acylaminoacyl-peptidase EC#: 3.4.19.1; ChemWhat Code: 1380419
| Product Name | acylaminoacyl-peptidase |
| Example Structure |  |
| Synonyms | AAP, AARE, AARE/OPH, AAREP, AcpH, acyl peptide hydrolase, Acyl-peptide hydrolase, acyl-peptide releasing enzyme, acylamino acid-releasing enzyme, acylamino acid-releasing enzyme/oxidized protein hydrolase, acylamino-acid-releasing enzyme, acylaminoacyl peptidase, Acylaminoacyl-peptidase, acylpeptide hydrolase, acylpeptide hydrolase/esterase, alpha-N-acylpeptide hydrolase, ApAAP, apAPH, APEH, APEH-1, apeH-2, APEH-3, APEH-3Ss, APEHs, APH, APHdr, AtAARE, cAARE, DNF15S2 protein, N-acylaminoacyl-peptide hydrolase, N-acylpeptide hydrolase, N-formylmethionine (fMet) aminopeptidase, OP85, PhAAP, pi-APH, PM hydrolase, PMH, SpAAP, sso2141, SSO2693, ST0779 |
| EC Number | 3.4.19.1 |
| CAS Registry Number | 73562-30-8 |
| Comments | Active at neutral pH. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of?N-acetylalanine from peptides. Displays dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of mis-recognition of the glycyl residue as an uncharged?N-acyl group. Inhibited by diisopropyl fluorophosphate. In peptidase family?S9?(prolyl oligopeptidase family). Formerly EC?3.4.14.3. |
| Cofactor | |
| History | |
| Reactions | Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. |
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