Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis

Biological Chemistry

Volumn 380, Issue 7-8, 1999, Pages 993-1000

  Gruber, Karl ^a   Gugganig, Monika ^a,b   Wagner, Ulrike G ^a   Kratky, Christoph ^a  

^a UNIVERSITY OF GRAZ   (Austria)

^b GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

hydrolase fold; Anisotropic refinement; Biocatalysis; Cyanohydrin formation; Enzyme mechanism; Protein crystallography

Indexed keywords

ASPARAGINE; GLUTAMINE; HISTIDINE; HYDROGEN; LYASE; SERINE;

ANISOTROPY; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HIGHER PLANT; NONHUMAN; PRIORITY JOURNAL;

ALDEHYDE-LYASES; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; EUPHORBIACEAE; HYDROGEN; MODELS, MOLECULAR; PROTEIN CONFORMATION;

EMBRYOPHYTA; HEVEA BRASILIENSIS;

EID: 0032847750     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.1999.123     Document Type: Article

References (35)

1. Bauer, M., Griengl, H., and Steiner, W. (1999). Kinetic studies on the enzyme (S)-hydroxynitrile lyase from Hevea brasiliensis using initial rate methods and progress curve analysis. Biotechnol. Bioeng. 62, 20-29.
2. Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer, E.F.J., Brice, M.D., Rodgers, J.R., Kennard, O., Shimanouchi, T., and Tasumi, M. (1977). The protein data bank: A computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
3. Conn, E.E. (1981). Secondary plant products. In: The Biochemistry of Plants: A Comprehensive Treatise, Vol. 7, P.K. Stumpf and E.E. Conn, eds. (London, UK: Academic Press), pp. 479-500.
4. Dauter, Z., Lamzin, V.S., and Wilson, K.S. (1997). The benefits of atomic resolution. Curr. Opin Struct. Biol. 7, 681-688.
5. Effenberger, F. (1994). Synthesis and reactions of optically-active cyanohydrins. Angew. Chem. Int. Ed. Engl. 33, 1555-1564.
6. Engh, R.A., and Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A47, 392-400.
7. Hasslacher, M., Kratky, C., Griengl, H., Schwab, H., and Kohlwein, S.D. (1997). Hydroxynitrile lyase from Hevea brasiliensis: molecular characterization and mechanism of enzyme catalysis. Proteins: Structure, Function and Genetics 27, 438-449.
8. Hickel, A., Hasslacher, M., and Griengl, H. (1996). Hydroxynitrile lyases: Functions and properties. Physiologia Plantarum 98, 891-898.
9. Johnson, D.V., and Griengl, H. (1997). The chemoenzymatic synthesis of (S)-13-hydroxyoctadeca-(9z,11e)-dienoic acid using the hydroxynitrile lyase from Hevea brasiliensis. Tetrahedron 53, 617-624.
10. Johnson, D.V., and Griengl, H. (1999). Biocatalytic applications of hydroxynitrile lyases. Adv. Biochem. Eng. Biotechnol. 63, 31-55.
11. Jones, T.A., Zou, J.Y., Cowan, S., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
12. Klempier, N., Griengl, H., and Hayn, M. (1993). Aliphatic (S)-cyanohydrins by enzyme catalysed synthesis. Tetrahedron Letters 34, 4769-4772.
13. Klempier, N., Pichler, U., and Griengl, H. (1995). Synthesis of α,β-unsaturated (S)-cyanohydrins using the oxynitrilase from Hevea brasiliensis. Tetrahedron Asymmetry 6, 845-848.
14. Kleywegt, G.J., and Brunger, A.T. (1996). Checking your imagination - applications of the free R-value. Structure 4, 897-904.
15. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
16. Kruse, C.G. (1992). Chiral cyanohydrins - Their manufacture and utility as chiral building blocks. In: Chirality in Industry, A.N. Collins, G.N. Sheldrake and J. Crosby, eds. (New York: John Wiley and Sons Ltd), pp. 279-299.
17. Kuhn, P., Knapp, M., Soltis, S.M., Ganshaw, G., Thoene, M., and Bott, R. (1998). The 0.78 Å structure of a serine protease: Bacillus lentus subtilisin. Biochemistry 37, 13446-13452.
18. Kuroki, G.W., and Conn, E.E. (1989). Mandelonitrile lyase from Ximenia americana L: Stereospecificity and lack of flavin prosthetic group. Proc. Natl. Acad. Sci. USA 86, 6978-6981.
19. Langan, P., Lehmann, M., Wilkinson, C., Jogl, G., and Kratky, C. (1999). Neutron Laue diffraction studies on coenzyme cob(II)alamin. Acta Cryst. D55, 51-59.
20. Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
21. Longhi, S., Czjzek, M., Lamzin, V., Nicols, A., and Cambillau, C. (1997). Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: Stereochemical analysis. J. Mol. Biol. 268, 779-799.
22. Merritt, E.A., and Bacon, D.J. (1997). Raster3D: Photorealistic molecular graphics. Meth. Enzymol. 277, 505-524.
23. Moews, P.C., and Kretsinger, R.H. (1975). Refinement of the structure of carp muscle calcium binding parvalbumin by model building and difference Fourier analysis. J. Mol. Biol. 91, 201 -228.
24. Ollis, D.L., Cheah, 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., and Goldman, A. (1992). The α/β hydrolase fold. Protein Eng. 5, 197-211.
25. Otwinowski, Z. (1990). DENZO Data Processing Package. Yale University, New Haven, CT USA.
26. Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst A42, 140-149.
27. Schall, M. (1996). Isolation and characterization of a (S)-hydroxynitrile lyase from Hevea brasiliensis. Ph.D. Thesis, Karl Franzens Universität Graz.
28. Sheldrick, G.M. (1997). SHELXL-97, a program for the refinement of crystal structures from diffraction data. University of Göttingen, Göttingen, Germany.
29. Wagner, U.G., Hasslacher, M., Griengl, H., Schwab, H., and Kratky, C. (1996a). Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure 4, 811-822.
30. Wagner, U.G., Schall, M., Hasslacher, M., Hayn, M., Griengl, H., Schwab, H., and Kratky, C. (1996b). Crystallization and preliminary X-ray diffraction studies of a hydroxynitrile lyase from Hevea brasiliensis. Acta Cryst. D52, 591-593.
31. Wajant, H., and Effenberger, F. (1996). Hydroxynitrile lyases of higher plants. Biol. Chem. 377, 611-617.
32. Wajant, H., and Pfizenmaier, K. (1996). Identification of potential active-site residues in the hydroxynitrile lyase from Manihot esculenta by site-directed mutagenesis. J. Biol. Chem. 271, 25830-25834.
33. Walsh, M.A., Schneider, T.R., Sieker, L.C., Dauter, Z., Lamzin, V.S., and Wilson, K.S. (1998). Refinement of triclinic hen egg-white lysozyme at atomic resolution. Acta Cryst. D54, 522-546.
34. Wharton, C.W. (1998). The serine proteinases. In: Comprehensive Biological Catalysis, Vol. 1, M. Sinnott, ed. (London: Academic Press), pp. 345-379.
35. Zuegg, J., Gruber, K., Gugganig, M., Wagner, U.G., and Kratky, C. (1999). 3D structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis. Prot. Sci., in press.