Recombinant Human Acylamino-acid-releasing enzyme (APEH)

Function

Aminopeptidase involved in the degradation of N(alpha)-acylated peptides. Displays exopeptidase activity toward N-formyl and N-acetyl peptides with a preference for dipeptide substrates (By similarity). Catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus (PubMed:10719179, PubMed:1740429, PubMed:2006156). It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity). Hydrolyzes N-formylated peptides likely arising from N-terminal proteolytic cleavage of bacterial and mitochondrial proteins. May act sequentially with ACY1 in the degradation of N-acylated peptides: APEH first cleaves N-acylaminoacids from N-acylated peptides, then ACY1 further hydrolyzes the N-acylaminoacid into free aminoacid and a carboxylate (By similarity). Displays endopeptidase activity involved in the degradation of oxidized and glycated proteins (PubMed:10719179)

Subcellular Location

Cytoplasm

Tissue Specificity

Expressed in erythrocytes (at protein level)

Subunit

Homotetramer

• Mitta M. et al. The nucleotide sequence of human acylamino acid-releasing enzyme. — DNA Res. (1996)
• Fujino T. et al. Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase. — Biochim. Biophys. Acta (2000)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Naylor S.L. et al. The DNF15S2 locus at 3p21 is transcribed in normal lung and small cell lung cancer. — Genomics (1989)
• Scaloni A. et al. Structural investigations on human erythrocyte acylpeptide hydrolase by mass spectrometric procedures. — J. Protein Chem. (1999)
• Erlandsson R. et al. The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase. — Oncogene (1991)
• Jones W.M. et al. Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities. — Proc. Natl. Acad. Sci. U.S.A. (1991)
• Scaloni A. et al. Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme. — J. Biol. Chem. (1992)