| Entry |
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| Name |
acylaminoacyl-peptidase;
acylamino-acid-releasing enzyme;
N-acylpeptide hydrolase;
N-formylmethionine (fMet) aminopeptidase;
alpha-N-acylpeptide hydrolase
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| Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Omega peptidases
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| Reaction(IUBMB) |
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
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| Comment |
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).
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| History |
EC 3.4.19.1 created 1978 as EC 3.4.14.3, transferred 1981 to EC 3.4.19.1
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| Orthology |
| K01303 | acylaminoacyl-peptidase |
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| Genes |
» show all
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| Reference |
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| Authors |
Tsunasawa S, Narita K, Ogata K. |
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| Title |
Purification and properties of acylamino acid-releasing enzyme from rat liver. |
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| Journal |
J Biochem (Tokyo) 77:89-102 (1975) |
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| Reference |
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| Authors |
Unger T, Nagelschmidt M, Struck H. |
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| Title |
N-Acetylaminoacyl-p-nitranilidase from human placenta. Purification and some properties. |
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| Journal |
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| Reference |
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| Authors |
Kobayashi K, Smith JA. |
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| Title |
Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction. |
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| Journal |
J Biol Chem 262:11435-45 (1987) |
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| Sequence |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 3.4.19.1 |
| ExPASy - ENZYME nomenclature database: | 3.4.19.1 |
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