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Cat No.
NATE-0378
Description
Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, Escherichia coli (E. coli) LAP (also known as PepA or XerB), and the solanaceous-specific acidic LAP (LAP-A) in tomato (Solanum lycopersicum).
Abbr
LAP, Native (Porcine)
Alias
LAP
Source
Porcine kidney
Species
Porcine
Form
Type VI-S, lyophilized powder; Type IV-S, ammonium sulfate suspension
Enzyme Commission Number
EC 3.4.11.1
Bio-activity
Type VI-S, > 12 units/mg protein (biuret); Type IV-S, 10-40 units/mg protein (Bradford)
CAS No.
9054-63-1
Unit Definition
One unit will hydrolyze 1.0 μmole of L-leucine-p-nitroanilide to L-leucine and p-nitroaniline per min at pH 7.2 at 37°C. (At 25°C, approx. 40% of the activity at 37°C is obtained.) The activity obtained using L-leucine p-nitroanilide as substrate is 2-5 times that obtained with L-leucinamide as substrate.
Synonyms
Leucine Aminopeptidase, microsomal; 9054-63-1; leucine aminopeptidase; 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
