Reaction Details
Reaction: Thumb
a [protein]-L-proline (ω = 180) = a [protein]-L-proline (ω = 0)
Enzymes:
External Links:
ResourceLink
PseudoCyc Reaction ID:PEPTIDYLPROLYL-ISOMERASE-RXN
References:
  • Eisenmesser EZ, Bosco DA, Akke M, Kern D (2002). "Enzyme dynamics during catalysis." Science 295(5559);1520-3. PMID: 11859194
  • Fischer G, Bang H, Mech C (1984). "[Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides]." Biomed Biochim Acta 43(10);1101-11. PMID: 6395866
  • Fischer G, Bang H (1985). "The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase." Biochim Biophys Acta 828(1);39-42. PMID: 3882150
  • Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX (1989). "Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins." Nature 337(6206);476-8. PMID: 2492638
  • Harrison RK, Stein RL (1990). "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(16);3813-6. PMID: 1693856
  • Hennig L, Christner C, Kipping M, Schelbert B, Rucknagel KP, Grabley S, Kullertz G, Fischer G (1998). "Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone." Biochemistry 37(17);5953-60. PMID: 9558330
  • Takahashi N, Hayano T, Suzuki M (1989). "Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin." Nature 337(6206);473-5. PMID: 2644542