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PLANT PHYSIOLOGY , Vol 106, Issue 1 271-279, Copyright © 1994 by American Society of Plant Biologists
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METABOLISM AND ENZYMOLOGY |
Biosynthesis of p-Hydroxybenzoate from p-Coumarate and p-Coumaroyl-Coenzyme A in Cell-Free Extracts of Lithospermum erythrorhizon Cell Cultures
R. Loscher and L. Heide
Institut fur Pharmazeutische Biologie, Albert-Ludwigs-Universitat Freiburg, Schanzlestrasse 1, 79104 Freiburg im Breisgan, Germany
The enzymatic formation of p-hydroxybenzoate from p-coumarate in cell-free
extracts of cell cultures of Lithospermum erythrorhizon Sieb. et Zucc. was
investigated. p-Coumaroyl-coenzyme A (p-coumaroyl-CoA) is the activated
intermediate in this biosynthetic reaction. It is formed by an ATP-, Mg2+
-, and CoA-dependent 4-hydroxycinnamate:CoA ligase reaction.
p-Coumaroyl-CoA is oxidized and cleaved to p-hydroxybenzoyl-CoA and
acetyl-CoA in a thioclastic reaction in which NAD is an essential cofactor.
These CoA esters are rapidly hydrolyzed to acetate and p-hydroxybenzoate,
probably by thioesterases. The enzymes involved in the formation of
p-hydroxybenzoate are soluble. p-Hydroxybenzalde-hyde is not an
intermediate in this conversion, and S-denosylmethionine and
uridine-5[prime]-diphosphoglucose do not enhance formation of
p-hydroxybenzoate in our system.
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