The 4-coumarate:CoA Ligase Gene Family in Arabidopsis Thaliana Comprises One Rare, Sinapate-activating and Three Commonly Occurring Isoenzymes

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2004 Feb 11

PMID 14769935

Citations 79

Authors

Bjorn Hamberger

Klaus Hahlbrock

Affiliations

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Abstract

4-Coumarate:CoA ligase (4CL; EC 6.2.1.12) has a pivotal role in the biosynthesis of plant secondary compounds at the divergence point from general phenylpropanoid metabolism to several major branch pathways. In Arabidopsis thaliana, we have identified a previously undetected, fourth and final member of the At4CL gene family. The encoded enzyme, At4CL4, exhibits the rare property of efficiently activating sinapate, besides the usual 4CL substrates (4-coumarate, caffeate, and ferulate), indicating a distinct metabolic function. Phylogenetic analysis suggests an early evolutionary and functional divergence of three of the four gene family members, At4CL2-4, whereas At4CL1 appears to have originated much later by duplication of its structurally and functionally closest relative, At4CL2. Various characteristics shared by all known plant 4CL genes, as well as by the encoded proteins, define and delimit the At4CL gene family and distinguish it from the closely related family of "At4CL-like" genes.

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