Leucine methyl ester is a powerful allosteric activator of the neutral amino acid cotransport system in Bombyx mori larval midgut.

We have identified three methyl esters that have a potent stimulatory effect on the cotransport system responsible for the absorption of most essential amino acids in the silkworm Bombyx mori. L-Leucine methyl ester, the most powerful activator, determined a large dose-dependent, K(+)-independent increase of leucine uptake into midgut brush border membrane vesicles. Kinetic experiments revealed non-essential mixed-type activation, with K(a) values of 27+/-2 and 47+/-8 microM in the presence and in the absence of K(+), respectively. The activation increased K(m) twofold, and V(max) up to 18-fold depending upon the experimental conditions. Leucine uptake mediated by the amino acid uniport appears to be unaffected by the activator.