Premium
Direct and selective small‐molecule inhibition of photosynthetic PEP carboxylase: New approach to combat C 4 weeds in arable crops
Author(s) -
Paulus Judith Katharina,
Förster Kerstin,
Groth Georg
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.04.043
Subject(s) - phosphoenolpyruvate carboxylase , photosynthesis , allosteric regulation , biochemistry , c4 photosynthesis , enzyme , chemistry , biology
Phosphoenolpyruvate carboxylase (PEPC) is a key enzyme of C 4 photosynthesis. Besides, non‐photosynthetic isoforms of PEPC are found in bacteria and all types of plants, although not in animals or fungi. A single residue in the allosteric feedback inhibitor site of PEPC was shown to adjust the affinity of the photosynthetic and non‐photosynthetic isoforms for feedback inhibition by metabolites of the C 4 pathway. Here, we applied computational screening and biochemical analyses to identify molecules that selectively inhibit C 4 PEPC, but have no effect on the activity of non‐photosynthetic PEPCs. We found two types of selective inhibitors, catechins and quinoxalines. Binding constants in the lower μM range and a strong preference for C 4 PEPC qualify the quinoxaline compounds as potential selective herbicides to combat C 4 weeds.