p coumarate/potato

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Biosynthetic origin of the 1-oxygen of umbelliferone in the root tissue of sweet potato.

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Oxidation of p-coumarate at the ortho-position is a key step to form umbelliferone. A tracer analysis using (18)O2 was performed in order to take information about the formation of umbelliferone in the root tissue of sweet potato. Mass fragmentation experiments revealed incorporation of an 18O atom

l-Phenylalanine Ammonia-Lyase (Maize): Evidence for a Common Catalytic Site for l-Phenylalanine and l-Tyrosine.

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l-Phenylalanine ammonia-lyase (E.C. 4.3.1.5) from maize is active with l-tyrosine and l-phenylalanine and exhibits atypical Michaelis-Menten kinetics with both substrates. With phenylalanine as a substrate, the pH optimum is 8.7 and with tyrosine, 7.7. The estimated Km at high substrate

Inhibition of insect glutathione S-transferase (GST) by conifer extracts.

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Insecticide synergists biochemically inhibit insect metabolic enzyme activity and are used both to increase the effectiveness of insecticides and as a diagnostic tool for resistance mechanisms. Considerable attention has been focused on identifying new synergists from phytochemicals with recognized

p-Coumaroylnoradrenaline, a novel plant metabolite implicated in tomato defense against pathogens.

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The Avr9 peptide elicitor from the fungus Cladosporium fulvum, the bacterial pathogen Pseudomonas syringae pathovar tomato carrying the avirulence gene avrPto (Pst (avrPto)), and the organophosphorous insecticide fenitrothion induce resistance-related responses in tomato lines carrying the Cf-9,

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