Abstract
The inhibitory effects of flavonoids on the activity of two photosynthetic enzymes such as phosphoenolpyruvate carboxylase (PEPCase) and NADP-dependent malic enzyme (NADP-ME) were evaluated. The glycosylation of hydroxyl groups on the flavonoids resulted in compounds that behaved as gradually weaker inhibitors with increased size of the substituent. Quercetin and baicalein showed a competitive inhibition pattern vs. NADP+ for NADP-ME, and a similar model for both tlavonoids vs. phosphoenolpyruvate (PEP) was observed when tested on PEPCase. Ki for NADP-ME inhibition at pH 7.0 were 0.83 μM and 1.54 μM for quercetin and baicalein, respectively. Ki for PEPCase inhibition were 0.17 μM and 0.79 μM (quercetin and baicalein, respectively), indicating that these compounds are the most potent inhibitors described for this carboxylase. I50 values for these and other flavonoids were in the micromolar range. A tentative physiological role for the inhibitory effects observed on PEPCase is discussed.
