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ARS Home » Plains Area » Manhattan, Kansas » Center for Grain and Animal Health Research » Stored Product Insect and Engineering Research » Research » Publications at this Location » Publication #286307
Title: A digestive prolyl carboxypeptidase in Tenebrio molitor larvae

Author
item GOPTAR, IRINA - Moscow State University
item SHAGIN, DMITRY - Institute Of Bioorganic Chemistry
item SHAGINA, IRINA - Evrogen Jsc
item MUDRIK, ELENA - Evrogen Jsc
item SMIRNOVA, YULIA - Moscow State University
item ZHUZHIKOV, DMITRY - Moscow State University
item BELOZERSKY, MIKHAIL - Moscow State University
item DUNAEVSKY, YAKOV - Moscow State University
item Oppert, Brenda
item FILIPPOVA, IRINA YU. - Moscow State University
item ELPIDINA, ELENA - Moscow State University

Submitted to: Journal of Insect Biochemistry and Molecular Biology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/28/2013
Publication Date: 4/23/2013
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 Insect Biochemistry and Molecular Biology. 43(6): 501-509. http://dx.doi.org/10.1016/j.ibmb.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.