leucine aminopeptidase

Leucine Aminopeptidase (microsomal), Porcine (EC 3.4.11.2), is an enzyme that specifically catalyzes the hydrolysis of N-terminal leucine residues in peptides and proteins.

LeucineAminopeptidase, Porcine (EC 3.4.11.1), is a proteolytic enzyme that hydrolyzes peptide bonds adjacent to free amino groups. This enzyme rapidly catalyzes the hydrolysis of peptides containing leucine and can also facilitate the breakdown of various peptides and proteins, releasing other amino acids from the N-terminus.

Actinonin is a natural antibacterial agent produced by Streptomyces, also serving as an effective PDF (peptide deformylase) inhibitor and apoptosis inducer. It inhibits APN (Aminopeptidase N), MMPs and heparin α, exhibiting antiproliferative and antitumour activity.

Bestatin (Ubenimex) competitively inhibits many aminopeptidases, including B, N and leucine aminopeptidases. Ubenimex is a microbial metabolite and dipeptide with potential immunomodulatory and antitumor activities. Aminopeptidases has been implicated in the process of cell adhesion and invasion of tumor cells. Therefore, inhibiting aminopeptidases may partially attribute to the antitumor effect of ubenimex. This agent also activates T lymphocyte, macrophage, and bone marrow stem cell as well as stimulates the release of interleukin-1 and -2, thus further enhances its antitumor activity.

L(+)-Leucinol is a potent inhibitor of leucine aminopeptidase.

Enocyanin, an anthocyanin extracted from grapes, exhibits inhibitory effects on leucine aminopeptidase, acid phosphatase, γ-glutamyl transpeptidase, and esterase activity.

L-Leucine-p-nitroanilide is a substrate. It is used for the colorimetric determination of leucine aminopeptidase.

L-Val-P is an effective inhibitor of leucine aminopeptidase (LAP) with a Ki value of 0.15 μM. It holds significant potential for research in HIV infection, inflammation, cataracts, and cancer.

Amastatin is a non-toxic inhibitor of aminopeptidase A and leucine aminopeptidase, and its Ki for aminopeptidase A is 1 µM .

Microginin 527, a compound found in Microcystis, is an inhibitor of protein phosphatase, ACE, and leucine aminopeptidase.

Cyanostatin B, a lipopeptide derived from cyanobacteria, acts as a leucine aminopeptidase (LAP) inhibitor with an IC50 of 12 ng/mL. It exhibits weak inhibitory effects on protein phosphatase (PP2A) and angiotensin-converting enzyme (ACE), with an IC50 of 130 μg/mL. While Cyanostatin B shows no toxicity to brine shrimp, it demonstrates cytotoxicity and genotoxicity in human liver cells in vitro. Furthermore, Cyanostatin B inhibits the proliferation of HepG cells, induces DNA single-strand breaks, and causes genomic instability.