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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.
Entry Term(s)
Cytosol Aminopeptidase
L-Leucylnaphthylamidase
Leucine Aminopeptidase
Methoxyleucine Aminopeptidase
Peptidase S
Zinc-Manganese-Leucine Aminopeptidase
Registry Numbers
EC 3.4.11.1
0
Public MeSH Note
1999; see LEUCINE AMINOPEPTIDASE 1965-1998; PEPTIDASE S was indexed under AMINOPEPTIDASES 1979-1998; for LEUCYL-BETA-NAPTHYLAMIDASE see LEUCYL-BETA-NAPTHYLAMIDASE 1991-2009
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.