The enzyme has been purified from Solanum lycopersicum (tomato) fruits. In the vacuole, at pH 4-5, it produces 3,5-dicaffeoylquinic acid from cholorgenic acid. In the cytoplasm, at pH 6-7, it can use aromatic acyl-CoAs as donors and catalyses the reaction of EC 2.3.1.99 (quinate O-hydroxycinnamoyltransferase). The initial product, 3,5-dicaffeoylquinic acid, undergoes spontaneous acyl migration to form 4,5-dicaffeoylquinic acid. Small amounts of 1,5-dicaffeoylquinic acid are formed as a byproduct.
Moglia A, Lanteri S, Comino C, Hill L, Knevitt D, Cagliero C, Rubiolo P, Bornemann S, Martin C.
Title
Dual catalytic activity of hydroxycinnamoyl-coenzyme A quinate transferase from tomato allows it to moonlight in the synthesis of both mono- and dicaffeoylquinic acids.
