Acetyl-CoA carboxylase (ACCase) (ACCase)

Acetyl-CoA carboxylase (ACCase) is a vital biotin-dependent enzyme that catalyzes the first committed step of fatty acid biosynthesis by converting acetyl-CoA into malonyl-CoA [Frontiers in Plant Science, 2023]. In grass weeds (Poaceae), the plastidic form of this enzyme is a homomeric protein, a structural feature that differentiates it from the heteromeric ACCase found in the plastids of most dicots [NIH, 2007]. This uniqueness allows for the selective targeting of grass weeds in broadleaf crops using herbicides such as aryloxyphenoxypropionates (FOPs), cyclohexanediones (DIMs), and phenylpyrazolines (DENs) [University of California, 2020]. These herbicides specifically inhibit the carboxyltransferase (CT) domain of the enzyme, leading to a cessation of lipid production and subsequent plant death [Cambridge University Press, 2025]. However, the efficacy of these compounds is increasingly challenged by the evolution of herbicide resistance, often caused by specific point mutations within the CT domain, such as Ile1781Leu or Asp2078Gly [NIH, 2021]. Understanding the structural and molecular basis of these interactions is essential for developing new herbicide chemistries and managing resistant weed populations in global agriculture [ResearchGate, 2020].

Other names

Acetyl-coenzyme A carboxylasePlastidic homomeric ACCaseACCase CT domainGraminicide targetPoaceae ACCase

Inhibition of the carboxyltransferase (CT) domain of the plastidic homomeric acetyl-CoA carboxylase enzyme, which prevents the conversion of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid biosynthesis [NIH, 2007; Cambridge University Press, 2025].