Leucine Aminopeptidase, microsomal from porcine kidney

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.

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.

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.

Contains primarily phosphate buffer salts, pH 7.0

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.