Thimet oligopeptidase

Thimet oligopeptidase
Identifiers
EC number 3.4.24.15
CAS number 110639-28-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Thimet oligopeptidase (EC 3.4.24.15, Pz-peptidase, soluble metalloendopeptidase, endo-oligopeptidase A, tissue-endopeptidase degrading collagenase-synthetic-substrate) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical 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

Thiol compounds activate this enzyme at low concentrations.

References

  1. Cicilini, M.A.; Ribeiro, M.J.F.; de Oliveira, E.B.; Mortara, R.A.; de Camargo, A.C.M. (1988). "Endooligopeptidase A activity in rabbit heart: generation of enkephalin from enkephalin containing peptides". Peptides (Fayetteville). 9: 945–955. doi:10.1016/0196-9781(88)90072-1. PMID 3244563.
  2. Orlowski, M.; Reznik, S.; Ayala, J.; Pierotti, A.R. (1989). "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: 951–958. PMID 2803255.
  3. Barrett, A.J.; Brown, M.A. (1990). "Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase". Biochem. J. 271: 701–706. PMID 2123097.
  4. Pierotti, A.; Dong, K.W.; Glucksman, M.J.; Orlowski, M.; Roberts, J.L. (1990). "Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15". Biochemistry. 29: 10323–10329. doi:10.1021/bi00497a006. PMID 2261476.
  5. Tisljar, U.; Barrett, A.J. (1990). "Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit". Biochem. J. 267: 531–533. PMID 2185743.
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