Dual activities of ACC synthase: Novel clues regarding the molecular evolution of ACS genes

Ethylene plays profound roles in plant development. The rate-limiting enzyme of ethylene biosynthesis is 1-aminocyclopropane-1-carboxylate (ACC) synthase (ACS), which is generally believed to be a single-activity enzyme evolving from aspartate aminotransferases. Here, we demonstrate that, in addition to catalyzing the conversion of S-adenosyl-methionine to the ethylene precursor ACC, genuine ACSs widely have C-beta-S lyase activity. Two N-terminal motifs, including a glutamine residue, are essential for conferring ACS activity to ACS-like proteins. Motif and activity analyses of ACS-like proteins from plants at different evolutionary stages suggest that the ACC-dependent pathway is uniquely developed in seed plants. A putative catalytic mechanism for the dual activities of ACSs is proposed on the basis of the crystal structure and biochemical data. These findings not only expand our current understanding of ACS functions but also provide novel insights into the evolutionary origin of ACS genes.

Automated summary

Genuine ACSs not only catalyze the conversion of S-adenosyl-methionine to the ethylene precursor ACC, but also widely have C-beta-S lyase activity. Analysis of ACS-like proteins from plants at different evolutionary stages suggests that the ACC-dependent pathway is uniquely developed in seed plants.