Structural basis of enzymatic (S)-norcoclaurine biosynthesis

Journal of Biological Chemistry

Volumn 284, Issue 2, 2009, Pages 897-904

  Ilari, Andrea ^a   Franceschini, Stefano ^a   Bonamore, Alessandra ^a   Arenghi, Fabio ^b   Botta, Bruno ^a   Macone, Alberto ^a   Pasquo, Alessandra ^c   Bellucci, Luca ^d   Boffi, Alberto ^a  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b CPC Biotech Srl   (Italy)

^c ENEA C R CASACCIA   (Italy)

^d UNIVERSITY OF SIENA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; BRAIN; CYCLIZATION; ENZYMES; ORGANIC ACIDS;

4-HYDROXYBENZALDEHYDE; ACTIVE SITES; BIOSYNTHETIC PATHWAYS; CATALYTIC PROCESS; COMMON FEATURES; CRYSTALLOGRAPHIC STRUCTURES; GLUTAMIC ACIDS; INDOLE ALKALOIDS; PICTET-SPENGLER CYCLIZATION; SIDE CHAINS; SITE-DIRECTED MUTATIONS; STEREO-SELECTIVE; STRUCTURAL BASIS; STRUCTURAL DETERMINANTS; SYNTHASE;

SUBSTRATES;

4 HYDROXYBENZALDEHYDE; 4 HYDROXYPHENYLACETALDEHYDE; ALDEHYDE DERIVATIVE; ASPARTIC ACID; BENZYLISOQUINOLINE DERIVATIVE; DOPAMINE; ENZYME; GLUTAMIC ACID; INDOLE ALKALOID; LYSINE; NORCOCLAURINE SYNTHASE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SYNTHESIS; GEOMETRY; MUTATION; PICTET SPENGLER REACTION; PRIORITY JOURNAL; STEREOCHEMISTRY; STEREOSPECIFICITY; THALICTRUM;

ALKALOIDS; BIOCATALYSIS; CARBON-NITROGEN LIGASES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; TETRAHYDROISOQUINOLINES; THALICTRUM;

THALICTRUM FLAVUM;

EID: 59449099013     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M803738200     Document Type: Article

References (30)

1. Ziegler, J., and Facchini, P. J. (2008) Annu. Rev. Plant. Biol. 59, 735-769
2. Facchini, P. J., and St-Pierre, B. (2005) Curr. Opin. Plant Biol. 8, 657-666
3. Stadler, R., and Zenk, M. H. (1990) LiebigsAnn. Chem. 6, 555-562
4. Maryanoff, B. E., Zhang, H. C., Cohen, J. H., Turchi, I. J., and Maryanoff, C. A. (2004) Chem. Rev. 144, 1431-1628
5. Kutchan, T. M. (1993) Phytochemistry 32, 493-506
6. Ma, X., Panjikar, S., Koepke, J., Loris, E., and Stöckigt, J. (2006) Plant Cell 18, 907-920
7. Samanani, L., and Facchini, P. J. (2002) J.Biol. Chem. 277, 33878-33883
8. Samanani, L., Liscombe, D. K., and Facchini, P. J. (2004) Plant J. 40, 302-316
9. Luk, L. Y., Bunn, S., Liscombe, D. K., and Facchini, P. J., Tanner, M. E. (2007) Biochemistry 46, 10153-10161
10. Minami, H., Dubouzet, E., Iwasa, K., and Sato, F. (2007) J.Biol. Chem. 282, 6274-6282
11. Berkner, H., Schweimer, K., Matecko, I., and Rösch, P. (2008) Biochem. J. 413, 281-290
12. Pasquo, A., Bonamore, A., Franceschini, S., Macone, A., Boffi, A., and Ilari, A. (2008) Acta Crystallogr. Sect. F Struct. Biol. Crystallogr. Commun. 64, 281-283
13. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
14. Cowtan, K. (1994) Jnt. CCP4/ESF-EACBM Newsl. Protein Crystallogr. 31, 34-38
15. Matthews, B. W. (1968) J. Mol. Biol. 33, 491-497
16. Terwilliger, T. C., and Berendzen, J. (1999) Acta Crystallogr. D Biol. Crys-tallogr. 55, 849-861
17. Lamzin, V. S., Perrakis, A., and Wilson, K. S. (2001) International Tables for Crystallography. Volume F: Crystallography of biological macromole-cules (Rossmann, M. G., and Arnold, E., eds) pp. 720-722, Kluwer Aca-demic Publishers, Dordrecht, The Netherlands
18. Cowtan, K.D., and Main, P. (1996) Acta Crystallogr. Sect. D Biol. Crystal-logr. 52, 43-4814
19. Murshudov, N., Lebedev, A., Vagin, A., Wilson, K. S., and Dodson, E. J. (1999) Acta Crystallogr. Sect. D Biol. Crystallogr. 55, 247-255
20. Emsley, P., and Cowtan, K. (2004) Acta Crystallogr. Sect. D Biol. Crystal-logr. 60, 2126-2132
21. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M., (1993) J.Appl. Crystallogr. 26, 283-291
22. Vagin, A. A., and Teplyakov, A. J. (1997) J. Appl. Crystallogr. 30, 1022-1025
23. Hazen, S. L., Gaut, J. P., Hsu, F. F., Crowley, J. R., d'Avignon, A., and Heinecke, J. W. (1997) J.Biol. Chem. 272, 16990-16998
24. Gajhede, M., Osmark, P., Poulsen, F. M., Ipsen, H., Larsen, J. N., van Neerven, R. J. J., Schou, C., L0wenstein, H., and Spangford, M. D. (1996) Nat. Struct. Biol. 3, 1040-1045
25. Ames, B. D., Korman, T. P., Zhang, W., Smith, P., Vu, T., Tang, Y., and Tsai, S. C. (2008) Proc. Natl. Acad. Sci. U. S. A. 105, 5345-5349
26. Pasternak, O., Bujacz, G. D., Fujimoto, Y., Jelen, F., Otlewski, J., Sikorski, M. M., and Jaskolski, M. (2006) Plant Cell 18, 2622-2634
27. Seayed, J., Seayed, A. M., and List, B. (2006) J. Am. Chem. Soc. 128, 1086-1087
28. Noyori, R., Masato, K., Hidemasa, T., Hidenori, K., and Sasumu, A. (July 25, 1989) U. S. Patent 4851537
29. DeLano, W. L. (2002) The PyMOL User's Manual, DeLano Scientific, San Carlos, CA
30. Petřek, M., Otyepka, M., Banáš, P., Košinová, P., Koča, J., and Damborský, J. (2006) BMC Bioinformatics 7, 316