| EC |
3.4.11.14 |
| Accepted name: |
cytosol alanyl aminopeptidase |
| Reaction: |
Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides |
| Other name(s): |
arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase |
| Comments: |
A puromycin-sensitive, Co2+-activated zinc-sialoglycoprotein that is generally cytosolic. Multiple forms are widely distributed in mammalian tissues and body fluids. In peptidase family M1 (membrane alanyl aminopeptidase family) |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 243859-94-1 |
| References: |
| 1. |
Starnes, W.L. and Behal, F.J. A human liver aminopeptidase. The amino acid and carbohydrate content, and some physical properties of a sialic acid containing glycoprotein. Biochemistry 13 (1974) 3221–3227. [PMID: 4841062] |
| 2. |
Kao, Y.J., Starnes, W.L. and Behal, F.J. Human kidney alanine aminopeptidase: physical and kinetic properties of a sialic acid containing glycoprotein. Biochemistry 17 (1978) 2990–2994. [PMID: 698181] |
| 3. |
Sidorowicz, W., Hsia, W.-C., Maslej-Zownir, M. and Behal, F.J. Multiple molecular forms of human alanine aminopeptidase: imunochemical properties. Clin. Chim. Acta 107 (1980) 245–256. [DOI] [PMID: 6108169] |
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| [EC 3.4.11.14 created 1978] |
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