Reaction: Preferential cleavage of bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5-15 residues
Other names: Pz-peptidase; soluble metalloendopeptidase; endo-oligopeptidase A; tissue-endopeptidase degrading collagenase-synthetic-substrate
Comment: Thiol compounds activate at low concentrations. Type example of peptidase family M3.
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 110639-28-6
References:
1. Cicilini, M.A., Ribeiro, M.J.F., de Oliveira, E.B., Mortara, R.A. and de Camargo, A.C.M. Endooligopeptidase A activity in rabbit heart: generation of enkephalin from enkephalin containing peptides. Peptides (Fayetteville) 9 (1988) 945-955. [PMID: 3244563]
2. Orlowski, M., Reznik, S., Ayala, J. and Pierotti, A.R. Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides. Biochem. J. 261 (1989) 951-958. [PMID: 2803255]
3. Barrett, A.J. and Brown, M.A. Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase. Biochem. J. 271 (1990) 701-706. [PMID: 2123097]
4. Pierotti, A., Dong, K.-W., Glucksman, M.J., Orlowski, M. and Roberts, J.L. Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15. Biochemistry 29 (1990) 10323-10329. [PMID: 2261476]
5. Tisljar, U. and Barrett, A.J. Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit. Biochem. J. 267 (1990) 531-533. [PMID: 2185743]