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Background  Juvenile hormones (JH) regulate development and reproductive maturation in insects. JHs are synthesized through the mevalonate pathway (MVAP), an ancient metabolic pathway present in the three domains of life. Mevalonate kinase (MVK) is a key enzyme in the MVAP. MVK catalyzes the synthesis of phosphomevalonate (PM) by transferring the γ-phosphoryl group from ATP to the C 5  hydroxyl oxygen of mevalonic acid (MA). Despite the importance of MVKs, these enzymes have been poorly characterized in insects.    Results  We functionally characterized an  Aedes aegypti  MVK ( Aa MVK) expressed in the  corpora allata  (CA) of the mosquito.  Aa MVK displayed its activity in the presence of metal cofactors. Different nucleotides were used by  Aa MVK as phosphoryl donors. In the presence of Mg 2+ , the enzyme has higher affinity for MA than ATP. The activity of  Aa MVK was regulated by feedback inhibition from long-chain isoprenoids, such as geranyl diphosphate (GPP) and farnesyl diphosphate (FPP).    Conclusions    Aa MVK exhibited efficient inhibition by GPP and FPP (K i  less than 1 μM), and none by isopentenyl pyrophosphate (IPP) and dimethyl allyl pyrophosphate (DPPM). These results suggest that GPP and FPP might act as physiological inhibitors in the synthesis of isoprenoids in the CA of mosquitoes. Changing MVK activity can alter the flux of precursors and therefore regulate juvenile hormone biosynthesis.

Negative Feedbacks by Isoprenoids on a Mevalonate Kinase Expressed in the Corpora Allata of Mosquitoes