ARS | Publication request: A digestive prolyl carboxypeptidase in Tenebrio molitor larvae

Submitted to: Journal of Biological Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: February 28, 2013
Publication Date: April 23, 2013
Citation: Goptar, I.A., Shagin, D.A., Shagina, I.A., Mudrik, E.S., Smirnova, Y.A., Zhuzhikov, D.P., Belozersky, M.A., Dunaevsky, Y.E., Oppert, B.S., Filippova, I., Elpidina, E.N. 2013. A digestive prolyl carboxypeptidase in Tenebrio molitor larvae. Journal of Biological Chemistry. 43(6): 501-509. http://dx.doi.org/10.1016/j.bmb.2013.02.009.

Interpretive Summary: We are studying enzymes in insects to determine their function and to determine whether we can interfere with the way that they operate to develop new insect control methods. We examined the function of one enzyme, prolyl carboxypeptidase (PRCP), in the yellow mealworm, a pest of stored products. We discovered that PRCP aids in the digestion of proteins in cereals. Our data indicate that the enzyme may be a target for the development of new control methods to prevent damage to stored grains and products.

Technical Abstract: Prolyl carboxypeptidase (PRCP) was purified from the anterior midgut of larvae of a stored product pest, Tenebrio molitor. The cDNA of PRCP was cloned, and the predicted protein was identical to the proteomic sequences of the purified enzyme. The substrate specificity of the enzyme was studied, and kinetic parameters of the substrate hydrolysis were calculated. T. molitor enzyme participates in the hydrolysis of the insect’s major dietary proteins, gliadins, and is the first digestive PRCP to be described.