| EC |
3.4.11.5 |
| Accepted name: |
prolyl aminopeptidase |
| Reaction: |
Release of N-terminal proline from a peptide |
| Other name(s): |
proline aminopeptidase; Pro-X aminopeptidase; cytosol aminopeptidase V; proline iminopeptidase |
| Comments: |
A Mn2+-requiring enzyme present in the cytosol of mammalian and microbial cells. In contrast to the mammalian form, the bacterial form of the enzyme (type example of peptidase family S33) hydrolyses both polyproline and prolyl-2-naphthylamide. The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1, leucyl aminopeptidase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-40-5 |
| References: |
| 1. |
Sarid, S., Berger, A. and Katchalski, E. Proline iminopeptidase. II. Purification and comparison with iminopeptidase (prolinase). J. Biol. Chem. 237 (1962) 2207–2212. [PMID: 14497218] |
| 2. |
Nordwig, A. and Mayer, H. The cleavage of prolyl peptidases by kidney peptidases. Hoppe-Seyler's Z. Physiol. Chem. 354 (1973) 380–383. [PMID: 4803482] |
| 3. |
Turzynski, A. and Mentlein, R. Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase. Eur. J. Biochem. 190 (1990) 509–515. [DOI] [PMID: 2373079] |
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| [EC 3.4.11.5 created 1965 as EC 3.4.1.4, transferred 1972 to EC 3.4.11.5] |
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