| EC |
3.4.21.26 |
| Accepted name: |
prolyl oligopeptidase |
| Reaction: |
Hydrolysis of —Pro┼ and to a lesser extent —Ala┼ in oligopeptides |
| Other name(s): |
post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase |
| Comments: |
Found in vertebrates, plants and Flavobacterium. Generally cytosolic, commonly activated by thiol compounds. Type example of peptidase family S9. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 72162-84-6 |
| References: |
| 1. |
Walter, R. and Yoshimoto, T. Postproline cleaving enzyme: kinetic studies of size and stereospecificity of its active site. Biochemistry 17 (1978) 4139–4144. [PMID: 708698] |
| 2. |
Nomura, K. Specificity of prolyl endopeptidase. FEBS Lett. 209 (1986) 235–237. [DOI] [PMID: 3539636] |
| 3. |
Moriyama, A., Nakanishi, M. and Sasaki, M. Porcine muscle prolyl endopeptidase and its endogenous substrates. J. Biochem. (Tokyo) 104 (1988) 112–117. [PMID: 2851585] |
| 4. |
Rennex, D., Hemmings, B.A., Hofsteenge, J. and Stone, S.R. cDNA cloning of porcine brain prolyl endopeptidase and identification of the active-site seryl residue. Biochemistry 30 (1991) 2195–2203. [PMID: 1900195] |
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| [EC 3.4.21.26 created 1978, modified 1981 (EC 3.4.22.18 created 1981, incorporated 1992)] |
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