APEH
APEH (acylaminoacyl-peptide hydrolase, also called acylamino-acid-releasing enzyme or acylpeptide hydrolase) is a cytoplasmic aminopeptidase that degrades N-acylated peptides. It removes N-acetylated and N-formylated amino acids from peptide N-termini and also contributes to the breakdown of damaged proteins. Browse Assay Genie's current range of APEH research reagents below, or read on for the biology behind the target.
APEH is an aminopeptidase involved in the degradation of N(alpha)-acylated peptides. It acts as an exopeptidase on N-formyl and N-acetyl peptides, with a preference for dipeptide substrates. The enzyme hydrolyses the N-terminal peptide bond of an N-acetylated peptide, releasing an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. It also hydrolyses N-formylated peptides, which are likely to arise from N-terminal proteolytic cleavage of bacterial and mitochondrial proteins.
APEH may act sequentially with ACY1 in the turnover of N-acylated peptides. APEH first releases the N-acylamino acid from the peptide, and ACY1 then hydrolyses that N-acylamino acid into a free amino acid and a carboxylate. The NCBI Gene summary describes the same two-step route, with an aminoacylase processing the acetyl amino acid to acetate and a free amino acid. Beyond exopeptidase activity, APEH shows endopeptidase activity involved in degrading oxidised and glycated proteins, and it can play an important role in destroying oxidatively damaged proteins in living cells.
The human APEH gene encodes a 732-residue subunit, and the active enzyme is a homotetramer of about 300 kDa. The protein belongs to the peptidase S9C family and is found in the cytoplasm. The gene lies in the 3p21 region, close to the aminoacylase gene, and deletions at this locus are associated with reduced aminoacylase activity. Deletions of the APEH locus have been reported in several carcinomas, including small cell lung carcinoma and renal cell carcinoma. Earlier symbols and names include D3F15S2, DNF15S2, D3S48E and N-acylaminoacyl-peptide hydrolase.
APEH removes N-acetylated and N-formylated amino acids from peptides, and works with ACY1 to return them to free amino acids.
APEH shows endopeptidase activity towards oxidised and glycated proteins and can help clear oxidatively damaged proteins in cells.
APEH hydrolyses N-formylated peptides likely derived from N-terminal cleavage of bacterial and mitochondrial proteins.
Deletions at the APEH locus on chromosome 3p21 occur in carcinomas such as small cell lung carcinoma and renal cell carcinoma.
APEH is a cytoplasmic aminopeptidase that cleaves the N-terminal acylated amino acid from N-acetylated or N-formylated peptides, preferring dipeptide substrates. It favours Ac-Ala, Ac-Met and Ac-Ser, and also degrades oxidised and glycated proteins through endopeptidase activity.
APEH is also called acylamino-acid-releasing enzyme, acylpeptide hydrolase and N-acylaminoacyl-peptide hydrolase. Earlier gene symbols include D3F15S2, DNF15S2 and D3S48E. Its EC number is 3.4.19.1, and it belongs to the peptidase S9C family.
Deletions of the APEH locus at 3p21 are found in carcinomas, including small cell lung carcinoma and renal cell carcinoma. Orthologues exist in mouse and rat, both named Apeh; check the datasheet of any product for its validated reactivity.
Aminoacylases and other peptidases that work alongside APEH in the turnover of N-acylated peptides.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P13798; product specifications from Assay Genie datasheets.