9,10-Dihydrophenanthrenes as phytoalexins of Orchidaceae. Biosynthetic studies in vitro and in vivo proving the route from L-phenylalanine to dihydro-m-coumaric acid, dihydrostilbene and dihydrophenanthrenes.

Hydroxy derivatives of 9,10-dihydrophenanthrenes, orchinol and hircinol, were isolated from bulbs of Orchidaceae which had been induced to accumulate phytoalexins. Incorporation of radioactive precursors, L-phenylalanine and various hydroxycinnamic acids, has been investigated by feeding experiments in vivo. m-Coumaric acid and dihydro-m-coumaric acid were found to be efficiently incorporated into the dihydrophenanthrene derivatives. Dihydro-m-coumaric acid was not only converted into the dihydrophenanthrenes but was also formed from L-phenylalanine in the same tissue; it was thus proved to be an intermediate. The role of dihydro-m-coumaric acid was substantiated by studies in vitro. An active stilbene synthase was detected in enzyme preparations from induced orchid bulbs and assayed with different CoA esters. The enzyme, characterized on the basis of its substrate specificity, selectively converted dihydro-m-coumaroyl-CoA plus malonyl-CoA into 3,3',5-trihydroxybibenzyl. The role of 3,3',5-trihydroxybibenzyl as physiological intermediate was further corroborated by investigations with intact plants. Both its formation from phenylpropanoids and its conversion into orchinol was demonstrated. The data provided evidence for a biosynthetic sequence originating from L-phenylalanine and leading to 9,10-dihydrophenanthrenes via m-coumaric acid, dihydro-m-coumaric acid, and 3,3',5-trihydroxybibenzyl.

Coordinated regulation of 4-coumarate:CoA ligase and phenylalanine ammonia-lyase mRNAs in cultured plant cells.

4-Coumarate:CoA ligase (EC 6.2.1.12) from cell suspension cultures of parsley (Petroselinum hortense) was extensively purified. The enzyme behaved as a monomer with a molecular weight of approximately 60,000. A rabbit antiserum to the purified enzyme was obtained and used to determine the rates of 4-coumarate:CoA ligase synthesis under various conditions of induction, such as short term or continuous irradiation and treatment of the cells with an "elicitor" preparation from a fungal pathogen. In all cases, the time course of changes in the rate of synthesis, measured both in vivo and in vitro, was very similar for 4-coumarate:CoA ligase and a closely related enzyme, phenylalanine ammonia-lyase (EC 4.3.1.5). The results suggest that the mRNA activities encoding the two enzymes are regulated in a coordinated manner.

[Potent natural inhibitors of tobacco mosaic virus multiplication]. / Sur de puissants inhibiteurs naturels de multiplication du virus de la mosaique du tabac

The hypersensitivity reaction in Nicotiana tabacum var. Xanthi n.c. infected with Tobacco mosaic virus (T.M.V.) leads to the production of aromatic amides (ferulylputrescine, diferulylputrescine, p-coumarylputrescine and di-p-coumarylputrescine) inthe cells around the necroses. Similar compounds are formed in Xanthi plants after floral induction. p-coumarylputrescine, di-p-coumarylputrescine and caffeylputrescine strongly inhibit T.M.V. multiplication.