| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1982228 | Insect Biochemistry and Molecular Biology | 2013 | 9 Pages |
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.
Graphical abstractFigure optionsDownload full-size imageDownload high-quality image (150 K)Download as PowerPoint slideHighlights► The first prolyl carboxypeptidase (PRCP) from the midgut of Tenebrio molitor larvae was purified and characterized. ► The gene encoding the PRCP was cloned and sequenced. ► Digestion of proline-rich dietary proteins was determined to be a new function of PRCP in a stored product pest. ► Evolution of digestive complex in insects with slightly acidic midgut pH may include incorporation of lysosomal peptidases.
