Abstract
Tyrosine decarboxylase (EC 4.1.1.25) from Syringa vulgaris L. cell cultures and from Hordeum vulgare L. seedlings is strongly inhibited by the phenylalanine analogue, l-α-aminooxy-β-phenylpropionate. l-α-Aminooxy-β-phenylpropionate is therefore not specific in its inhibitory action against phenylalanine ammonia-lyase (EC 4.3.1.5). Hordeum tyrosine decarboxylase is also very sensitive to α-fluoromethyl(3,4-dihydroxyphenyl)alanine, but preparations from Nicotiana tabacum L. and Sanguinaria canadensis L. are largely unaffected by either type of inhibitor.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Abbreviations
- AOPP:
-
l-α-aminooxy-β-phenylpropionic acid
- PAL:
-
l-phenylalanine ammonia-lyase
- TDC:
-
l-tyrosine decarboxylase
References
Allenmark, S., Servenius, B. (1978) Characterization of bacterial l-(-)-tyrosine decarboxylase by isoelectric focussing and gel chromatography. J. Chromatogr. 153, 239–245
Amrhein, N., Diederich, E. (1980) Turnover of isoflavones in Cicer arietinum L. Naturwissenschaften 67, 40
Amrhein, N., Frank, G., Lemm, G., Luhmann, H.-B. (1983) Inhibition of lignin formation by l-α-aminooxy-β-phenylpropionic acid, an inhibitor of phenylalanine ammonialyase. Eur. J. Cell Biol. 29, 139–144
Amrhein, N., Gödeke, K.-H. (1977) α-Aminooxy-β-phenylpropionic acid — a potent inhibitor of l-phenylalanine ammonia-lyase in vitro and in vivo. Plant Sci. Lett. 8, 313–317
Amrhein, N., Gödeke, K.-H., Kefeli, V.I. (1976) The estimation of relative intracellular phenylalanine ammonia-lyase (PAL) activities and the modulation in vivo and in vitro by competitive inhibitors. Ber. Dtsch. Bot. Ges. 89, 247–259
Amrhein, N., Holländer, H. (1979) Inhibition of anthocyanin formation in seedlings and flowers by the enantiomers of α-aminooxy-β-phenylpropionic and their N-benzyloxycarbonyl derivatives. Planta 144, 385–389
Berlin, J., Vollmer, B. (1979) Effects of α-aminooxy-β-phenylpropionic acid on phenylalanine metabolism in p-fluorophenylalanine sensitive and resistant tobacco cells. Z. Naturforsch. Teil C 34, 770–775
Briggs, M.T., Morley, J.S. (1979) Polypeptides. Part 17. Aminoxy-analogues of aspartame and gastrin C-terminal tetrapeptide amide. J. Chem. Soc., Perkin Trans. I 1979, 2138–2143
Clarke, D.D. (1982) The accumulation of cinnamic acid amides in the cell walls of potato tissue as an early response to fungal attack. In: Active defense mechanisms in plants, p. 321, Wood, R.K.S., ed. Plenum Press, New York London
Cottle, W., Kolattukudy, P.E. (1982) Biosynthesis, deposition, and partial characterization of potato suberin phenolics. Plant Physiol. 69, 393–399
Ellis, B.E. (1983) Production of hydroxyphenylethanol glycosides in suspension cultures of Syringa vulgaris. Phytochemistry 22, 1941–1943
Ellis, B.E., Remmen, S., Goeree, G. (1979) Interactions between parallel pathways during biosynthesis of rosmarinic acid in cell suspension cultures of Coleus blumei. Planta 147, 163–167
Hanson, K.R., Havir, E.A. (1970) l-phenylalanine ammonialyase. IV. Evidence that the prosthetic groups contains a dehydroalanyl residue and mechanism of action. Arch. Biochem. Biophys. 141, 1–17
Hosoi, K. (1974) Purification and some properties of l-tyrosine carboxylyase from barley roots. Plant Cell Physiol. 15, 429–440
John, R.A., Charteris, A., Fowler, L.J. (1978) The reaction of aminooxyacetate with pyridoxal phosphate-dependent enzymes. Biochem. J. 171, 771–779
Kamisaka, S., Shibata, K. (1982) Identification in lettuce seedlings of a catecholamine active in synergistically enhancing the gibberellin effect on lettuce hypocotyl elongation. Plant Growth Regul. 1, 3–10
Leete, E., Marison, L. (1953) The biogenesis of alkaloids. VII. The formation of hordenine and N-methyltyramine from tyrosine in barley. Can. J. Chem. 31, 126–128
Lovenberg, W., Weisbach, H., Udenfriend, S. (1962) Aromatic l-amino acid decarboxylase. J. Biol. Chem. 237, 89–92
Maycock, A.L., Aster, S.D., Patchett, A.A. (1980) Inactivation of 3-(3,4-dihydroxyphenyl)alanine decarboxylase by 2-(fluoromethyl)-3-(3,4-dihydroxyphenyl)alanine. Biochemistry 19, 709–718
Michell, S.D., Firmin, J.L., Gray, D.O. (1984) Enhanced 3-methoxytyramine levels in crown gall tumours and other undifferentiated plant tissues. Biochem. J. 221, 891–895
Moesta, P., Grisebach, H. (1982) l-2-Aminooxy-3-phenylpropionic acid inhibits phytoalexin accumulation in soybean with concomitant loss of resistance against Phytophthora megasperma f. sp. glycinea. Physiol. Plant Pathol. 21, 65–70
Negrel, J., Martin, C. (1984) The biosynthesis of feruloyltyramine in Nicotiana tabacum. Phytochemistry 23, 2797–2801
Negrel, J., Vallee, J.C., Martin, C. (1984) Ornithine decarboxylase activity and the hypersensitive reaction to tobacco mosaic virus in Nicotiana tabacum. Phytochemistry 23, 2747–2751
Noé, W., Langebartels, C., Seitz, H.U. (1980) Anthocyanin accumulation and PAL activity in a suspension culture of Daucus carota L. Inhibition by l-α-aminooxy-β-phenylpropionic acid and t-cinnamic acid. Planta 149, 283–287
Noé, W., Seitz, H.U. (1983) Studies on the regulatory role of trans-cinnamic acid on the activity of the phenylalanine ammonia-lyase (PAL) in suspension cultures of Daucus carota L. Z. Naturforsch. Teil C 38, 408–412
Ramsey, N.B. (1984) Purification and properties of l-phenylalanine ammonia-lyase from cell suspension cultures of Syringa vulgaris L. M.Sc. thesis, University of Guelph
Schumacher, H.M., Ruffer, M., Nagakura, N., Zenk, M.H. (1983) Partial purification and properties of (S)-norlaudanosoline synthase from Eschscholtzia tenuifolia cell cultures. Planta Med. 48, 212–220
Smart, C.C., Amrhein, N. (1985) The influence of lignification on the development of vascular tissue in Vigna radiata L. Protoplasma 124, 87–95
Smith, T.A. (1977) Phenethylamine and related compounds in plants. Phytochemistry 16, 9–18
Tutschek, R. (1982) Interference of l-α-aminooxy-β-phenylpropionic acid with cold-induced sphagnorubin synthesis in Sphagnum magellanicum Brid. Planta 155, 307–309
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Chapple, C.C.S., Walker, M.A. & Ellis, B.E. Plant tyrosine decarboxylase can be strongly inhibited by l-α-aminooxy-β-phenylpropionate. Planta 167, 101–105 (1986). https://doi.org/10.1007/BF00446375
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00446375