Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

4CL3 - 4-coumarate--CoA ligase 3

Arabidopsis thaliana

Synonyms: 4-COUMARATE:COA LIGASE, 4-coumarate--CoA ligase isoform 3, 4-coumarate:CoA ligase 3, 4-coumaroyl-CoA synthase 3, 4CL 3, ...

Ehlting, J. et al., Stuible, H.P. et al., Costa, M.A. et al.

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High impact information on 4CL3

Among these amino acids, representing the putative "substrate specificity motif," only one residue, Met(293), was not conserved in At4CL2, compared with At4CL1 and At4CL3, two isoforms using ferulate [1].
Based on their enzymatic properties, expression characteristics and evolutionary relationships, At4CL3 is likely to participate in the biosynthetic pathway leading to flavonoids whereas At4CL1 and At4CL2 are probably involved in lignin formation and in the production of additional phenolic compounds other than flavonoids [2].
At4CL3 also displayed broad substrate specificity efficiently converting p-coumaric, caffeic and ferulic acids into their CoA esters, whereas 5-hydroxyferulic acid was not as effectively utilized [3].

References

Identification of the substrate specificity-conferring amino acid residues of 4-coumarate:coenzyme A ligase allows the rational design of mutant enzymes with new catalytic properties. Stuible, H.P., Kombrink, E. J. Biol. Chem. (2001) [Pubmed]
Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms. Ehlting, J., Büttner, D., Wang, Q., Douglas, C.J., Somssich, I.E., Kombrink, E. Plant J. (1999) [Pubmed]
Characterization in vitro and in vivo of the putative multigene 4-coumarate:CoA ligase network in Arabidopsis: syringyl lignin and sinapate/sinapyl alcohol derivative formation. Costa, M.A., Bedgar, D.L., Moinuddin, S.G., Kim, K.W., Cardenas, C.L., Cochrane, F.C., Shockey, J.M., Helms, G.L., Amakura, Y., Takahashi, H., Milhollan, J.K., Davin, L.B., Browse, J., Lewis, N.G. Phytochemistry (2005) [Pubmed]

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