APEH hydrolyses NAc-Ser-protein

Stable Identifier
R-HSA-5691512
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
1861871 The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase

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

Oncogene 1991
2006156 Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities

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

Proc. Natl. Acad. Sci. U.S.A. 1991
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
serine-type endopeptidase activity of APEH [cytosol]
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Activity
Orthologous Events
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