APEH hydrolyses NAc-Ser-protein

Stable Identifier
Reaction [transition]
Homo sapiens
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Protein acetylation, which can occur during or after polypeptide chain biosynthesis, helps protect the intracellular proteins from proteolysis. Acylamino-acid-releasing enzyme (APEH) is a cytosolic enzyme able to catalyse the preferential hydrolysis of terminal acetylated amino acids from small acetylated peptides. APEH prefers substrates with acetylated methionine, alanine and serine residues. Hydrolysis produces an acetylated amino acid and a N-terminus protein (Jones et al. 1991). APEH expression is reduced in renal cell carcinoma therefore may represent a tumor suppressor gene, whose loss contributes to the development of renal cell carcinoma (Erlandsson et al. 1991). The hydrolysis of an acetylated serine residue (NAc-Ser-protein) is shown here.

Literature References
PubMed ID Title Journal Year
2006156 Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities

Popowicz, AM, Jones, WM, Bossa, F, Schneewind, O, Scaloni, A, Manning, JM

Proc. Natl. Acad. Sci. U.S.A. 1991
1861871 The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase

Boldog, F, Erlandsson, R, Jörnvall, H, Sümegi, J, Persson, B, Zabarovsky, ER, Klein, G, Allikmets, RL

Oncogene 1991
Catalyst Activity

serine-type endopeptidase activity of APEH [cytosol]

Orthologous Events
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