Reduction of coenzyme a thioesters of cinnamic acids with an enzyme preparation from lignifying tissue of Forsythia
Reduction of coenzyme a thioesters of cinnamic acids with an enzyme preparation from lignifying tissue of Forsythia
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DOI：
10.1016/0014-5793(75)80087-1
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发表时间：
1975-06
期刊：
影响因子：
3.5
通讯作者：
G. Gross;W. Kreiten
中科院分区：
文献类型：
--
作者：
G. Gross;W. Kreiten
It is well established that the lignin macromolecule is built up by the condensation of differently ringsubstituted cinnamyl alcohols [l]. By tracer experiments it has been shown that these alcohols must be formed by the reduction of the corresponding cinnamic acids [1, 2]. Such a reaction is an endergonic process requiring activation of the carboxyl group of the acid, and cinnamoylCoA esters have been postulated as these intermediates [3, 4]. In fact, it was demonstrated by in vitro experiments, with extracts from higher plants, that the reduction of p-coumarate and ferulate was dependent on the presence of CoA [. 5-g]. Furthermore, authentic p-coumaroyl-CoA and feruloyl-CoA were found to be reduced in the presence of NADPH by extracts from soybean cell cultures [6] or from lignifying tissue of Forsythia [7, 9]. In the present paper we describe some properties of the enzyme from Forsythia which catalyzes the reduction of cinnamoyl-CoA esters.
