Artigo Acesso aberto

Enzymes of Flavone and Flavonol-Glycoside Biosynthesis. Coordinated and Selective Induction in Cell-Suspension Cultures of Petroselinum hortense

1977; Wiley; Volume: 75; Issue: 1 Linguagem: Inglês

10.1111/j.1432-1033.1977.tb11518.x

ISSN

1432-1033

Autores

Jürgen Ebel, Klaus Hahlbrock,

Tópico(s)

Plant tissue culture and regeneration

Resumo

European Journal of BiochemistryVolume 75, Issue 1 p. 201-209 Free Access Enzymes of Flavone and Flavonol-Glycoside Biosynthesis Coordinated and Selective Induction in Cell-Suspension Cultures of Petroselinum hortense Jürgen EBEL, Jürgen EBEL Lehrstuhl für Biochemie der Pflanzen, Institut für Biologie II, Albert-Ludwigs-Universität Freiburg, Schänzlestraße 9/11, D-7800 Freiburg i. Br., Federal Republic of GermanySearch for more papers by this authorKlaus HAHLBROCK, Klaus HAHLBROCK Lehrstuhl für Biochemie der Pflanzen, Institut für Biologie II, Albert-Ludwigs-Universität Freiburg, Schänzlestraße 9/11, D-7800 Freiburg i. Br., Federal Republic of GermanySearch for more papers by this author Jürgen EBEL, Jürgen EBEL Lehrstuhl für Biochemie der Pflanzen, Institut für Biologie II, Albert-Ludwigs-Universität Freiburg, Schänzlestraße 9/11, D-7800 Freiburg i. Br., Federal Republic of GermanySearch for more papers by this authorKlaus HAHLBROCK, Klaus HAHLBROCK Lehrstuhl für Biochemie der Pflanzen, Institut für Biologie II, Albert-Ludwigs-Universität Freiburg, Schänzlestraße 9/11, D-7800 Freiburg i. Br., Federal Republic of GermanySearch for more papers by this author First published: May 1977 https://doi.org/10.1111/j.1432-1033.1977.tb11518.xCitations: 58 Definition. Numbering of carbon atoms of the flavones and flavonols (3-hydroxyflavones) mentioned in the text: AboutSectionsPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Abstract We have extended our previous studies, which had resulted in the classification of two groups of coordinately induced enzymes of phenylpropanoid metabolism in irradiated cell-suspension cultures of Petroselinum hortense Hoffm. The additional enzymes investigated were acetyl-CoA carboxylase, a methyltransferase, and a flavonol-specific glucosyltransferase. The results indicate that the second group (group II) includes the enzymes of both flavone and flavonol glycoside formation from 4-coumaroyl-CoA and acetyl-CoA (utilized via malonyl-CoA). The enzymes of this pathway, as opposed to those of the general phenylpropanoid metabolism (group I), met the following operational criteria for their common classification into group II. Under the experimental conditions employed, they increased in activity after a considerably longer, but uniform, lag period of about 4 h, as compared with about 2 h for group I; pronounced peaks of the individual enzyme activities in the range between about 25 and 40 h after the onset of induction occurred significantly later than in the case of group I; subsequent periods of exponential decline of the enzyme activities occurred with relatively long apparent half-lives of the order of 30–70 h. The induction of the two groups of enzymes was shown to be highly selective. Several enzymes involved in various pathways of intermediary metabolism were not affected by irradiation of the cell cultures. Even those enzymes, which are assumed to catalyze the formation of the various intermediary metabolites serving as substrates for the light-induced reactions, remained unaffected by the irradiation program. Enzymes UDP glucose dehydrogenase (EC 1.1.1.22), S-adenosylmethionine: flavone/flavonol 3′-O-methyltransferase (EC 2.1.1.42), sucrose synthase (EC 2.4.1.13), UDPglucose): flavone/flavonol 7-O-glucosyltransferase (EC 2.4.1.81), UDPglucose: flavonol 3-O-glucosyltransferase (EC 2.4.1.–), UDPapiose: flavone-7-O-glucoside 2″-O-apiosyltransferase (EC 2.4.2.25), methionine adenosyl-transferase (EC 2.5.1.6), phenylalanine: 2-oxoglutarate aminotransferase (EC 2.6.1.5) UDPglucuronate pyrophosphorylase (EC 2.7.7.–) ATP citrate (pro-3S)lyase (ADP-forming) (EC 4.1.3.8) phenylalanine ammonia-lyase (EC 4.3.1.5) acetate: CoA ligase (EC 6.2.1.1) succinate: CoA ligase (ADP-forming) (EC 6.2.1.5) malonate: CoA ligase (EC 6.2.1.–) 4-coumarate: CoA ligase (EC 6.2.1.12) acetyl-CoA carboxylase (EC 6.4.1.2) cinnamate 4-hydroxylase, flavanone synthase REFERENCES 1 Hahlbrock, K., Ebel, J., Ortmann, R., Sutter, A., Wellmann, E. & Grisebach, H. (1971) Biochim. Biophys. Acta, 244, 7– 15. 2 Hahlbrock, K., Knobloch, K.-H., Kreuzaler, F., Potts, J. R. M. & Wellmann, E. (1976) Eur. J. Biochem. 61, 199– 206. 3 Ebel, J., Hahlbrock, K. & Grisebach, H. (1972) Biochim. Biophys. Acta, 268, 313– 326. 4 Sutter, A. & Grisebach, H. (1973) Biochim. Biophys. Acta, 309, 289– 295. 5 Kreuzaler, F. & Hahlbrock, K. (1973) Phytochemistry, 12, 1149– 1152. 6 Hahlbrock, K. (1975) Planta (Berl.) 124, 311– 319. 7 Hahlbrock, K. & Schröder, J. (1975) Arch. Biochem. Biophys. 171, 500– 506. 8 Poulton, J., Grisebach, H., Ebel, J., Schaller-Hekeler, B. & Hahlbrock, K. (1976) Arch. Biochem. Biophys. 173, 301– 305. 9 Hatch, M. D. & Stumpf, P. K. (1961) J. Biol. Chem. 236, 2879– 2885. 10 Fujioka, M., Morino, Y. & Wada, H. (1970) Methods Enzymol. 17A, 585– 596. 11 Knobloch, K.-H. & Hahlbrock, K. (1975) Eur. J. Biochem. 52, 311– 320. 12 Hahlbrock, K. (1965) Ph. D. Thesis, p. 31, University of Freiburg. 13 Grimes, W. J., Jones, B. L. & Albersheim, P. (1970) J. Biol. Chem. 245, 188– 197. 14 Roberts, R. M. (1971) J. Biol. Chem. 246, 4995– 5002. 15 Takeda, Y., Suzuki, F. & Inoue, H. (1969) Methods Enzymol. 13, 153– 160. 16 Stadtman, E. R (1957) Methods Enzymol. 3, 230– 231. 17 Bergmeyer, H. U. (1974) Methoden der enzymatischen Analyse, p. 554, Verlag Chemie, Weinheim . 18 Layne, E. (1957) Methods Enzymol. 3, 447– 454. 19 Maurer, H. R. (1968) Disk-Elektrophorese, p. 42, de Gruyter, Berlin . 20 Hahlbrock, K. & Wellmann, E. (1973) Biochim. Biophys. Acta, 304, 702– 706. 21 Hahlbrock, K. & Grisebach, H. (1970) FEBS Lett. 11, 62– 64. 22 Roberts, R. M. & Cetorelli, J. J. (1973) in Biogenesis of Plant Cell Wall Polysaccharides ( F. Loewus, ed.) pp. 49– 68, Academic Press, New York . 23 Sutter, A., Ortmann, R. & Grisebach, H. (1972) Biochim. Biophys. Acta, 258, 71– 87. 24 Volpe, J. J. & Vagelos, P. R. (1973) Annu. Rev. Biochem. 42, 21– 60. 25 Scheel, D. & Sandermann, H. (1975) Planta (Berl.) 124, 211– 214. Citing Literature Volume75, Issue1May 1977Pages 201-209 ReferencesRelatedInformation

Referência(s)