EC 3.4.24.15 - Thimet oligopeptidase

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IntEnz Enzyme Nomenclature
EC 3.4.24.15

Names

Accepted name:
thimet oligopeptidase
Other names:
Pz-peptidase
endo-oligopeptidase A
soluble metalloendopeptidase
tissue-endopeptidase degrading collagenase-synthetic-substrate
Systematic name:

Reaction

Cofactor

Comments:

Thiol compounds activate at low concentrations. Type example of peptidase family M3. Formerly also EC 3.4.22.19 and EC 3.4.99.31.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00129
Structural data: CSA , EC2PDB
CAS Registry Number: 110639-28-6
UniProtKB/Swiss-Prot:

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: 945-955 (1988). [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: 951-958 (1989). [PMID: 2803255]
  3. Barrett, A.J. and Brown, M.A.
    Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase.
    Biochem. J. 271: 701-706 (1990). [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: 10323-10329 (1990). [PMID: 2261476]
  5. Tisljar, U. and Barrett, A.J.
    Thiol-dependent metallo-endopeptidase characteristics of Pz-peptidase in rat and rabbit.
    Biochem. J. 267: 531-533 (1990). [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)]