4-Coumarate: Coenzyme a ligase in black locust (Robinia pseudoacacia) catalyses the conversion of sinapate to sinapoyl-CoA

Katsuyoshi Hamada, Tomoaki Nishida, Kazuchika Yamauchi, Kazuhiko Fukushima, Ryuichiro Kondo, Yuji Tsutsumi

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

4-Coumarate:coenzyme A (CoA) ligase (4CL, EC 6.2.1.12) in crude enzyme preparation from the developing xylem of black locust (Robinia pseudoacacia) converted sinapate to sinapoyl CoA. The sinapate-converting activity was not inhibited by other cinnamate derivatives, such as p-coumarate, caffeate or ferulate, in the mixed-substrate assay. The crude extract prepared from the developing xylem was separated by anion-exchange chromatography into three different 4CL isoforms. The isoform 4CL1 had a strong substrate preference for p-coumarate, but lacked the activity for ferulate and sinapate. On the other hand, 4CL2 and 4CL3 displayed activity toward sinapate and also possessed high activity toward caffeate as well as p-coumarate. The crude extract from the shoots exhibited a very similar substrate preference to that of the developing xylem; therefore, 4CL2 may be a major isoform in both crude enzyme preparations. These results support the hypothesis that sinapate-converting 4CL isoform is constitutively expressed in lignin-forming cells.

Original languageEnglish
Pages (from-to)303-310
Number of pages8
JournalJournal of Plant Research
Volume117
Issue number4
DOIs
Publication statusPublished - Aug 1 2004

All Science Journal Classification (ASJC) codes

  • Plant Science

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