3-Hydroxybenzoate:coenzyme A ligase and 4-coumarate:coenzyme A ligase from cultured cells of Centaurium erythraea.
3-Hydroxybenzoate:coenzyme A ligase, an enzyme involved in xanthone biosynthesis, was detected in cell-free extracts from cultured cells of Centaurium erythraea Rafn. The enzyme was separated from 4-coumarate:coenzyme A ligase by fractionated ammonium sulphate precipitation and hydrophobic interaction chromatography. The CoA ligases exhibited different substrate specificities. 3-Hydroxybenzoate:coenzyme A ligase activated 3-hydroxybenzoic acid most efficiently and lacked affinity for cinnamic acids. In contrast, 4-coumarate:CoA ligase mainly catalyzed the activation of 4-coumaric acid but did not act on benzoic acids. The two enzymes were similar with respect to their relative molecular weight, their pH and temperature optima, their specific activity and the changes in their activity during cell culture growth.
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Institut für Pharmazeutische Biologie, Bonn, Germany.
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D002478:Cells, Cultured; D003066:Coenzyme A Ligases / Q000032:analysis*; D015394:Molecular Structure; D010946:Plants, Medicinal / Q000201:enzymology*
C058481:4-hydroxybenzoate coenzyme A ligase; D003066:Coenzyme A Ligases; C019943:4-coumarate-CoA ligase