lipoprotein lipase. Effects on stability, immunoreactivity, and catalytic properties
    • A. Lookene, N. B. Groot, J. J. P. Kastelein, G. Olivecrona, T. Bruin: Mutation of tryptophan residues in lipoprotein lipase. Effects on stability, immunoreactivity, and catalytic properties. J. Biol. Chem. 272 (1997) 766-772.
    • (1997) J. Biol. Chem. , vol.272 , pp. 766-772
    • Lookene, A.1    Groot, N.B.2    Kastelein, J.J.P.3    Olivecrona, G.4    Bruin, T.5
  • 25
    • 0027401019 scopus 로고
    • Chymotryptic cleavage of lipoprotein lipase. Identification of cleavage sites and functional studies of the truncated molecule
    • A. Lookene, G. Bengtsson-Olivecrona: Chymotryptic cleavage of lipoprotein lipase. Identification of cleavage sites and functional studies of the truncated molecule. Eur. J. Biochem. 213 (1993) 185-194.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 185-194
    • Lookene, A.1    Bengtsson-Olivecrona, G.2
  • 26
    • 0030736867 scopus 로고    scopus 로고
    • The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
    • S. A. Gillmor, A. Villasenor, R. Fletterick, E. Sigal, M. F. Browner: The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity. Nat. Struct. Biol. 4 (1997) 1003-1009.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 1003-1009
    • Gillmor, S.A.1    Villasenor, A.2    Fletterick, R.3    Sigal, E.4    Browner, M.F.5
  • 28
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • E. A. Nalefski, J. J. Falke: The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5 (1996) 2375-2390.
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 29
    • 0032568662 scopus 로고    scopus 로고
    • C2-domains, structure and function of a universal Ca2+-binding domain
    • J. Rizo, T. C. Südhof: C2-domains, structure and function of a universal Ca2+-binding domain. J. Biol. Chem. 273 (1998) 15879-15882.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15879-15882
    • Rizo, J.1    Südhof, T.C.2
  • 30
    • 0022504365 scopus 로고
    • Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signalling pathways
    • L. Coussens, P. J. Parker, L. Rhee, T. L. Yang-Feng, E. Chen, M. D. Waterfield, U. Francke, A. Ullrich: Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signalling pathways. Science 233 (1986) 859-866.
    • (1986) Science , vol.233 , pp. 859-866
    • Coussens, L.1    Parker, P.J.2    Rhee, L.3    Yang-Feng, T.L.4    Chen, E.5    Waterfield, M.D.6    Francke, U.7    Ullrich, A.8
  • 31
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: A novel Ca2+/phospholipid-binding fold
    • R. B. Sutton, B. A. Davletov, A. M. Berghuis, T. C. Südhof, S. R. Sprang: Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell 80 (1995) 929-938.
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Südhof, T.C.4    Sprang, S.R.5
  • 32
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • L. O. Essen, O. Perisic, R. Cheung, M. Katan, R. L. Williams: Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature 380 (1996) 595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 33
    • 0032533457 scopus 로고    scopus 로고
    • Structure of the proteine kinase C-β phospholipid-binding C2 domain complexed with Ca2+
    • R. B. Sutton, S. R. Sprang: Structure of the proteine kinase C-β phospholipid-binding C2 domain complexed with Ca2+. Structure 6 (1998) 1395-1405.
    • (1998) Structure , vol.6 , pp. 1395-1405
    • Sutton, R.B.1    Sprang, S.R.2
  • 35
    • 0031892519 scopus 로고    scopus 로고
    • Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2
    • O. Perisic, S. Fong, D. E. Lynch, M. Bycroft, R. L. Williams: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J. Biol. Chem. 273 (1998) 1596-1604.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1596-1604
    • Perisic, O.1    Fong, S.2    Lynch, D.E.3    Bycroft, M.4    Williams, R.L.5
  • 36
    • 0033591353 scopus 로고    scopus 로고
    • Mapping the phospholipid-binding surface and translocation determinants of the C2 domain from cytosolic phospholipase A2
    • O. Perisic, H. F. Paterson, G. Mosedale, S. Lara-Gonzalez, R. L. Williams: Mapping the phospholipid-binding surface and translocation determinants of the C2 domain from cytosolic phospholipase A2. J. Biol. Chem. 274 (1999) 14979-14987.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14979-14987
    • Perisic, O.1    Paterson, H.F.2    Mosedale, G.3    Lara-Gonzalez, S.4    Williams, R.L.5
  • 37
    • 0032527312 scopus 로고    scopus 로고
    • Ca2+ binding to synaptotagmin: How many Ca2+ ions bind to the tip of a C2 domain?
    • J. Ubach, X. Zhang, X. Shao, T. Südhof, J. Rizo: Ca2+ binding to synaptotagmin: how many Ca2+ ions bind to the tip of a C2 domain? EMBO J. 17 (1998) 3921-3930.
    • (1998) EMBO J. , vol.17 , pp. 3921-3930
    • Ubach, J.1    Zhang, X.2    Shao, X.3    Südhof, T.4    Rizo, J.5
  • 38
    • 0032497406 scopus 로고    scopus 로고
    • Mechanism of phospholipid binding by the C2A domain of synaptotagmin I
    • X. Zhang, J. Rizo, T. Südhof: Mechanism of phospholipid binding by the C2A domain of synaptotagmin I. Biochemistry 37 (1998) 12395-12403.
    • (1998) Biochemistry , vol.37 , pp. 12395-12403
    • Zhang, X.1    Rizo, J.2    Südhof, T.3
  • 39
    • 0032540860 scopus 로고    scopus 로고
    • Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2
    • G. Y. Xu, T. McDonagh, H. A. Yu, E. A. Nalefski, J. D. Clark, D. A. Cumming: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J. Mol. Biol. 280 (1998) 485-500.
    • (1998) J. Mol. Biol. , vol.280 , pp. 485-500
    • Xu, G.Y.1    McDonagh, T.2    Yu, H.A.3    Nalefski, E.A.4    Clark, J.D.5    Cumming, D.A.6
  • 40
    • 0033536066 scopus 로고    scopus 로고
    • Interfacial membrane docking of cytosolic phospholipase A2 C2 domain using electrostatic potential-modulated spin relaxation magnetic resonance
    • A. Ball, R. Nielsen, M. H. Gelb, B. H. Robinson: Interfacial membrane docking of cytosolic phospholipase A2 C2 domain using electrostatic potential-modulated spin relaxation magnetic resonance. Proc. Natl. Acad. Sci. USA 96 (1999) 6637-6642.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6637-6642
    • Ball, A.1    Nielsen, R.2    Gelb, M.H.3    Robinson, B.H.4
  • 42
    • 0032577067 scopus 로고    scopus 로고
    • Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers
    • E. R. Chapman, A. F. Davis: Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers. J. Biol. Chem. 273 (1998) 13995-14001.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13995-14001
    • Chapman, E.R.1    Davis, A.F.2
  • 43
    • 0347298574 scopus 로고    scopus 로고
    • C2 domain of protein kinase calpha: Elucidation of the membrane docking surface by site-directed fluorescence and spin labeling
    • S. C. Kohout, S. Corbalan-Garcia, J. C. Gomez-Fernandez, J. J. Falke: C2 domain of protein kinase calpha: elucidation of the membrane docking surface by site-directed fluorescence and spin labeling. Biochemistry 42 (2003) 1254-1265.
    • (2003) Biochemistry , vol.42 , pp. 1254-1265
    • Kohout, S.C.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3    Falke, J.J.4
  • 44
    • 0032504259 scopus 로고    scopus 로고
    • Mutagenesis of the C2 domain of protein kinase C-alpha. Differential roles of Ca2+ ligands and membrane binding residues
    • M. Medkova, W. Cho: Mutagenesis of the C2 domain of protein kinase C-alpha. Differential roles of Ca2+ ligands and membrane binding residues. J. Biol. Chem. 273 (1998) 17544-17552.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17544-17552
    • Medkova, M.1    Cho, W.2
  • 45
    • 0037435606 scopus 로고    scopus 로고
    • Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling
    • A. A. Frazier, C. R. Roller, J. J. Havelka, A. Hinderliter, D. S. Cafiso: Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling. Biochemistry 42 (2003) 96-105.
    • (2003) Biochemistry , vol.42 , pp. 96-105
    • Frazier, A.A.1    Roller, C.R.2    Havelka, J.J.3    Hinderliter, A.4    Cafiso, D.S.5
  • 46
    • 0033617291 scopus 로고    scopus 로고
    • Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism
    • A. Dessen, J. Tang, H. Schmidt, M. Stahl, J. D. Clark, J. Seehra, W. S. Somers: Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. Cell 97 (1999) 349-360.
    • (1999) Cell , vol.97 , pp. 349-360
    • Dessen, A.1    Tang, J.2    Schmidt, H.3    Stahl, M.4    Clark, J.D.5    Seehra, J.6    Somers, W.S.7
  • 48
    • 0020382687 scopus 로고
    • Lipid-protein interactions in monolayers
    • R. Verger, F. Pattus: Lipid-protein interactions in monolayers. Chem. Phys. Lipids 30 (1982) 189-227.
    • (1982) Chem. Phys. Lipids , vol.30 , pp. 189-227
    • Verger, R.1    Pattus, F.2


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