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A digestive prolyl carboxypeptidase in Tenebrio molitor larvae

Permanent URL:
http://handle.nal.usda.gov/10113/56702
File:
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Abstract:
Prolyl carboxypeptidase (PRCP) is a lysosomal proline specific serine peptidase that also plays a vital role in the regulation of physiological processes in mammals. In this report, we isolate and characterize the first PRCP in an insect. PRCP was purified from the anterior midgut of larvae of a stored product pest, Tenebrio molitor, using a three-step chromatography strategy, and it was determined that the purified enzyme was a dimer. The cDNA of PRCP was cloned and sequenced, and the predicted protein was identical to the proteomic sequences of the purified enzyme. The substrate specificity and kinetic parameters of the enzyme were determined. The T. molitor PRCP participates in the hydrolysis of the insect’s major dietary proteins, gliadins, and is the first PRCP to be ascribed a digestive function. Our collective data suggest that the evolutionary enrichment of the digestive peptidase complex in insects with an area of acidic to neutral pH in the midgut is a result of the incorporation of lysosomal peptidases, including PRCP.
Author(s):
Irina A. Goptar , Dmitry A. Shagin , Irina A. Shagina , Elena S. Mudrik , Yulia A. Smirnova , Mikhail A. Belozersky , Yakov E. Dunaevsky , Brenda Oppert
Subject(s):
Tenebrio molitor , amino acid sequences , complementary DNA , dietary protein , digestive enzymes , enzyme activity , gliadin , hydrolysis , larvae , midgut , nucleotide sequences , pH , serine-type carboxypeptidases , storage insects , substrate specificity
Source:
Insect biochemistry and molecular biology 2013 v.43 no.6
Language:
English
Year:
2013
Collection:
Journal Articles, USDA Authors, Peer-Reviewed
Rights:
Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.