EC 5.2.1.8 - Peptidylprolyl isomerase

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IntEnz Enzyme Nomenclature
EC 5.2.1.8

Names

Accepted name:
peptidylprolyl isomerase
Other names:
PPIase
cyclophilin [misleading]
peptide bond isomerase
peptidyl-prolyl cis-trans isomerase
rotamase
peptidylprolyl cis-trans isomerase
Systematic name:
peptidylproline cis-trans-isomerase

Reaction

Comments:

The first type of this enzyme found [1] proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00154 , PROSITE:PDOC00426 , PROSITE:PDOC00840
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003755
CAS Registry Number: 95076-93-0
UniProtKB/Swiss-Prot: (1517) [show] [UniProt]

References

  1. Fischer, G. and Bang, H.
    The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase.
    Biochim. Biophys. Acta 828: 39-42 (1985). [PMID: 3882150]
  2. Fischer, G., Bang, H. and Mech, C.
    [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides].
    Biomed. Biochim. Acta 43: 1101-1111 (1984). [PMID: 6395866]
  3. Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T. and Schmid, F.X.
    Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.
    Nature 337: 476-478 (1989). [PMID: 2492638]
  4. Takahashi, N., Hayano, T. and Suzuki, M.
    Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin.
    Nature 337: 473-475 (1989). [PMID: 2644542]
  5. Hennig, L., Christner, C., Kipping, M., Schelbert, B., Rucknagel, K.P., Grabley, S., Kullertz, G. and Fischer, G.
    Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone.
    Biochemistry 37: 5953-5960 (1998). [PMID: 9558330]
  6. Fischer, G.
    Peptidyl-prolyl cis/trans isomerases and their effectors.
    Angew. Chem. Int. Ed. Engl. 33: 1415-1436 (1994).
  7. Harrison, R.K. and Stein, R.L.
    Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes.
    Biochemistry 29: 3813-3816 (1990). [PMID: 1693856]
  8. Eisenmesser, E.Z., Bosco, D.A., Akke, M. and Kern, D.
    Enzyme dynamics during catalysis.
    Science 295: 1520-1523 (2002). [PMID: 11859194]

[EC 5.2.1.8 created 1989, modified 2002]