Structural basis of the chiral selectivity of Pseudomonas cepacia lipase

European Journal of Biochemistry

Volumn 254, Issue 2, 1998, Pages 333-340

  Lang, Dietmar A ^a   Mannesse, Maurice L M ^b   De Haas, Gerard H ^b   Verheij, Hubertus M ^b   Dijkstra, Bauke W ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UTRECHT UNIVERSITY   (Netherlands)

Author keywords

Crystal structure; Enantioselectivity; Lipase; Stereospecificity; Transition state analog

Indexed keywords

ANION; ASPARTIC ACID; BACTERIAL ENZYME; DIACYLGLYCEROL; GLUTAMIC ACID; HISTIDINE; PHOSPHONIC ACID DERIVATIVE; SERINE; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE;

ARTICLE; BURKHOLDERIA CEPACIA; CHIRALITY; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; NONHUMAN; PH; PRIORITY JOURNAL; X RAY ANALYSIS;

BACTERIA (MICROORGANISMS); BURKHOLDERIA; BURKHOLDERIA CEPACIA; PSEUDOMONAS; PSEUDOMONAS CEPACIA;

EID: 0032102134     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2540333.x     Document Type: Article

References (43)

1. Bando, T., Namba, Y. & Shishido, K. (1997) Lipase-mediated asymmetric construction of 2-arylpropionic acids: enantiocontrolled syntheses of S-naproxen and S-ibuprofen, Tetrahedron: Asymmetry 8, 2159-2165.
2. Theil, F. (1995) Lipase-supported synthesis of biologically active compounds, Chem. Rev. 95, 2203-2227.
3. Ollis, D. L., Shea, 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. (1992) The α/β hydrolase fold, Protein Eng. 5, 197-211.
4. Brady, L., Brzozowski, A. M., Derewenda, Z. S., Dodson, E., Dodson, G., Tolley, S., Turkenburg, J. P., Christiansen, L., Huge-Jensen, B., Norskov, L., Thim, L. & Menge, U. (1990) A serine protease triad forms the catalytic centre of a triacylglycerol lipase, Nature 343, 767-770.
5. Schrag, J. D., Li, Y., Wu, S. & Cygler, M. (1991) Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum, Nature 351, 761-764.
6. Winkler, F. K., D'Arcy, A. & Hunziker, W. (1990) Structure of human pancreatic lipase, Nature 343, 771-774.
7. Grochulski, P., Li, Y., Schrag, J. D. & Cygler, M. (1994) Two conformational states of Candida rugosa lipase, Protein Sci. 3, 82-91.
8. 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. (1991) A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex, Nature 351, 491-494.
9. Derewenda, U., Brzozowski, A. M., Lawson, D. M. & Derewenda, Z. S. (1992) Catalysis at the interface: the anatomy of a conformational change in a triacylglycerol lipase, Biochemistry 31, 1532-1541.
10. Egloff, M.-P., Marguet, F., Buono, G., Verger, R., Cambillau, C. & van Tilbeurgh, H. (1995) The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate, Biochemistry 34, 2751-2762.
11. Grochulski, P., Li, Y., Schrag, J. D., Bouthillier, F., Smith, P., Harrison, D., Rubin, B. & Cygler, M. (1993) Insights into interfacial activation from an open structure of Candida rugosa lipase, J. Biol. Chem. 268, 12843-12847.
12. van Tilbeurgh, H., Egloff, M.-P., Martinez, C., Rugani, N., Verger, R. & Cambillau, C. (1993) Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography, Nature 362, 814-820.
13. Derewenda, Z. S. (1994) Structure and function of lipases, Adv. Protein Chem. 45, 1-52.
14. Longhi, S., Mannesse, M., Verheij, H. M., de Haas, G. H., Egmond, M., Knoops-Mouthuy, E. & Cambillau, C. (1997) Crystal structure of cutinase covalently inhibited by a triacylglycerol analogue, Protein Sci. 6, 275-286.
15. Kim, K. K., Song, H. K., Shin, D. H., Hwang, K. Y. & Suh, S. W. (1997) The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor, Structure 5, 173-185.
16. 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. (1997) The open conformation of a Pseudomonas lipase, Structure 5, 187-202.
17. Kordel, M., Hofmann, B., Schomburg, D. & Schmid, R. D. (1991) Extracellular lipase of Pseudomonas sp. strain ATCC 21808: purification, characterization, crystallization, and preliminary X-ray diffraction data, J. Bacteriol. 173, 4836-4841.
18. Winkler, U. K. & Stuckmann, M. (1979) Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens, J. Bacteriol. 138, 663-670.
19. Mannesse, M. L. M., Boots, J. W. P., Dijkman, R., Slotboom, A. J., van der Hijden, H. T. W. V., Egmond, M. R., Verheij, H. M. & de Haas, G. H. (1995) Phosphonate analogues of triacylglycerols are potent inhibitors of lipase, Biochim. Biophys. Acta 1259, 56-64.
20. Jancarik, J. & Kim, S. H. (1991) Sparse matrix sampling: a screening method for crystallization of proteins, J. Appl. Crystallogr. 24, 409-411.
21. Matthews, B. W. (1968) Solvent content of protein crystals, J. Mol. Biol. 33, 491-497.
22. Navaza, J. (1994) AMoRe: an automated package for molecular replacement, Acta Crystallogr. A50, 157-163.
23. Brünger, A. T. (1991) Crystallographic phasing and refinement of macromolecules, Curr. Opin. Struct. Biol. 1, 1016-1022.
24. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
25. Nakanishi, Y., Watanabe, H., Washizu, K., Narahashi, Y. & Kurono, Y. (1991) Cloning, sequencing and regulation of the lipase gene from Pseudomonas sp. M-12-33, in Lipases: structure, mechanism and genetic engineering (Alberghina, L., Schmid, R. D. & Verger, R., eds) pp. 263-266, VCH, Weinheim.
26. Gilbert, E. J. (1993) Pseudomonas lipases: biochemical properties and molecular cloning, Enzyme Microb. Technol. 15, 634-645.
27. Bender, M. L. & Wedler, F. C. (1972) Phosphate and carbonate ester 'aging' reactions with α-chymotrypsin, J. Am. Chem. Soc. 94, 2101-2109.
28. Bencsura, A., Enyedy, I. & Kovach, I. M. (1995) Origins and diversity of the aging reaction in phosphonate adducts of serine hydrolase enzymes: what characteristics of the active site do they probe? Biochemistry 34, 8989-8999.
29. Luzzati, V. (1952) Traitement statistique des erreurs dans la détermination des structures cristallines, Acta Crystallogr. 5, 802-810.
30. Cygler, M., Grochulski, P., Kazlauskas, R. J., Schrag, J. D., Bouthillier, F., Rubin, B., Serreqi, A. N. & Gupta, A. K. (1994) A structural basis for the chiral preferences of lipases, J. Am. Chem. Soc. 116, 3180-3186.
31. Noble, M. E. M., Cleasby, A., Johnson, L. N., Egmond, M. R. & Frenken, L. G. J. (1993) The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate, FEBS Lett. 331, 123-128.
32. Lang, D., Hofmann, B., Haalck, L., Hecht, H.-J., Spener, F., Schmid, R. D. & Schomburg, D. (1996) Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 Å resolution, J. Mol. Biol. 259, 704-717.
33. Kovach, I. M., Huhta, D. & Baptist, S. (1991) Active site interactions in hydrated trypsin organophosphate adducts: a yeti molecular mechanics study, J. Mol. Struct. 226, 99-110.
34. Cahn, R. S., Ingold, C. & Prelog, V. (1966) Spezifikation der molekularen chiralität, Angew Chem. 78, 413-447.
35. Pascher, I. (1996) The different conformations of the glycerol region of crystalline acylglycerols, Curr. Opin. Struct. Biol. 6, 439-448.
36. Sundaralingam, M. (1972) Molecular structures and conformations of the phospholipids and sphingomyelins, Ann. N. Y. Acad. Sci. 195, 324-355.
37. IUPAC-IUB Commission on Biochemical Nomenclature (1977) The nomenclature of lipids, Eur. J. Biochem. 79, 11-21.
38. Stadler, P., Kovac, A., Haalck, L., Spener, F. & Paltauf, F. (1995) Stereoselectivity of microbial lipases. The substitution at position sn-2 of triacylglycerol analogs influences the stereoselectivity of different microbial lipases, Eur. J. Biochem. 227, 335-343.
39. Rogalska, E., Cudrey, C., Ferrato, F. & Verger, R. (1993) Stereo-selective hydrolysis of triacylglycerols by animal and microbial lipases, Chirality 5, 24-30.
40. Zandonella, G., Haalck, L., Spener, F., Faber, K., Paltauf, F. & Hermetter, A. (1995) Inversion of lipase stereospecificity for fluorogenic alkyldiacyl glycerols. Effect of substrate solubilization, Eur. J. Biochem. 231, 50-55.
41. Jaeger, K.-E., Ransac, S., Dijkstra, B. W., Colson, C., van Heuvel, M. & Missel, O. (1994) Bacterial lipases, FEMS Microbiol. Rev. 15, 29-63.
42. Esnouf, R. M. (1997) An extensively modified version of Molscript that includes greatly enhanced coloring capabilities, J. Mol. Graph. Modell. 15, 133-138.
43. Connolly, M. L. (1983) Solvent-accessible surfaces of proteins and nucleic acids, Science 221, 709-711.