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Leucyl Aminopeptidase

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.

Year introduced: 1999(1965)

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Subheadings:

Tree Number(s): D08.811.277.656.350.100.511, D08.811.277.656.350.555.700, D08.811.277.656.675.555.700

MeSH Unique ID: D007931

Registry Number: EC 3.4.11.1

Entry Terms:

  • Aminopeptidase, Leucyl
  • Cytosol Aminopeptidase
  • Aminopeptidase, Cytosol
  • L-Leucylnaphthylamidase
  • Leucine Aminopeptidase
  • Aminopeptidase, Leucine
  • Zinc-Manganese-Leucine Aminopeptidase
  • Aminopeptidase, Zinc-Manganese-Leucine
  • Zinc Manganese Leucine Aminopeptidase
  • Peptidase S
  • Methoxyleucine Aminopeptidase
  • Aminopeptidase, Methoxyleucine

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