THE PHOSPHOHYDROLYSIS OF HYDROXYCINNAMOYL-COENZIME A THIOESTERS IN PLANT EXTRACTS

Article abstract of DOI:10.1016/0031-9422(84)83072-1

In barley seedling extracts, p-coumaroyl-CoA is rapidly hydrolysed to p-coumaroyl-dephospho-CoA, p-coumaroyl-4'-phosphopantetheine and p-coumaroyl-pantetheine. p-Coumaroyl-4'-phosphopantetheine is active as a substrate of agmatine coumaroyl transferase in the formation of p-coumaroyl agmatine, but p-coumaroyl-pantetheine is inactive.The phosphohydrolysis can be partly inhibited by inorganic pyrophosphate, sodium fluoride and purine nucleotides.A simplified method for the synthesis of N-hydroxysuccinimide esters of hydroxycinnamic acids, used in the synthesis of CoA thioesters, is also described.Key Word Index -- Hordeum vulgare; Gramineae; barley seedlings; plant extracts; phosphohydrolysis; hydroxycinnamoyl-CoA; p-coumaroylagmatine.