Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensis

Journal of Biotechnology

Volumn 129, Issue 1, 2007, Pages 87-97

  Gartler, Günter ^a   Kratky, Christoph ^a   Gruber, Karl ^a,b  

^a UNIVERSITY OF GRAZ   (Austria)

^b RESEARCH CENTRE APPLIED BIOCATALYSIS   (Austria)

Author keywords

C C bond formation; Complexes with chiral substrates; Crystal structure analysis; Cyanogenesis; Stereospecificity

Indexed keywords

CONFORMATIONS; COVALENT BONDS; CRYSTAL STRUCTURE; FORESTRY;

CYANOGENESIS; HYDROXYNITRILE LYASE; STEREOSPECIFICITY;

ENZYME KINETICS;

ACETONE; ALDEHYDE; BUTYRONITRILE; CYANOHYDRIN; HYDROXYNITRILE LYASE;

ARTICLE; BIOCATALYST; CHEMICAL REACTION; CRYSTAL STRUCTURE; ENANTIOMER; ENANTIOSELECTIVITY; HEVEA BRASILIENSIS; NONHUMAN; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

ALDEHYDE-LYASES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; HEVEA; MODELS, MOLECULAR; NITRILES; PROTEIN STRUCTURE, SECONDARY; STEREOISOMERISM;

COVALENT BONDS; CRYSTAL STRUCTURE; ENZYMATIC ACTIVITY; HEVEA; MOLECULAR STRUCTURE;

HEVEA BRASILIENSIS;

EID: 33947124469     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.12.009     Document Type: Article

References (45)

1. Bauer M., Griengl H., and Steiner W. Kinetic studies on the enzyme (S)-hydroxynitrile lyase from Hevea brasiliensis using initial rate methods and progress curve analysis. Biotechnol. Bioeng. 62 (1999) 20-29
2. Bauer M., Geyer R., Griengl H., and Steiner W. The use of Lewis cell to investigate the enzyme kinetics of an (S)-hydroxynitrile lyase in two-phase systems. Food Technol. Biotechnol. 40 (2002) 9-19
3. Brünger A.T., Adams P.D., Clore G.M., Delano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., and Warren G.L. Crystallography and NMR system (CNS): a software system for macromolecular structure determination. Acta Crystallogr. D54 (1998) 905-921
4. Buhler H., Effenberger F., Forster S., Roos J., and Wajant H. Substrate specificity of mutants of the hydroxynitrile lyase from Manihot esculenta. Chembiochem 4 (2003) 211-216
5. CCP4. The CCP4 suite-programs for protein crystallography. Acta Crystallogr. D50 (1994) 760-763
6. Cheng I.P., and Poulton J.E. Cloning of cDNA of Prunus serotina (R)-(+)-mandelonitrile lyase and identification of a putative FAD-binding site. Plant Cell Physiol. 34 (1993) 1139-1143
7. Conn E.E. Secondary plant products. In: Conn E.E., and Stumpf P.K. (Eds). The Biochemistry of Plants: A Comprehensive Treatise vol. 7 (1981), Academic Press, New York, NY 479-500
8. Dreveny I., Kratky C., and Gruber K. The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesis. Protein Sci. 11 (2002) 293-300
9. Effenberger F., Forster S., and Wajant H. Hydroxynitrile lyases in stereoselective catalysis. Curr. Opin. Biotechnol. 11 (2000) 532-539
10. Engh R.A., and Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A47 (1991) 392-400
11. Fechter, M.H., Griengl, H., 2002. Enzymatic synthesis of cyanohydrins. Enzyme Catalysis in Organic Synthesis (2nd Edition), 2, 974-989.
12. Fessner W.D. Enzyme mediated C-C bond formation. Curr. Opin. Chem. Biol. 2 (1998) 85-97
13. Glieder A., Weis R., Skranc W., Pöchlauer P., Dreveny I., Majer S., Schwab H., and Gruber K. Comprehensive step-by-step engineering of an (R)-hydroxynitrile lyase for large-scale asymmetric synthesis. Angew. Chem. Int. Ed. 42 (2003) 4815-4818
14. Gregory R.J.H. Cyanohydrins in nature and the laboratory: biology, preparations and synthetic applications. Chem. Rev. 99 (1999) 3649-3682
15. Griengl H., Klempier N., Pochlauer P., Schmidt M., Shi N.Y., and Zabelinskaja-Mackova A.A. Enzyme catalysed formation of (S)-cyanohydrins derived from aldehydes and ketones in a biphasic solvent system. Tetrahedron 54 (1998) 14477-14486
16. Gruber K. Elucidation of the mode of substrate binding to hydroxynitrile lyase from Hevea brasiliensis. Proteins 44 (2001) 26-31
17. Gruber K., Gugganig M., Wagner U.G., and Kratky C. Atomic resolution structure of hydroxynitrile lyase from Hevea brasiliensis. Biol. Chem. 380 (1999) 993-1000
18. Gruber K., Gartler G., Krammer B., Schwab H., and Kratky C. Reaction mechanism of hydroxynitrile lyases of the α/β-hydrolase superfamily: the 3D structure of the transient enzyme-substrate complex certifies the crucial role of Lys236. J. Biol. Chem. 279 (2004) 20501-20510
19. Hasslacher M., Schall M., Hayn M., Griengl H., Kohlwein S.D., and Schwab H. (S)-Hydroxynitrile lyase from Hevea brasiliensis. Ann. N.Y. Acad. Sci. 799 (1996) 707-712
20. Hasslacher M., Schall M., Hayn M., Griengl H., Kohlwein S.D., and Schwab H. Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis functional expression in Escherichia coli and Saccharomyces cerevisiae and identification of an active site residue. J. Biol. Chem. 271 (1996) 5884-5891
21. Hasslacher M., Kratky C., Griengl H., Schwab H., and Kohlwein S.D. Hydroxynitrile lyase from Hevea brasiliensis: molecular characterization and mechanism of enzyme catalysis. Proteins 27 (1997) 438-449
22. Hickel A., Hasslacher M., and Griengl H. Hydroxynitrile lyases: functions and properties. Physiol. Plant 98 (1996) 891-898
23. Hu Z., and Poulton J.E. Sequencing, genomic organization, and preliminary promoter analysis of a black cherry (R)-(+)-mandelonitrile lyase gene. Plant Physiol. 115 (1997) 1359-1369
24. Jones T.A., Zou J.Y., Cowan S., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47 (1991) 110-119
25. Kleywegt G.J., and Brunger A.T. Checking your imagination-applications of the free R-value. Structure 4 (1996) 897-904
26. Kleywegt G.J., and Jones T.A. Model-building and refinement practice. Meth. Enzymol. 277 (1997) 208-230
27. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24 (1991) 946-950
28. Lauble H., Miehlich B., Forster S., Wajant H., and Effenberger F. Mechanistic aspects of cyanogenesis from active-site mutant Ser80Ala of hydroxynitrile lyase from Manihot esculenta in complex with acetone cyanohydrin. Protein Sci. 10 (2001) 1015-1022
29. Lieberei R., Selmar D., and Biehl B. Metabolization of cyanogenic glucosides in Hevea brasiliensis. Plant Syst. Evol. 150 (1985) 49-63
30. Merritt E.A., and Bacon D.J. Raster3D: photorealistic molecular graphics. Meth. Enzymol. 277 (1997) 505-524
31. 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. The α/β hydrolase fold. Protein Eng. 5 (1992) 197-211
32. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276 (1997) 307-326
33. Pöchlauer P. Syntheses of homochiral cyanohydrins in an industrial environment: hydroxynitrile lyases offer new options. Chim. Oggi 16 (1998) 15-19
34. Read R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A42 (1986) 140-149
35. Schmidt M., Herve S., Klempier N., and Griengl H. Preparation of optically-active cyanohydrins using the (S)-hydroxynitrile lyase from Hevea brasiliensis. Tetrahedron 52 (1996) 7833-7840
36. Schwab, H., Steiner, E., Wagner, U., Kratky, C., Effenberger, F., Wajant, H., Bühler, H., Lauble, P., Förster, S., 2000. (S)-Hydroxynitrile lyases with improved substrate acceptance and uses thereof. DSM FINE CHEM AUSTRIA GMBH (AT), European Patent.
37. Selmar D. Apoplastic occurrence of cyanogenic beta-glucosidases and consequences for the metabolism of cyanogenic glucosides. ACS Symp. Ser. 13 (1993) 191-204
38. Stranzl G.R., Gruber K., Steinkellner G., Zangger K., Schwab H., and Kratky C. Observation of a short, strong hydrogen bond in the active site of hydroxynitrile lyase from Hevea brasiliensis explains a large pKa-shift of the catalytic base induced by the reaction intermediate. J. Biol. Chem. 279 (2004) 3699-3707
39. Trummler K., and Wajant H. Molecular cloning of acetone cyanohydrin lyase from flax (Linum usitatissimum) definition of a novel class of hydroxynitrile lyases. J. Biol. Chem. 272 (1997) 4770-4774
40. Wagner U.G., Hasslacher M., Griengl H., Schwab H., and Kratky C. Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure 4 (1996) 811-822
41. Wajant H., and Effenberger F. Hydroxynitrile lyases of higher plants. Biol. Chem. 377 (1996) 611-617
42. Wajant H., and Foerster S. Purification and characterization of hydroxynitrile lyase from Hevea brasiliensis. Plant Sci. 115 (1996) 25-31
43. Wajant H., and Mundry K.W. Hydroxynitrile lyase from Sorghum bicolor: a glycoprotein heterotetramer. Plant Sci. 89 (1993) 127-133
44. Wajant H., and Pfizenmaier K. Identification of potential active-site residues in the hydroxynitrile lyase from Manihot esculenta by site-directed mutagenesis. J. Biol. Chem. 271 (1996) 25830-25834
45. Zuegg J., Gruber K., Gugganig M., Wagner U.G., and Kratky C. Three-dimensional structure of enzyme-substrate complexes of hydroxynitrile lyase from Hevea brasiliensis: implications for the enzymic mechanism. Protein Sci. 8 (1999) 1990-2000