Anatomy of lipase binding sites: The scissile fatty acid binding site

Chemistry and Physics of Lipids

Volumn 93, Issue 1-2, 1998, Pages 67-80

  Pleiss, Jürgen ^a   Fischer, Markus ^a   Schmid, Rolf D ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

Author keywords

Chain length specificity; Esterase; Modeling; Mutant; Protein engineering; Structure

Indexed keywords

FATTY ACID; SERINE PROTEINASE; TRIACYLGLYCEROL LIPASE;

CANDIDA; CANDIDA RUGOSA; CATALYSIS; CONFERENCE PAPER; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS; RHIZOPUS;

CANDIDA; CANDIDA ANTARCTICA; CANDIDA RUGOSA; MAMMALIA; PSEUDOMONAS; RHIZOMUCOR MIEHEI; RHIZOPUS;

EID: 0032103791     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-3084(98)00030-9     Document Type: Conference Paper

References (43)

1. Adlercreutz P. On the importance of the support material for enzymatic synthesis in organic media. Support effects at controlled water activity. Eur. J. Biochem. 199:1991;609-614.
2. Atomi, H., Bornscheuer, U, Soumanou, M.M., Beer, H.D., Wohlfahrt, G., Schmid, R.D., 1996. Microbial lipases-from screening to design. In: Oils-Fats-Lipids, Proceedings of the Twenty-first World Congress of the International Society on Fat Research, PJ Barnes and Associates, Bridgewater, pp. 49-50.
3. Bairoch A., Boeckmann B. The SWISS-PROT protein sequence data bank. Nucleic Acids Res. 19:1991;2247-2249.
4. Berger M., Schneider M.P. Lipases in organic solvents: The fatty acid chain length profile. Biotechnol. Lett. 13:1991;641-645.
5. Bernstein F.C., Koetzle T.F., Williams G.J., Meyer E.E. Jr., Brice M.D., Rodgers J.R., Kennard O., Shimanouchi T., Tasumi M. The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112:1977;535-542.
6. 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.
7. Connolly M.L. Solvent-accessible surfaces of proteins and nucleic acids. Science. 221:1983;709-713.
8. Cygler M., Grochulski P., Kazlauskas R.J., Schrag J.D., Bouthillier F., Rubin B., Serreqi A.N., Gupta A.K. A structural basis for the chiral preferences of lipases. J. Am. Chem. Soc. 116:1994;3180-3186.
9. Derewenda U., Brzozowski A.M., Lawson D.M., Derewenda Z.S. Catalysis at the interface: The anatomy of a conformational change in a triglyceride lipase. Biochemistry. 31:1992;1532-1541.
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. Ferri S.R., Meighen E.A. A lux-specific myristoyl transferase in luminescent bacteria related to eukaryotic serine esterases. J. Biol. Chem. 266:1991;12852-12857.
12. Goodford P.J. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28:1985;849-857.
13. Grochulski P., Bouthillier F., Kazlauskas R.J., Serreqi A.N., Schrag J.D., Ziomek E., Cygler M. Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase. Biochemistry. 33:1994;3494-3500.
14. Haalck, L., Paltauf, F., Pleiss, J., Schmid, R.D., Spener, F., Stadler, P., 1997. Stereoselectivity of lipase from Rhizopus oryzae towards triacylglycerols and analogs: computer aided modeling and experimental validation, Methods Enzymol. Lipases 284 (in press).
15. Halling P.J. Thermodynamic predictions for biocatalysis in nonconventional media: theory, tests and recommendations for experimental design and analysis. Enzyme Microbiol. Technol. 16:1994;178-206.
16. Harel M., Quinn D.M., Nair H.K., Silman I., Sussman J.L. The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. J. Am. Chem. Soc. 118:1996;2340-2346.
17. Hecht H.J., Sobek H., Haag T., Pfeifer O., van Pee K.H. The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold. Nat. Struct. Biol. 1:1994;532-537.
18. Holzwarth H.-C., Pleiss J., Schmid R.D. Computer-aided modeling of stereoselective triglyceride hydrolysis catalyzed by Rhizopus oryzae lipase. J. Mol. Catal. B: Enzym. 3:1997;73-82.
19. Joerger R.D., Haas M.J. Alteration of chain length selectivity of a Rhizopus delemar lipase through site-directed mutagenesis. Lipids. 29:1994;377-384.
20. Kirk O., Bjoerkling F., Godtfredsen S.E., Larsen T.O. Fatty acid specificity in lipase-catalyzed synthesis of glucoside esters. Biocatalysis. 6(2):1992;127-134.
21. Klein R.R., King G., Moreau R.A., Haas M.J. Altered acyl chain length specificity of Rhizopus delemar lipase through mutagenesis and molecular modeling. Lipids. 32:1997;123-130.
22. Lawson D.M., Derewenda U., Serre L., Ferri S., Szittner R., Wei Y., Meighen E.A., Derewenda Z.S. Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi. Biochemistry. 33:1994;9382-9388.
23. Lawson D.M., Brzozowski A.M., Rety S., Vemag C., Dodson G.G. Probing the nature of substrate binding in Humicola lanuginosa lipase through X-ray crystallography and intuitive modelling. Protein Eng. 7:1994;543-550.
24. Longhi S., Nicolas A., Creveld L., Egmond M., Verrips C.T., de Vlieg J., Martinez C., Cambillau C. Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants. Proteins. 26:1996;442-458.
25. Mannesse M.L., Cox R.C., Koops B.C., Verheij H.M., de Haas G.H., Egmond M.R., van der Hijden H.T., de Vlieg J. Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity. Biochemistry. 34:1995;6400-6407.
26. Martinelle M., Holmquist M., Clausen I.G., Patkar S., Svendsen A., Hult K. The role of Glu87 and Trp89 in the lid of Humicola lanuginosa lipase. Protein Eng. 9:1996;519-524.
27. 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.
28. Murzin A.G., Brenner S.E., Hubbard T., Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;536-540.
29. Norin M., Haeffner F., Achour A., Norin T., Hult K. Computer modeling of substrate binding to lipases from Rhizomucor miehei, Humicola lanuginosa and Candida rugosa. Protein Sci. 3:1994;1493-1503.
30. Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J. et al. The alpha/beta hydrolase fold. Protein Eng. 5:1992;197-211.
31. Pathak D., Ollis D. Refined structure of dienelactone hydrolase at 1.8 Å J. Mol. Biol. 214:1990;497-525.
32. Pleiss, J., Mionetto, N., Schmid, R.D., 1998. Improving insecticide binding of acetylcholinesterase by protein engineering, Biochim. Biophys. Acta submitted.
33. Rangheard M.S., Langrand G., Triantaphylides C., Baratti J. Multi-competitive enzymatic reactions in organic media: a simple test for the determination of lipase fatty acid specificity. Biochim. Biophys. Acta. 1004:1989;20-28.
34. Sarda L., Desnuelle P. Action de la lipase pancréatique sur les esters en émulsion. Biochim. Biophys. Acta. 30:1958;513-521.
35. Schmid, R.D., Verger, R., 1998. Lipases: interfacial enzymes with attractive applications, Angew. Chem. in press.
36. Schonheyder F., Volqvartz K. On the affinity of pig pancreas lipase for tricaproin in heterogeneous solution. Acta Physiol. Scand. 9:1945;57-67.
37. Schrag J.D., Li Y., Cygler M., Lang D., Burgdorf T., Hecht H.J., Schmid R., Schomburg D., Rydel T.J., Oliver J.D., Strickland L.C., Dunaway C.M., Larson S.B., Day J., McPherson A. The open conformation of a Pseudomonas lipase. Structure. 5:1997;187-202.
38. Sussman J.L., 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.
39. Uppenberg J., Ohrner N., Norin M., Hult K., Kleywegt G.J., Patkar S., Waagen V., Anthonsen T., Jones T.A. Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols. Biochemistry. 34:1995;16838-16851.
40. Vasel B., Hecht H.J., Schmid R.D., Schomburg D. 3D-structures of the lipase from Rhizomucor miehei at different temperatures and computer modelling of a complex of the lipase with trilaurylglycerol. J. Biotechnol. 28:1993;99-105.
41. Verger R. Interfacial activation of lipases: facts and artifacts. Trends Biotechnol. 15:1997;32-38.
42. Wei Y., Schottel J.L., Derewenda U., Swenson L., Patkar S., Derewenda Z.S. A novel variant of the catalytic triad in the Streptomyces scabies esterase. Nat. Struct. Biol. 2:1995;218-223.
43. Woolley, P., Petersen, S.B. (Eds.), Lipases: Their Structure, Biochemistry and Application. Cambridge University Press, Cambridge, 1994.