Purification and Characterization of Strictosidine Synthase from a Suspension-Culture of Cinchona-Robusta

Détails

ID Serval
serval:BIB_4DA004394402
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Purification and Characterization of Strictosidine Synthase from a Suspension-Culture of Cinchona-Robusta
Périodique
Phytochemistry
Auteur⸱e⸱s
Stevens  L. H., Giroud  C., Pennings  E. J. M., Verpoorte  R.
ISSN
0031-9422
Statut éditorial
Publié
Date de publication
05/1993
Volume
33
Numéro
1
Pages
99-106
Notes
Cited References:
AERTS RJ, 1991, PLANTA, V183, P536
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248
CHUNG ACT, 1988, PLANTA MED, V54, P206
GAMBORG OL, 1968, EXP CELL RES, V50, P151
GIROUD C, 1991, PLANTA MED, V57, P143
HAMPP N, 1988, PHYTOCHEMISTRY, V27, P3811
KEENE AT, 1983, J CHROMATOGR, V260, P123
MIZUKAMI H, 1979, BIOCHEMISTRY-US, V18, P3760
MULDERKRIEGER T, 1982, PLANTA MED, V46, P19
NAGAKURA N, 1979, J CHEM SOC P1, P2308
PENNINGS EJM, 1989, ANAL BIOCHEM, V176, P412
PETERSON GL, 1977, ANAL BIOCHEM, V83, P346
PFITZNER U, 1989, PLANTA MED, V55, P525
SKINNER SE, 1987, PHYTOCHEMISTRY, V26, P721
STEVENS LH, 1992, IN PRESS PLANT PHYSL, V30
STOCKIGT J, 1980, INDOLE BIOGENETICALL, P113
TREIMER JF, 1979, EUR J BIOCHEM, V101, P225
YUN SL, 1977, BIOCHIM BIOPHYS ACTA, V480, P1 --- Old month value: May
Résumé
Four isoforms of strictosidine synthase (EC 4.3.3.2), which catalyses the stereospecific condensation of secologanin and tryptamine, were purified to homogeneity from a suspension culture of Cinchona robusta. The M(r)s are 35 000, 33 000, 35 000 and 33 000, and the isoelectric points are 6.5, 6.5, 7.5 and 7.5, respectively. The K(m) values of the four proteins for tryptamine are in the micromolar range. The enzymes are inhibited by the product strictosidine and by quinoline alkaloids. The K(i) of quinine for one of the main isoforms is ca 7 muM. No substrate inhibition was observed. In contrast with strictosidine synthase from Catharanthus roseus (Apocynaceae), all four isoforms of Cinchona robusta accepted 5-methoxytryptamine as a substrate. The enzyme does not catalyse the condensation of corynantheal with tryptamine derivatives. All four isoforms are glycosylated.
Mots-clé
cinchona-robusta, rubiaceae, strictosidine synthase, purification, characterization, alkaloid biosynthesis performance liquid-chromatography, alkaloids, enzyme, assay
Web of science
Création de la notice
05/02/2008 18:19
Dernière modification de la notice
20/08/2019 15:02
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