Divergent members of a soybean (Glycine max L.) 4‐coumarate:coenzyme A ligase gene family

• DOI: 10.1046/j.1432-1033.2002.02775.x
• Publication Date: 2003-03-11T18:39:06Z
• Authors: Christian Lindermayr; Britta Möllers; Judith Fliegmann; Annette Uhlmann; Friedrich Lottspeich; Harald Meimberg; Jürgen Ebel
• Keywords: Coenzyme A

4‐Coumarate:CoA ligase (4CL) is involved in the formation of coenzyme A thioesters hydroxycinnamic acids that are central substrates for subsequent condensation, reduction, and transfer reactions biosynthesis plant phenylpropanoids. Previous studies 4CL appear to suggest many isoenzymes functionally equivalent supplying various branches phenylpropanoid biosyntheses. In contrast, divergent members a gene family were identified soybean ( Glycine max L.). We isolated three structurally distinct cDNAs encoding 4CL1, 4CL2, 4CL3 Gm4CL3 . fourth cDNA 4CL4 had high similarity with 4CL3. The recombinant proteins expressed Escherichia coli possessed highly catalytic efficiency acids. Remarkably, one isoenzyme (4CL1) was able convert sinapate; thus first accepts substituted cinnamic available further on metabolism probably lead precursors lignin. Surprisingly, activity levels four steady‐state their transcripts differently affected after elicitor treatment cell cultures β‐glucan Phytophthora sojae , revealing down‐regulation 4CL1 vs. up‐regulation 4CL3/4. similar regulation transcript different isoforms observed seedlings infection zoospores. Thus, partitioning acid building units between branch pathways could be regulated at level specificity expression isoenzymes.