ID 3.4.19.1 DE acylaminoacyl-peptidase. AN acylamino-acid-releasing enzyme. AN alpha-N-acylpeptide hydrolase. AN N-acylpeptide hydrolase. AN oxidized protein hydrolase. CA (1) Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of CA a polypeptide. CA (2) Internal cleavage of oxidized and glycated proteins. CC -!- This is a bifunctional serine protease that has exopeptidase activity CC against N(alpha)-acylated peptides and endopeptidase activity against CC oxidized and glycated proteins. CC -!- In its exopeptidase mode the enzyme cleaves an N-acetyl or N-formyl CC amino acid from the N-terminus of a polypeptide. CC -!- This class of enzymes is evolutionary deeply conserved and is found CC in bacteria, archaea, animals and plants with different quartenary CC structures. CC -!- In humans, malfunction is linked to different types of cancer and CC sarcoma cell viability. CC -!- Belongs to peptidase family S9C. CC -!- Formerly EC 3.4.14.3. DR Q0IXP9, AARE1_ORYSJ; Q338C0, AARE2_ORYSJ; Q84LM4, AARE_ARATH ; DR P80227, ACPH_BOVIN ; P13798, ACPH_HUMAN ; Q8R146, ACPH_MOUSE ; DR P19205, ACPH_PIG ; P25154, ACPH_RABIT ; P13676, ACPH_RAT ; DR Q9YBQ2, APEH_AERPE ; //