Hydroxynitrile lyase from Hevea brasiliensis: Molecular characterization and mechanism of enzyme catalysis

Proteins: Structure, Function and Genetics

Volumn 27, Issue 3, 1997, Pages 438-449

  Hasslacher, Meinhard ^a   Kratky, Christoph ^b   Griengl, Herfried ^a   Schwab, Helmut ^a   Kohlwein, Sepp D ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b UNIVERSITY OF GRAZ   (Austria)

Author keywords

hydrolase fold; catalytic triad; cyanolysis; heterologous expression; Saccharomyces cerevisiae

Indexed keywords

HYDROLASE; LYASE; NITRILE;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; TREE;

ALDEHYDE-LYASES; AMINO ACID SEQUENCE; BINDING SITES; CONSERVED SEQUENCE; HYDROLASES; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TREES;

HEVEA BRASILIENSIS; SACCHAROMYCES CEREVISIAE;

EID: 0030975258     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199703)27:3<438::AID-PROT11>3.0.CO;2-M     Document Type: Article

References (49)

1. Nahrstedt, A. Cyanogenic compounds as protecting agent for organisms. Plant Syst. Evol. 150:35-47, 1985.
2. Selmar, D. "Cyanogenese in Hevea: Zwei Wege zur Metabolisierung cyanogener Glycoside." Ph.D. thesis, University of Braunschweig, Germany, 1986.
3. Hughes, J., Decarvalho, J., Hughes, M.A. Purification, characterization, and cloning of α-hydroxynitrile lyase from cassava (Manihot esculenta Crantz). Arch. Biochem. Biophys. 311:496-502, 1994.
4. Kruse, C.G. Chiral cyanohydrins: Their manufacture and utility as chiral building blocks. In: "Chirality in Industry." Collins, A.N., Sheldrake, G.N., Crosby, J. (eds.). New York: Wiley, 1992:279-299.
5. Effenberger, F. Synthesis and reactions of optically-active cyanohydrins. Angew. Chem. Int. Ed. 33:1555-1564, 1994.
6. Klempier, N., Griengl, H., Hayn, M. Aliphatic (S)-cyanohydrins by enzyme-catalyzed synthesis. Tetrahedron Lett. 34:4769-4772, 1993.
7. Klempier, N., Pichler, U., Griengl, H. Synthesis of α/β-unsaturated (S)-cyanohydrins using oxynitrilase from Hevea brasiliensis. Tetrahedron Asym. 6:845-848, 1995.
8. Schall, M. "Isolation and Characterization of a (S)-Hydroxynitrile Lyase From Hevea brasiliensis." Ph.D. thesis, University of Graz, Austria, 1996.
9. Hasslacher, M., Schall, M., Hayn, M., Griengl, H., Kohlwein, S.D., Schwab, H. Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis. J. Biol. Chem. 271:5884-5891, 1996.
10. Bove, C., Conn, E.E. Metabolism of aromatic compounds in higher plants. J. Biol. Chem. 236:207-236, 1961.
11. Kuroki, G.W., Conn, E.E. Mandelonitrile lyase from Ximenia americana L.: Stereospecificity and lack of flavin prosthetic group. Proc. Natl. Acad. Sci. USA 86:6978-6981, 1989.
12. Xu, L.L., Singh, B.K., Conn, E.E. Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum. Arch. Biochem. Biophys. 263:256-263, 1988.
13. Wajant, H., Mundry, K.W., Pfizenmaier, K. Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L). Homologies to serine carboxypeptidases. Plant Mol. Biol. 26:735-746, 1994.
14. Cheng, I.P., Poulton, J.E. Cloning of cDNA of Prunus serotina (R)-(+)-mandelonitrile lyase and identification of a putative FAD-binding site. Plant Cell Physiol. 34:1139-1143, 1993.
15. Wajant, H., Mundry, K.W. Hydroxynitrile lyase from Sorghum bicolor: A glycoprotein heterotetramer. Plant Sci. 89:127-133, 1993.
16. Wajant, H., Förster, S., Selmar, D., Effenberger, F., Pfizenmaier, K. Purification and characterization of a novel (R)-mandelonitrile lyase from the fern Phlebodium aureum. Plant Physiol. 109:1231-1238, 1995.
17. Ollis, D.L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S.M., Harel, M., Remington, J.S., Silman, I., Schrag, J., Sussman, J.L., Verschueren, K.H.G., Goldman, A. The α/β hydrolase fold. Prot. Eng. 5:197-211, 1992.
18. Ausubel, F., Brent, R., Kingston, R., Moore, D., Seidman, J., Smith, J., Struhl, K. "Current Protocols in Molecular Biology." New York: Greene Publishing Associates and Wiley-Interscience, 1990.
19. Hill, J.E., Myers, A.M., Koerner, T.J., Tzagloff, A. Yeast/E. coli shuttle vector with multiple unique restriction sites. Yeast 2:163-167, 1986.
20. Kingsman, S.M., Cousens, D., Stanway, C.A., Chambers, A., Wilson, M., Kingsman, A.J. High-efficiency yeast expression vectors based on the promoter of the phosphoglycerate kinase gene. Methods Enzymol. 185:329-341, 1990.
21. Sanger, F., Niklen, S., Coulsen, A.R. DNA Sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467, 1977.
22. Pearson, W.R., Lipman, D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85-2444-2448, 1988.
23. Altschul, S.F., Gish, W., Miller, W., Meyers, E.W. Basic local alignment search tool. J. Mol. Biol. 215:403-410, 1990.
24. Rost, B., Sander, C. Prediction of protein secondary structure better than 70% accurancy. J. Mol. Biol. 232-584-599, 1993.
25. Rao, M.J.K., Argos, P. A conformational preference parameter to predict helices in integral membrane proteins. Biochim. Biophys. Acta 869:197-214, 1986.
26. Klein, P., Kanehisa, M., DeLisi, C. The detection and classification of membrane-spanning proteins. Biochim. Biophys. Acta 815:468-476, 1985.
27. Michael, S.F. Mutagenesis by incorporation of a phosphorylated oligo during PCR amplification. Biotechniques 16:410-412, 1994.
28. Ito, H., Fukuda, Y., Murata, K., Kimura, A. Transformation of intact yeast cells treated with alkali cations. J Bacteriol. 153:163-168, 1983.
29. King, J., Laemmli, U.K. J. Mol. Biol. 62:465-477, 1971.
30. Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. Protein measurement with folin phenol reagent. J. Biol. Chem. 193:265-275, 1951.
31. Reimann, C., Hoffmann, C., Mauch, F., Dudler, R. Characterization of a rice gene induced by Pseudomonas syringae pv. syringae: Requirement for the bacterial lemA gene. Physiol. Mol. Plant Pathol. 46:71-81, 1995.
32. Gribskov, M., McLachlan, A.D., Eisenberg, D. Profile analysis: detection of distantely related proteins. Proc. Natl. Acad. Sci. USA 84:4355-4358, 1987.
33. Sander, C., Schneider, R. Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 9:56-68, 1991.
34. Pearson, W.P. Indentifying distantly related protein sequences. Curr. Opin. Struct. Biol. 1:321-326, 1991.
35. Franken, S.M., Rozeboom, H.J., Kalk, K.H., Dijkstra, B.W. Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes. EMBO J. 10:1297-1302 1991.
36. Hecht, H.J., Sobek, H., Haag, T., Pfeifer, O., van Pee, K-H. The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an α/β hydrolase fold. Struct. Biol. 1:532-537, 1994.
37. Pathak, D., Ollis, D. Refined structure of dienelactone hydrolase at 1.8 Å. J. Mol. Biol. 214:497-525, 1990.
38. Arndt, M., Grant, D.F., Beetham, J.K., Friedberg, T., Oesch, F., Hammock, B.D. Sequence similarity of mammalian epoxide hydrolases to the bacterial haloalkane dehalogenase and other related proteins. FEBS Lett. 338:251-256, 1994.
39. Pinot, F., Grant, D.F., Beetham, J.K., Parker, A.G., Borhan, B., Landt, S., Jones, A.D., Hammock, B.D. Molecular and biochemical evidence for the involvement of the Asp-333-His-523 pair in the catalytic mechanism of soluble epoxide hydrolase. J. Biol. Chem. 270:7968-7974, 1995.
40. Diaz, E., Timmis, K.N. Identification of functional residues in a 2-hydroxymuconic semialdehyde hydrolase. J. Biol. Chem. 270:6403-6411, 1995.
41. Arpigny, J.L., Feller, G., Gerday, C. Cloning, sequence and structural features of a lipase from the antarctic psychrophile Psychrobacter immobilis B10. Biochim. Biophys. Acta 1171:331-333, 1993.
42. Bränden, C.-I. In: "Computer Graphics and Molecular Modelling." Fletterick, R., Zoller, M. (eds.). Cold Spring Harbour, NY: Cold Spring Harbour Laboratory Press, 1986:45-51.
43. Lesk, A.M., Chothia, C. How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins. J. Mol. Biol. 136:225-270, 1980.
44. Lawson, D.M., Derewenda, U., Serre, L., Fern, S., Szittner, R., Wei, Y., Meighen, E.A., Derewenda, Z.S. Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi. Biochemistry 33:9382-9388, 1994.
45. Verschueren, K.H.G., Seljée, F., Rozeboom, H.J., Kalk, K.H., Dijksra, B.W. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363: 693-698, 1993.
46. Cheah, E., Ashley, G.W., Gary, J., Ollis, D. Catalysis by dienlactone hydrolase: A variation on the protease mechanism. Proteins 16:64-78, 1993.
47. Kyte, J., Doolittle, R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132, 1982.
48. Hol, W.G.J., van Duijnen, P.T., Berendsen, II. J.C. The α-helix dipole and the properties of proteins Nature 273: 443-446, 1978.
49. Wagner, U.G., Hasslacher, M., Griengl, H., Schwab, H., Kratky, C. Mechanism of cyanogenesis: The crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Structure 4:811-822, 1996.