The molecular architecture of major enzymes from ajmaline biosynthetic pathway

Phytochemistry Reviews

Volumn 6, Issue 1, 2007, Pages 15-34

  Stöckigt, Joachim ^a,c   Panjikar, Santosh ^b   Ruppert, Martin ^a   Barleben, Leif ^a   Ma, Xueyan ^a   Loris, Elke ^a   Hill, Marco ^a  

^a JOHANNES GUTENBERG UNIVERSITY   (Germany)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c ZHEJIANG UNIVERSITY   (China)

Author keywords

3D structures; Rauvolfia alkaloids; Strictosidine glucosidase; Strictosidine synthase; Vinorine synthase; X ray crystallography

Indexed keywords

AJMALINE; COMPLEMENTARY DNA; INDOLE; SECOLOGANIN; STRICTOSIDINE; SYNTHETASE; TERPENOID; TRYPTAMINE; UNCLASSIFIED DRUG; VINORINE SYNTHASE;

BIOSYNTHESIS; CONFERENCE PAPER; CRYSTALLIZATION; DNA ISOLATION; DNA SEQUENCE; ENZYME SPECIFICITY; ENZYME SYNTHESIS; PRIORITY JOURNAL; PROTEIN ENGINEERING; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

RAUVOLFIA;

EID: 33947384079     PISSN: 15687767     EISSN: 1572980X     Source Type: Journal    
DOI: 10.1007/s11101-006-9016-2     Document Type: Conference Paper

References (54)

1. Barleben L, Ma X, Koepke J, Peng G, Michel H, Stöckigt J (2005) Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons. Biochim Biophys Acta 1747:89-92
2. Bayer A, Ma X, Stöckigt J (2004) Acetyltransfer in natural product biosynthesis - functional cloning and molecular analysis of vinorine synthase. Bioorg Med Chem 12:2787-2795
3. Bracher D, Kutchan TM (1992) Strictosidine synthase from Rauvolfia serpentina: analysis of a gene involved in indole alkaloid biosynthesis. Arch Biochem Biophys 294:717-723
4. Buglino J, Onwueme KC, Ferreras JA, Quadri LEN, Lima CD (2004) Crystal Structure of PapA5, a Phthiocerol Dimycocerosyl Transferase from Mycobacterium tuberculosis. J Biol Chem 279:30634-30642
5. Chrzanowska M, Rozwadowska MD (2004) Asymmetric synthesis of isoquinoline alkaloids. Chem Rev 104:3341-3370
6. Cox ED, Cook JC (1995) The Pictet-Spengler condensation: a new direction for an old reaction. Chem Rev 95:1791-1842
7. Creasey WA (1994) Pharmacology, biochemistry and clinical applications of the monoterpenoid alkaloids. In: Saxton JE (ed) Monoterpenoid Indole Alkaloids, Supplement to part 4. John Wiley & Sons, Chichester, New York, Brisbane, Toronto, Singapore, pp 715-753
8. D'Auria JC (2006) Acyltransferases in plants: a good time to be BAHD. Curr Opin Plant Biol 9:331-340
9. De-Eknamkul W, Ounaroon A, Tanahashi T, Kutchan T, Zenk MH (1997) Phytochemistry 45:477-484
10. De-Eknamkul W, Suttipanta N, Kutchan TM (2000) Purification and characterization of deacetylipecoside synthase from Alangium lamarckii. Thw. Phytochemistry 55:177-181
11. DeLucas LJ, Hamrick D, Cosenza L, Nagy L, McCombs D, Bray T, Chait A, Stoops B, Belgovskiy A, Wilson WW, Parham M, Chernov N (2005) Protein crystallization: virtual screening and optimization. Prog Biophys Mol Biol 88:285-309
12. DeWaal A, Meijer AH, Verpoorte R (1995) Strictosidine synthase from Catharanthus roseus: purification and characterization of multiple forms. Biochem J 306:571-580
13. Edwards TA, Wilkinson BD, Wharton RP, Aggarwal AK (2003) Model of the brain tumor-pumilio translation repressor complex. Genes Dev 17:2508-2513
14. Falbe J, Regitz M (1991) In: RÖMPP Chemie Lexikon, Georg Thieme Verlag Stuttgart-New York, Vol. 4, pp 34-37
15. Geerlings A, Ibanez MM, Memelink J, van Der Heijden R, Verpoorte R. (2000) Molecular cloning and analysis of strictosidine beta-D- glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus. J Biol Chem 275:3051-3056
16. Gerasimenko I, Sheludko Y, Ma X, Stöckigt J (2002) Heterologous expression of a Rauvolfia cDNA encoding strictosidine glucosidase, a biosynthetic key to over 2000 monoterpenoid indole alkaloids. Eur J Biochem 269:2204-2213
17. Gerasimenko I, Ma X, Sheludko Y, Mentele R, Lottspeich F, Stöckigt J (2004) Purification and partial amino acid sequences of the enzyme vinorine synthase involved in a crucial step of ajmaline biosynthesis. Bioorg Med Chem 12:2781-2786
18. 8 barrel enzymes. Curr Opin Chem Biol 7:252-264
19. Gibbs MR, Moody PCE, Leslie AGW (1990) Crystal Structure of the ASP-199 asparagine mutant of chloramphenicol acetyltransferase to 2.35. Å resolution: structural consequences of disruption of a buried salt bridge. Biochemistry 29:11261-11265
20. Gilliland GL, Tung M, Blakeslee DM, Ladner J (1994) The biological macromolecule crystallization database, version 3.0: new features, data, and the NASA archive for protein crystal growth data. Acta Crystallogr D 50:408-413
21. Harel M, Aharoni A, Gaidukov L, Brumshtein B, Khersonsky O, Meged R, Dvir H, Ravelle RBG, McCarthy A, Toker L, Silman L, Sussman JL, Tawfik DS (2004) Structure and evolution of the serum paraoxonase family of detoxifying and antiatherosclerotic enzymes. Nat Struct Mol Biol 11:412-419
22. Henrissat B (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280:309-316
23. Henrissat B, Bairoch A (1996) Updating the sequence-based classification of glycosyl hydrolases. J Biochem 316:695-696
24. Hoffmann L, Maury S, Martz F, Geoffry P, Legrand L (2003) Purification, cloning, and properties of an acyltransferase controlling shikimate and quinate ester intermediates in phenylpropanoid metabolism. J Biol Chem 278:95-103
25. Jawad Z, Paoli M (2002) Novel sequences propel familiar folds. Structure 10:447-454
26. Jeon H, Meng W, Takagi J, Eck MJ, Springer TA, Blacklow SC (2001) Implications for familial hypercholesterolemia from the structure of the LDL receptor YWTD-EGF domain pair. Nat Struct Biol 8:499-504
27. Koepke J, Ma X, Fritzsch G, Michel H, Stöckigt J (2005) Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine. Acta Crystallogr Sect D 61:690-693
28. Krupka HI, Rupp B, Segelke BW, Lekin TP, Wright D, Wu H-C, Todd P, Azarani A (2002) The high-speed Hydra-Plus-One system for a automated high-throughput protein crystallography. Acta Crystallogr D 58:1523-1526
29. Kutchan TM, Hampp N, Lottspeich F, Beyreuther K, Zenk MH (1988) The cDNA clone for strictosidine synthase from Rauvolfia serpentina. DNA sequence determination and expression in Escherichia coli. FEBS Lett 237:40-44
30. Kutchan TM (1993) Strictosidine: from alkaloid to enzyme to gene. Phytochemistry 32:493-506
31. Ma X, Koepke J, Fritzsch G, Diem R, Kutchan TM, Michel H, Stöckigt J (2004a) Crystallization and preliminary X-ray Crystallographic Analysis of strictosidine synthase from Rauvolfia - the first member of a novel enzyme family. Biochim Biophys Acta 1702:121-124
32. Ma X, Panjikar S, Koepke J Loris E, Stöckigt J (2006) The structure of Rauvolfia serpentina stritosidine synthase is a novel six-bladed beta-propeller fold in plant proteins. The Plant Cell 18:907-920
33. Ma X, Koepke J, Bayer A, Linhard V, Fritzsch G, Zhang B, Michel H, Stöckigt J (2004b) Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochim Biophys Acta 1701:129-132
34. Ma X, Koepke J, Bayer A, Fritzsch G, Michel H, Stöckigt J (2005a) Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina. Acta Crystallogr Sect D 61:694-696
35. Ma X, Koepke J, Panjikar S, Fritzsch G, Stöckigt J (2005b) Crystal structure of vinorine synthase, the first representative of the BAHD superfamily. J Biol Chem 280:13576-13583
36. Panjikar S, Parthasarathy V, Lamzin VS, Weiss MS, Tucker PA (2005) Auto-Rickshaw: an automated crystal structure determination platform as an effi-cient tool for the validation of an X-ray diffraction experiment. Acta Cryst D 61:449-457
37. Pfitzner A, Polz L, Stöckigt J (1986) Properties of Vinorine Synthase - the Rauvolfia Enzyme involved in the Formation of the Ajmaline Skeleton. Z Naturforsch 41c:103-114
38. Pfitzner M, Zenk MH (1989) Homogenous strictosidine synthase isoenzymes from cell suspension cultures of Catharanthus roseus. Planta Med 55:525-530
39. Pictet A, Spengler T (1911) Über die Bildung von Isochinolin-derivaten durch Übertragung von Methylal auf Phenyl-äthylamin, Phenyl-alanin und Tyrosin. Ber Dtsch Chem Ges 44:2030-2036
40. Pons T, Gomez R, Chinea G, Valencia A (2003) Betapropellers: associated functions and their role in human diseases. Curr Med Chem 10:505-524
41. Ruppert M, Stöckigt J (1999) Strictosidine - the biosynthetic key to monoterpenoid indole alkaloids. In: Sir Derek Barton, Nakanishi K (eds) Comprehensive Natural Products Chemistry Vol 4. Elsevier, Amsterdam, Lausanne, New York, Oxford, Shannon, Singapore, Tokyo, pp 109-138
42. Ruppert M, Ma X, Stöckigt J (2005) Alkaloid biosynthesis in Rauvolfia-cDNA cloning of major enzymes of the ajmaline pathway. In: Knölker H-J (eds) Current Org Chem 9:1431-1444
43. Ruppert M, Panjikar S, Barleben L, Stöckigt J (2006) Heterologous expression, purification, crystallization and preliminary X-ray analysis of raucaffricine glucosidase, a plant enzyme specifically involved in Rauvolfia alkaloid biosynthesis. Acta Crystallogr F 62:257-260
44. Ruyter CM, Stöckigt J (1991) Enzymatic formation of raucaffricine, the major indol alkaloid of Rauwolfia serpentina cell-suspension cultures. Helv Chim Acta 74:1707-1712
45. Samanani N, Liscombe DK, Facchini PJ (2004) Molecular cloning and characterization of norcoclaurine synthase, an enzyme catalyzing the first committed step in benzylisoquinoline alkaloid biosynthesis. Plant J 40:302-313
46. Scharff EI, Koepke J, Fritzsch G, Lücke C, Rüterjans H (2001) Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris. Structure 9:493-502
47. Schübel H, Stöckigt J, Feicht R, Simon H (1986) Partial purification and characterization of raucaffricine β-D-glucosidase from plant cell-suspension cultures of Rauwolfia serpentina. Helv Chim Acta 69:538-547
48. St-Pierre B, DeLuca V (2000) Evolution of acyltransferase genes: origin and diversification of the BAHD superfamily of acyltransferases involved in secondary metabolism. In: John RI, Romeo T, Varin L, DeLuca V (eds) Recent Advances in Phytochemistry, Evolution of Metabolic Pathways Vol 34. Elsevier Science, Oxford, pp 285-315
49. Suzuki H, Nakayama T, Nishino T (2003) Proposed mechanism and functional amino acid residues of malonyl-CoA: anthocyanin 5-O-glucoside-6‴- O-malonyltransferase from flowers of Salvia splendens, a member of the versatile plant acyltransferase family. Biochemistry 42:1764-1771
50. Treimer JE, Zenk MH (1979) Purification and properties of strictosidine synthase, the key enzyme in indole alkaloid formation. Eur J Biochem 101:225-233
51. Van Duyne GD, Standaert RF, Karplus A, Schreiber SL, Clardy J (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and Rapamycin. J Mol Biol 229:105-124
52. Warzecha H, Obitz P, Stöckigt J (1999) Purification, partial amino acid sequence and structure of the product of raucaffricine-O-beta-D- glucosidase from plant cell cultures of Rauvolfia serpentina. Phytochemistry 50:1099-1109
53. Warzecha H, Gerasimenko I, Kutchan TM, Stöckigt J (2000) Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis. Phytochemistry 54:657-666
54. Yamazaki Y, Sudo H, Yamazaki M, Aimi N, Saito K (2003) Camptothecin biosynthetic genes in hairy roots of Ophiorrhiza pumila: cloning, characterization and differential expression in tissues and by stress compounds. Plant Cell Physiol 44: 395-403