and to a lesser extent —Ala in oligopeptides
Reaction: Hydrolysis of —Pro and to a lesser extent —Ala in oligopeptides
Other names: 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, KEGG, MEROPS, Metacyc, 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. [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]