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.

Also Known As:

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

Enzymes and Coenzymes: 1
- Enzymes: 152586
  - Hydrolases: 2166
    - Peptide Hydrolases: 23957
      - Metalloproteases: 8276
        Metalloexopeptidases: 2
        Leucyl Aminopeptidase: 356
      - Exopeptidases: 68
        Aminopeptidases: 708
        Leucyl Aminopeptidase: 356
        Metalloexopeptidases: 2
        Leucyl Aminopeptidase: 356

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Disease

Drug/Important Bio-Agent (IBA)