peptidylprolyl isomerase EC#: 5.2.1.8; ChemWhat Code: 1383175

Product Name peptidylprolyl isomerase
Example Structure Example Structure of peptidylprolyl isomerase EC#: 5.2.1.8
Synonyms 12 kDa FKBP, 12.6 kDa FKBP, 13 kDa FKBP, 15 kDa FKBP, 19 kDa FK506-binding protein, 22 kDa FK506-binding protein, 25 kDa FKBP, 27 kDa membrane protein, 36 kDa FK506 binding protein, 40 kDa thylakoid lumen PPIase, 40 kDa thylakoid lumen rotamase, 51 kDa FK506-binding protein, 52 kDa FK506 binding protein, 54 kDa progesterone receptor-associated immunophilin, 65 kDa FK506-binding protein, At3g56070, CeCYP-16, CGI-124, Cgl0830, Chl-Mip, Cj0596, CPH, CTHT_0005290, Cwc27, Cyclophilin, Cyclophilin 18, cyclophilin 3, Cyclophilin 33, Cyclophilin A, Cyclophilin B, Cyclophilin C, Cyclophilin cyp2, cyclophilin H, cyclophilin hCyp-18, Cyclophilin homolog, cyclophilin J, Cyclophilin ScCypA, Cyclophilin ScCypB, Cyclophilin-10, Cyclophilin-11, Cyclophilin-40, Cyclophilin-60, cyclophilin-A, cyclophilin-D, Cyclophilin-like protein Cyp-60, Cyclophilin-related protein, Cyclosporin A-binding protein, Cyp, CYP-3, CYP-40, CYP-5, CYP-6, cyp-A, CYP-S1, Cyp1, Cyp18, Cyp19-3, Cyp2, CYP20-2, CYP20-3, Cyp3, Cyp3 PPIase, Cyp40, CyPA, CypA-1, CyPB, CyPJ, DDB_G0268618, Dod, EF0685, EF1534, EF2898, Estrogen receptor binding cyclophilin, FF1 antigen, FK506 binding protein 12, FK506 binding protein 35, FK506-binding protein, FKBP, FKBP 12, FKBP-12, FKBP-12.6, FKBP-13, FKBP-15, FKBP-19, FKBP-21, FKBP-22, FKBP-23, FKBP-25, FKBP-36, FKBP-51, FKBP-70, FkbP10, FKBP12, FKBP13, FKBP17, FKBP1B, FKBP22, FKBP25, FKBP3, FKBP33, FKBP35, FKBP38, FKBP51, FKBP52, FKBP52 protein, FKBP54, FKBP59, FKBP65, FKBP65RS, FKBP77, FklB, FkpA, h Par14, HBI, HcCYP, hCyP33, Histidine rich protein, hPar14, hPin1, HSP binding immunophilin, HSP90-binding immunophilin, Immunophilin FKBP12, Immunophilin FKBP12.6, Immunophilin FKBP36, Immunophilin FKBP65, Isomerase, peptidylprolyl cis-trans, L.p.Cyp18, Macrolide binding protein, Macrophage infectivity potentiator, mimicyp, MIP, mip-like peptidyl-prolyl cis-trans isomerase, More, MtFK, MtFKBP17, mzFKBP-66, Ng-MIP, NIMA-1, Nucleolar proline isomerase, OvCYP-16, p17.7, P31, P54, p59 protein, Par10, Par14, Par27, Par45, Parvulin, Parvulin 14, parvulin-like protein, parvulin-type peptidyl-prolyl isomerase, parvulin1 4, pCYP B, Peptide bond isomerase, peptidyl prolyl cis-trans isomerase, peptidyl prolyl isomerase-like protein 1, Peptidyl-prolyl cis-trans isomerase, peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Peptidyl-prolyl cis-trans isomerase plp, Peptidyl-prolyl cis-trans isomerase surA, peptidyl-prolyl cis/trans isomerase, Peptidyl-prolyl cis/trans isomerase EPVH, peptidyl-prolyl cis/trans isomerase NIMA-interacting 1, peptidyl-prolyl isomerase, peptidyl-prolyl isomerase 1, peptidylproline cis-trans-isomerase, peptidylprolyl cis,trans-isomerase, Peptidylprolyl cis-trans isomerase, peptidylprolyl cis/trans isomerase, peptidylprolyl isomerase, PfCyP, Pin1, PIN1-type parvulin 1, PIN1At, PinA, Planta-induced rust protein 28, Plp, PP2A phosphatase activator, PpiA, PPIase, PPIase Pin1, PPIase Pin4, PpiB, PPIC, PpiD, PPIE, PPIF, PPIG, PPIH, PPIL1, PPWD1, Proline rotamase, prolyl cis-trans isomerase, prolyl-peptidyl isomerase, protein phosphatase 2A phosphatase activator, Proteins, cyclophilins, Proteins, specific or class, cyclophilins, PrsA, Ptf1/Ess1, PtpA, PvFKBP35, Rapamycin-binding protein, Rapamycin-selective 25 kDa immunophilin, ROF2, Rotamase, Rotamase Pin1, Rotamase Pin4, Rotamase plp, S-cyclophilin, S1205-06, SAUSA300_0857, SCYLP, SDCCAG-10, sFkpA, SlrA, SLyD, SmCYP A, SmCYP B, Smp17.7, SP18, spliceosome-associated protein CWC27 homolog, SurA, TcFKBP18, TF, TLP20, trigger factor, TTHA0346, WHP, Ypa
EC Number 5.2.1.8
CAS Registry Number 95076-93-0
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.
Cofactor
History
Reactions Peptidylproline (omega=180) = peptidylproline (omega=0).

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