Description
Leucine aminopeptidase (LAP) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. It is called leucine aminopeptidase because it rapidly catalyzes the hydrolysis of leucine containing peptides. However, it also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins. The enzyme from porcine kidney has been extensively studied. It has a molecular weight of 255,000 and it consists of four subunits each having one atom of zinc.
Enzyme Commission Number
EC 3.4.11.1
Activity
>100 U/mg protein
Unit Definition
That amount of enzyme which catalyzes the hydrolysis of one micromole L-leucinamide per minute at 25°C at pH 8.5.
Storage
Stable when stored at 4°C. Do not freeze
Synonyms
Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP
Solubility
Soluble in distilled water or dilute buffer
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