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cytosol aminopeptidase; leucine aminopeptidase-3; LAP3; proline aminopeptidase; peptidase S (LAP3, LAPEP, PEPS)

Function: - presumably involved in the processing & regular turnover of intracellular proteins - catalyzes the removal of unsubstituted N-terminal amino acids from various peptides - removes mostly leucine & other hydrophobic residues - release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including pro although not Arg or Lys, & Yaa may be pro - amino acid amides & methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low - release of N-terminal proline from a peptide Cofactor: - binds 2 Zn+2 per subunit - one Zn+2 ion is tightly bound & essential for enzyme activity; the 2nd metal coordination site can be occupied by Zn+2, Mg+2 or Mn+2 to give enzymes of different activities (putative) Structure: - homohexamer - belongs to the peptidase M17 family Compartment: cytoplasm Alternative initiation: - named isoforms=2 Expression: - upregulated 3-fold after 14 days of environmental enrichment in mice [3]. Pathology: - serum levels elevated in hepatobiliary disease - no elevation of serum levels in bone disease Note: initiator methionine is removed

General

aminopeptidase oligomerizing protein

Properties

SIZE: entity length = 519 aa MW = 56 kD COMPARTMENT: cytoplasm MOTIF: Zn+2-binding site SITE: 282-282 Zn+2-binding site SITE: 287-287 lysine residue {K294} Zn+2-binding site SITE: 305-305 Zn+2-binding site SITE: 364-364 Zn+2-binding site SITE: 366-366 arginine residue {R368}

Database Correlations

OMIM 151300 UniProt P28838 ENZYME correlations

References

  1. Taylor A. Aminopeptidases: structure and function. FASEB J. 1993 Feb 1;7(2):290-8. Review. PMID: 8440407
  2. Clinical Diagnosis & Management by Laboratory Methods, J.B. Henry (ed), W.B. Saunders Co., Philadelphia, PA. 1991, pg 263
  3. Rampon C, Jiang CH, Dong H, Tang YP, Lockhart DJ, Schultz PG, Tsien JZ, Hu Y. Effects of environmental enrichment on gene expression in the brain. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12880-4. PMID: 11070096
  4. UniProt :accession P28838