The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 3.4.24.15     
Accepted name: thimet oligopeptidase
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 name(s): Pz-peptidase; soluble metalloendopeptidase; endo-oligopeptidase A; tissue-endopeptidase degrading collagenase-synthetic-substrate
Comments: Thiol compounds activate at low concentrations. Type example of peptidase family M3.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, 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]
[EC 3.4.24.15 created 1984 (EC 3.4.22.19 created 1989 and EC 3.4.99.31 created 1978 both incorporated 1992)]
 
 


Data © 2001–2014 IUBMB
Web site © 2005–2014 Andrew McDonald