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Your query returned 1 entry. Printable version
EC | 3.4.19.1 | ||||||||||||||||
Accepted name: | acylaminoacyl-peptidase | ||||||||||||||||
Reaction: | (1) cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide (2) internal cleavage of oxidized and glycated proteins |
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Other name(s): | acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase; oxidized protein hydrolase; acylpeptide hydrolase; AARE; AAP; OPH; AAH; APEH; ACPH | ||||||||||||||||
Comments: | This is a bifunctional serine protease that has exopeptidase activity against Nα-acylated peptides and endopeptidase activity against oxidized and glycated proteins. In its exopeptidase mode the enzyme cleaves an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. This class of enzymes is evolutionary deeply conserved and is found in bacteria, archaea, animals and plants with different quartenary structures. In humans, malfunction is linked to different types of cancer and sarcoma cell viability. In peptidase family S9 (prolyl oligopeptidase family). | ||||||||||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 73562-30-8 | ||||||||||||||||
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