Ett zinkhaltigt enzym av hydrolasklassen som katalyserar frånkopplingen av den aminosyra som utgör N-terminalen hos de flesta L-peptider, i synnerhet sådana vars N-terminal har leucin som restsekvens, men inte dem med lysin eller arginin. Denna process äger rum i vävnadscellscytosol, med hög aktivitet i tolvfingertarmen, levern och njurarna. EC 3.4.11.1.
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.
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Aminopeptidase, Leucyl — L-Leucylnaphthylamidase — Zinc-Manganese-Leucine Aminopeptidase — Aminopeptidase, Zinc-Manganese-Leucine — Zinc Manganese Leucine Aminopeptidase — Peptidase S — Cytosol Aminopeptidase — Aminopeptidase, Cytosol — Leucine Aminopeptidase — Aminopeptidase, Leucine — Methoxyleucine Aminopeptidase — Aminopeptidase, Methoxyleucine