Acyl glycerol hydrolases: Inhibitors, interface and catalysis

Current Opinion in Structural Biology

Volumn 6, Issue 4, 1996, Pages 449-455

  Cambillau, Christian ^a   Longhi, Sonia ^a   Nicolas, Anne ^a   Martinez, Chrislaine ^a  

^a Centre National de la Recherche Scientifique   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLGLYCEROL LIPASE; ENZYME INHIBITOR; PHOSPHOLIPASE A2;

CATALYSIS; ENZYME STRUCTURE; POINT MUTATION; PRIORITY JOURNAL; REVIEW;

EID: 0030220235     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80108-4     Document Type: Article

References (25)

1. Winkler FK, D'Arcy A, Hunziker W. Structure of human pancreatic lipase. Nature. 343:1990;771-774.
2. Brady L, Brzozowski A, Derewenda ZS, Dodson R, Dodson G, Tolley S, Turkenburg JP, Christiansen L, Huge-Jensen B, Norskov L, et al. Serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature. 343:1990;767-770.
3. Schrag JD, Li Y, Wu S, Cygler M. Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum Candidum. Nature. 351:1991;761-764.
4. Martinez C, de Geus P, Lauwereys M, Matthyssens G, Cambillau C. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature. 356:1992;615-618.
5. 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.
6. Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M. Insights into interfacial activation from an `open' structure of Candida rugosa lipase. J Biol Chem. 268:1993;12843-12847.
7. Noble MEM, Cleasby A, Johnson LN, Egmond MR, Frenken LGJ. The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. Protein Eng. 7:1994;559-562.
8. Derewenda U, Swenson L, Green R, Wei Y, Yamaguchi S, Joerger R, Haas MJ, Derewenda ZS. Current progress in crystallographic studies of new lipases from filamentous fungi. Protein Eng. 7:1994;551-557.
9. Uppenberg J, Hansen MT, Patkar S, Jones TA. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antartica. Structure. 2:1994;293-308.
10. of outstanding interest Ghosh D, Wawrzak Z, Pletner VZ, Li N, Kaiser R, Pangborn W, Jornvall H, Erman M, Duax WL. Structure of uncomplexed and linoleate bound Candida cylindracea cholesterol esterase. Structure. 3:1995;279-288 The structures of uncomplexed and linoleate bound C. cylindracea CE are found to consist of a dimeric association of monomers in which the two hydrophobic active site gorges face each other. The substrate can gain access to the catalytic site through two openings at the dimer interface, without any dissociation of the dimer. The poorly defined cholesterol moiety lies outside the catalytic gorge, whereas the fatty-acid chain is widely embedded in a deep hydrophobic channel.
11. Ollis DL, Chea E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, et al. The α/β hydrolase fold. Protein Eng. 5:1992;197-211.
12. Kraul J. Serine proteases: structure and mechanism of catalysis. Annu Rev Biochem. 46:1977;331-358.
13. Brzozowski AM, Derewenda U, Derewenda ZS, Dodson G, Lawson D, Turkenburg JP. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature. 351:1991;491-494.
14. Derewenda U, Brzozowski AM, Lawson DM, Derewanda ZS. Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. Biochemistry. 31:1992;1532-1541.
15. Grochulski P, Bouthillier F, Kazlauskas RJ, Serregi AN, Schrag JD, Ziomek M, Cygler M. Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase. Biochemistry. 33:1994;3494-3500.
16. van Tilbeurgh H, Egloff MP, 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.
17. of outstanding interest Uppenberg J, Öhrner N, Norin M, Hult K, Kleywegt GJ, Patkar S, Waagen V, Anthonsen T, Jones TA. Crystallographic and molecular-modeling studies of lipase B from Candida antartica reveal a stereospecificity pocket for secondary alcohols. Biochemistry. 34:1995;16838-16851 Two chiral substrates are modeled in the active site of CALB on the basis of the X-ray structures of CALB - Tween 80 and CALB - phosphonate complexes, combined with biochemical restrictions. As a result, a structural explanation is provided for the high degree of stereoselectivity of CALB towards secondary alcohols.
18. of outstanding interest Egloff MP, 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 In the 2.46 Å resolution structure of the ternary LCC complex, the position of the covalently bound phosphonate in the active site is comparable with that of a phospholipid described previously. This structure sheds light on the interaction of its hydrophobic interface with β-octyl glucoside, and on the mode of auto-association of the complex in the crystal, which buries the hydrophobic interfaces at the centre of a tetramer.
19. Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C. Cutinase, a lipolytic enzyme with a preformed oxyanion hole. Biochemistry. 33:1994;83-88.
20. Pancreatic lipase activity on emulsified esters Sarda L, Desnuelle P. Action de la lipase pancréatique sur les esters en émulsion. Biochem Biophys Acta. 30:1958;513-521.
21. Verger R, de Haas GH. Interfacial enzyme kinetics of lipolysis. Annu Rev Biophys Bioeng. 5:1976;77-119.
22. of outstanding interest van den Berg B, Tessari M, Boelens R, Dijkman R, de Haas G, Kaptein R, Verheij H. NMR structures of phospholipase A2 reveal conformational changes during interfacial activation. Nat Struct Biol. 2:1995;402-406 The two NMR structures of PLA2, alone and in the presence of micelles and inhibitor, show the existence of a conformational change in the three first amino-acids between the two states. This segment is disordered in the free structure, but it binds to active-site residues in the inhibited structure. On the basis of these findings, the authors give a structural explanation for the interfacial activation.
23. of outstanding interest Nicolas A, Egmond M, Verrips C T, de Vlieg J, Longhi S, Cambillau C, Martinez C. Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state. Biochemistry. 35:1996;398-410 The results of the kinetic experiments and the structural analysis performed on five cutinase mutants (S42A, N84A, N84L, N84D and N84W) located in the oxyanion hole pocket provide new evidence that Ser42 Oγ is an extra component of the cutinase oxyanion hole, acting in concert with the two main-chain nitrogen atoms of residues 42 and 121.
24. van Tilbeurgh H, Sarda L, Verger R, Cambillau C. Structure of the pancreatic lipase - procolipase complex. Nature. 359:1992;159-162.
25. Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science. 253:1991;872-879.