Description
General description
Leucine Aminopeptidase (LAP) from porcine is a 320-kDa exopeptidase present in cytosol. It contains zinc in its structure and belongs to the M1 and M17 peptidase families. LAP display bi-lobed structure and has the catalytic domain at the C-terminus and a variable N-terminal domain.
Application
Leucine Aminopeptidase, microsomal from porcine kidney has been used in aminopeptidase N (APN) inhibitor screening assay in adenocarcinoma cell line ES-2 and in the inhibition kinetic studies with APN inhibitor.
Biochem/physiol Actions
Leucine Aminopeptidase (LAP) catalyzes protein hydrolysis at the leucine residue at N-terminal. An altered level of LAP is implicated in tumor proliferation and progression. LAP is a potential biomarker for ovarian epithelial cancer therapy. Porcine LAP hydrolyzes glycine and arginine substrates.
Physical form
Contains primarily phosphate buffer salts, pH 7.0
Other Notes
One unit will hydrolyze 1.0 μmole of L-leucine-p-nitroanilide to L-leucine and p-nitroaniline per min at pH 7.2 at 37 °C. (At 25 °C, approx. 40% of the activity at 37 °C is obtained.) The activity obtained using L-leucine p-nitroanilide as substrate is 2-5 times that obtained with L-leucinamide as substrate.