Dipeptidyl Peptidase III human

Human dipeptidyl peptidase III has been used in a study to assess the effect of entropy-driven binding of opioid peptides on large domain motion in human dipeptidyl peptidase III. Human dipeptidyl peptidase III has also been used in a study to investigate Ets-1/Elk-1 as a critical mediator of its transcription in human glioblastoma cells.

DPP III is a cytosolic zinc-exopeptidase that is involved in the intracellular protein catabolism of eukaryotes. The enzyme is a monomeric acidic protein with a molecular mass of approximately 82,000 Da and a pI of 4.5-4.6. It is sensitive to freezing and temperatures above 40 °C. It is found to be inhibited by metallo-chelators and sulfydryl reagents. The activity can be restored by divalent cations and thiol compounds. It has a particularly high affinity for angiotensin III. It acts as a post-proline-cleaving enzyme on endomorphins.

One unit will hydrolyze 1.0 picomole of Arg-Arg-AMC per minute at pH 7.5 at 25 deg °C

Supplied as a solution in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 18 mM glutathione, 10% glycerol and 3 mM DTT.