5.2.1.8: peptidylprolyl isomerase
This is an abbreviated version!
For detailed information about peptidylprolyl isomerase, go to the full flat file.
Word Map on EC 5.2.1.8
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5.2.1.8
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cyclosporine
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immunophilins
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isomerization
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calcineurin
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isomerases
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necrosis
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cardiac
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lymphocyte
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immunodeficiency
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capsid
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ryanodine
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t-cells
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steroid
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glucocorticoid
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alzheimer
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tetratricopeptide
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tacrolimus
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refolding
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hsp70
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mtor
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interactor
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virion
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imperfecta
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gapdh
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co-chaperone
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genorm
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dnak
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anti-hcv
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ptp
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groel
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legionella
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osteogenesis
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sarcoplasmic
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translocase
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heterocomplexes
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pneumophila
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voltage-dependent
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phosphorylation-dependent
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ns5a
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analysis
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ca2+-induced
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direct-acting
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sirolimus
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csa-induced
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proline-directed
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bestkeeper
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excitation-contraction
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medicine
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ribavirin
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emmprin
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normfinder
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ribosome-associated
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agriculture
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pharmacology
- 5.2.1.8
-
cyclosporine
-
immunophilins
-
isomerization
- calcineurin
- isomerases
- necrosis
- cardiac
- lymphocyte
- immunodeficiency
- capsid
-
ryanodine
- t-cells
- steroid
- glucocorticoid
- alzheimer
-
tetratricopeptide
- tacrolimus
-
refolding
- hsp70
- mtor
- interactor
- virion
- imperfecta
- gapdh
-
co-chaperone
-
genorm
- dnak
-
anti-hcv
- ptp
- groel
- legionella
-
osteogenesis
-
sarcoplasmic
- translocase
-
heterocomplexes
- pneumophila
-
voltage-dependent
-
phosphorylation-dependent
- ns5a
- analysis
-
ca2+-induced
-
direct-acting
- sirolimus
-
csa-induced
-
proline-directed
-
bestkeeper
-
excitation-contraction
- medicine
- ribavirin
-
emmprin
-
normfinder
-
ribosome-associated
- agriculture
- pharmacology
Reaction
peptidylproline (omega = 180)
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
ECTree
5.2.1.8 peptidylprolyl isomeraseAdvanced search results
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results (Engineering
Engineering on EC 5.2.1.8 - peptidylprolyl isomerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C129S
presence of dithiothreitol, 49% of wild-type activity, presence of H2O2, 84% of wild-type activity
C171S
presence of dithiothreitol, 25% of wild-type activity, presence of H2O2, 87% of wild-type activity
C176S
presence of dithiothreitol, 94% of wild-type activity, presence of H2O2, 231% of wild-type activity
C54S
presence of dithiothreitol, 40% of wild-type activity, presence of H2O2, 123% of wild-type activity
A82P
mutation in hinge region, 41% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea. Mutation affects both the shape and size of the protein significantly
C69A
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about one equivalent of 5-hydroxy-1,4-naphthoquinone results in complete inactivation of the mutant enzyme compared to two equivalent for the wild-type enzyme
E178V
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slightly more active than wild-type enzyme with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, as active as wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
F198A
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inactive with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, inactive in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
F233L
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inactive with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, less active than wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
G148D
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the FkpA313 mutant protein, which contains a G148D replacement in the PPIase domain, shows only a very low in vitro PPIase activity with both peptides (the activity amounts to 0.4 and 0.2% that of wild type enzyme)
I42S
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about 50% of wild-type peptidylprolyl isomerase activity, cells show moderate deficiency in nickel uptake under anaerobic conditions
I42S/F132Y
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almost complete loss of peptidylprolyl isomerase activity, retains most of hydrogenase activity and cells show moderate deficiency in nickel uptake under anaerobic conditions
I65P
mutation in hinge region, 6% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea. Mutation affects both the shape and size of the protein significantly
V72P
mutation in hinge region, 60% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea
Y15A
residue Tyr 15 is indispensable for dimerization ability, catalytic activity, and structure but contributes little to its inhibitor binding ability and stability
Y221F
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mutant enzyme shows 15% of the activity of the wild-type enzyme with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide as substrate, less active than wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
G148D
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the FkpA313 mutant protein, which contains a G148D replacement in the PPIase domain, shows only a very low in vitro PPIase activity with both peptides (the activity amounts to 0.4 and 0.2% that of wild type enzyme)
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C138A
site-directed mutagenesis, the mutant shows 93% of wild-type activity
C41A
site-directed mutagenesis, the mutant shows 104% of wild-type activity
C51A
site-directed mutagenesis, the mutant shows 93% of wild-type activity
C90A
site-directed mutagenesis, the mutant shows 35% of wild-type activity
F111A
site-directed mutagenesis, the mutant shows 30% of wild-type activity
F111Y
site-directed mutagenesis, the mutant shows 20% of wild-type activity
H131A
site-directed mutagenesis, the mutant shows 19% of wild-type activity
H134A
site-directed mutagenesis, the mutant shows 30% of wild-type activity
H48A
site-directed mutagenesis, the mutant shows 7.8% of wild-type activity
M107A
site-directed mutagenesis, the mutant shows 73% of wild-type activity
T130A
site-directed mutagenesis, the mutant shows 68% of wild-type activity
C138A
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site-directed mutagenesis, the mutant shows 93% of wild-type activity
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C51A
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site-directed mutagenesis, the mutant shows 93% of wild-type activity
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H131A
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site-directed mutagenesis, the mutant shows 19% of wild-type activity
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H134A
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site-directed mutagenesis, the mutant shows 30% of wild-type activity
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H48A
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site-directed mutagenesis, the mutant shows 7.8% of wild-type activity
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C113A
C113D
mutation does not compromise isoform Pin1 function in vivo nor does it abolish catalytic activity. C113 may not be the catalytic nucleophile
C113S
C115A
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Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C161A
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Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C52A
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Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
C62A
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Cys at position 52, 62, 115, and 161 are mutated individually to Ala and the purified mutant proteins to retain full affinity for cyclosporin A and equivalent catalytic efficiency as a rotamase
D155R
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mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
D158R
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mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
DELTA208-213
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dramatic reduction of peptidylprolyl isomerase activity and 400fold reduction of protein phosphatase 2A activation
F133A
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mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
F60A
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mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
G77H
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mutant enzyme has intact isomerase activity and cyclosporin A-binding activity. When complexed to cyclosporin A, the mutant enzyme displays only reduced affinity for calcineurin and much decreased inhibition of calcineurin phosphatase activity
H126Q
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mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
H47Q
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mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
H59F
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mutant supports viability in yeast complementation assay but displays significantly reduced growth in yeast compared to wild-type Pin1
H59L/H157A
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about 50% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, no activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
H59L/H157F
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about 5% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, 3% activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
H59L/H157L
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mutant supports viability in yeast complementation assay, mutation H157L rescues mutant H59L
H59L/H157S
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about 5% of wild-type activity with substrate Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide, no activity with substrate Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
K63A
P16S
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10fold decrease in ratio kcat/Km at 10°C. Mutant is extremely sensitive to guanidinium-HCl and shows increased susceptibility to urea. Folding time of the mutant is extended
P9Q/R13F/K17V/R18F
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mutant designed for crytallizability, crystal structure in complex with 1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
Q111A
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mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
R55A
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mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
S16A
S16A/Y23A
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the mutations of Pin1 protein do not affect the structure of Pin1 but abolishes the ability of the WW domain to bind pSer/pThr-Pro ligands
S16E
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mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H
S19A
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mutation abolishes phosphorylation and alters the subcellular localization from predominantly nuclear to significantly cytoplasmic
S19E
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mutant enzyme is localized around the nuclear envelope, but does not penetrate into the nucleoplasm, in vitro DNA-binding affinity is strongly reduced
V55R
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site-directed mutagenesis, the mutation increases the PPIase activity by a factor of 11
W121A
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mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q. Mutants enzymes H54Q, Q111A, F113A, and W121A retain 3-15% of the catalytic efficiency of the wild-type recombinant enzyme. The mutants R55A, F60A and H126Q, each retain less than 1% of the wild-type recombinant catalytic efficiency. The wild-type enzyme and the mutants R55A, F60A, F113A, and H126Q inhibit calcineurin in the presence of cyclosporin A, whereas W121A does not
W34A
Y82K
-
site-directed mutagenesis, the mutation decreases the PPIase activity by a factor of 7
R68/69A
mutant has lost the binding site to the phosphorylated Ser/Thre-Pro residues of substrates, still is able to decrease the transcriptional activity of FOXO3
W34A
mutant lacks the WW motif of the FOXO3 binding site, is not able to decrease the transcriptional activity of FOXO3
DELTA208-213
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almost no enzymic activity, 400fold less activity in the activation reaction of PP2A phosphatase
Y100A
site-directed mutagenesis, the mutant shows about 10% reduced activity compared to the wild-type enzyme
Y100E
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
Y100F
site-directed mutagenesis, the mutant shows about 10% reduced activity compared to the wild-type enzyme
Y100L
site-directed mutagenesis, the mutant shows about 70% reduced activity compared to the wild-type enzyme
Y100P
site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme
Y100R
site-directed mutagenesis, the mutant shows about 40% reduced activity compared to the wild-type enzyme
Y100W
site-directed mutagenesis, the mutant shows about 30% reduced activity compared to the wild-type enzyme
R62A
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overexpression of wild-type isoform CypB attenuates endoplasmic reticulum stress-induced cell death, whereas overexpression of isomerase activity-defective mutant R62A increases Ca2+ leakage from the endoplasmic reticulum and generation of reactive oxygen species and decreases mitochondrial membrane potential resulting in cell death
D205G
additional information
C113A
-
mutation in isomerase domain, catalytically inert. Mutation diminishes binding to brain-specifc protein BNIP-H
C113S
decrease in kcat, small in Km value. C113 may not be the catalytic nucleophile
K63A
-
mutant lacking isomerase activity. Wild-type inhibits FOXO4-induced expression of p27kip1, while mutant K63A does not
S16A
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mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H
W34A
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cells expressing Pin1 mutant W34A do not inhibit FOXO4 relocalization to the nucleus upon stimulation with hydrogen peroxide
W34A
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mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H
D205G
-
essential for petidyl-prolyl cis/trans isomerase activity and activation of PP2A phosphatase
D205G
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D205 is required for both peptidylprolyl isomerase activity and protein phosphatase 2A activation
additional information
construction of DNA T-insertion mutants. PPIase activity in the thylakoid lumen of the mutants lacking either AtFKBP13 or both AtFKBP13 and AtCYP20-2 is 10% and 2%, respectively, of wild-type activity. Residual PPIase activity detected in the double mutant originates from AtCYP20-3. None of the mutants differs from the wild-type plants when grown under normal, cold stress or high light conditions
additional information
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construction of DNA T-insertion mutants. PPIase activity in the thylakoid lumen of the mutants lacking either AtFKBP13 or both AtFKBP13 and AtCYP20-2 is 10% and 2%, respectively, of wild-type activity. Residual PPIase activity detected in the double mutant originates from AtCYP20-3. None of the mutants differs from the wild-type plants when grown under normal, cold stress or high light conditions
additional information
overexpression of ROF2 confers tolerance to intracellular acidification by increasing proton extrusion from cells. Expression of ROF2 activates K+ uptake, causing depolarization of the plasma membrane, which activates the electrogenic plasma membrane proton pump, H+-ATPase
additional information
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overexpression of ROF2 confers tolerance to intracellular acidification by increasing proton extrusion from cells. Expression of ROF2 activates K+ uptake, causing depolarization of the plasma membrane, which activates the electrogenic plasma membrane proton pump, H+-ATPase
additional information
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construction of a cj0596 deletion mutant derivative of strain 81-176, isolation of a revertant of this mutant by restoring the gene to its original chromosomal location using streptomycin counterselection. The cj0596 mutant strain demonstrates a slightly decreased growth rate and lower final growth yield, yet it is more motile and more invasive of human intestinal epithelial cells than wild-type, phenotype, overview
additional information
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construction of a cj0596 deletion mutant derivative of strain 81-176, isolation of a revertant of this mutant by restoring the gene to its original chromosomal location using streptomycin counterselection. The cj0596 mutant strain demonstrates a slightly decreased growth rate and lower final growth yield, yet it is more motile and more invasive of human intestinal epithelial cells than wild-type, phenotype, overview
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additional information
generation of genes ef2898, ef0685, and ef1534 deletion mutants
additional information
generation of genes ef2898, ef0685, and ef1534 deletion mutants
additional information
generation of genes ef2898, ef0685, and ef1534 deletion mutants
additional information
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generation of genes ef2898, ef0685, and ef1534 deletion mutants
additional information
the deletion mutant comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and exhibits chaperone activity. The deletion mutant comprising the C-terminal domain only is monomeric, and although it shows peptidylprolyl isomerase activity, it is devoid of chaperone function
additional information
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the deletion mutant comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and exhibits chaperone activity. The deletion mutant comprising the C-terminal domain only is monomeric, and although it shows peptidylprolyl isomerase activity, it is devoid of chaperone function
additional information
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genetic inactivation of isoforms FkpA, PpiA, PpiD, SurA results in a viable strain with decreased growth rate and increased susceptibility to certain antibodies. Expression of P and type 1 pili is severely diminished in the quadruple mutant as well as in absence of SurA alone
additional information
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the temperature-sensitive mutant FkpA43 confers 10% activity to colicin M at 30°C and no activity at 42°C, displays a 2fold lower PPIase activity than wild type FkpA for Phe-Pro-176-Val and a 5fold lower activity for Leu-Pro-260-Gly than for Phe-Pro-176-Val (measured at 10°C)
additional information
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construction of FKBP22 four helix alpha3 mutant variants by various in vitro probes, rFKBP22D5 and rFKBP22D30 are deletion mutants, while rFKBP22I3 and rFKBP22I6 are insertion mutants. The molecular dimensions, dimerization efficiencies, secondary structures, tertiary structures, stabilities, and protein folding abilities of all mutant proteins differ from those of wild-type rFKBP22, but the rapamycin binding affinities of the mutant proteins are affected very little
additional information
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the temperature-sensitive mutant FkpA43 confers 10% activity to colicin M at 30°C and no activity at 42°C, displays a 2fold lower PPIase activity than wild type FkpA for Phe-Pro-176-Val and a 5fold lower activity for Leu-Pro-260-Gly than for Phe-Pro-176-Val (measured at 10°C)
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additional information
silencing of isoform cyclophilin A by RNAi leads to a significant reduction in the body weight of engorged ticks and their failure to lay eggs
additional information
silencing of isoform cyclophilin A by RNAi leads to a significant reduction in the body weight of engorged ticks and their failure to lay eggs
additional information
silencing of isoform cyclophilin B by RNAi does not lead to detectable phenotypic changes
additional information
silencing of isoform cyclophilin B by RNAi does not lead to detectable phenotypic changes
additional information
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depletion of enzyme by siRNA reduces hormone-dependent transcription from both transfected reporters and an endogenous steroid receptor target gene. Depletion of enzyme in MCF-7 cells reduces the endogenous estrogen-dependent recruitment of p300 to the promoters of estrogen receptor-dependent genes. Enzyme overexpression enhances SRC-3 cellular turnover
additional information
analysis of residues conserved in natural Pin1 sequences and during unigenic evolution and screen for completely conserved residues in functional Pin1 mutants by complementation of Ess1 mutant in Saccharomyces cerevisiae
additional information
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analysis of residues conserved in natural Pin1 sequences and during unigenic evolution and screen for completely conserved residues in functional Pin1 mutants by complementation of Ess1 mutant in Saccharomyces cerevisiae
additional information
both hydrogen peroxide and heat stresses induce phosphorylation of neurofilament protein NF-H in transfected HEK-293 cells and primary cortical cultures. Knockdown of Pin1 by transfected Pin1 short interference RNA and dominant negative-Pin1 rescues the effect of stress-induced NF-H phosphorylation
additional information
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co-expression of cyclophilin B with TRPV6 channel protein in Xenopus laevis oocytes results in significant increase in TRPV6-mediated calcium uptake. Effect is reversed by addition of cyclosporin A
additional information
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Pin1 overexpression increases the reporter activities in cells transfected with reporters containing the vascular endothelial growth factor VEGF gene promoter or with minimal reporters of activator protein-1 and hypoxia response element. VEGF reporter gene activity is significantly inhibited by either hypoxia-inducible factor-alpha siRNA or AP-1 decoy ODN. Pin1 stimulates VEGF expression by activating HIF-1alpha and AP-1, and is a potential therapeutic target of angiogenesis during cancer development
additional information
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a WW domain mutant of Pin1 can no longer interact with NF-kappaB
additional information
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depletion of Pin1 from HeLa cells causes a cytokinesis defect, overview
additional information
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introduction of point mutations in the prolyl-peptidyl isomerase motif of CyPA. Downregulation of host CyPA by RNA interference, and mutations in viral NS5B, that confers cyclosporine-resistant binding to CyPA, contribute to the cyclosporine resistance of the replicons harboring these mutations
additional information
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overexpression of Pin1 reduces wild-type tau stability but increases P301L mutant tau stability
additional information
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Par14 knockout leads to suppression of cell growth, phenotype, overview
additional information
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repression of Pin1 expression through either homologue Pin1 knockout or small interfering RNA-mediated knockdown compromises its ability to protect Akt from degradation
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mutation of active site residues of Pin1 results in weakened, but not total, abrogation of activity
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enzyme defective mutant lacks 40-70% of secreted p-nitrophenol phosphorylcholine hydrolase activity. C-terminus of Mip is required for activation/secretion of p-nitrophenol phosphorylcholine hydrolase
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mutants lacking PpiB activity exhibit reduced growth at 17°C
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Pin1 knockout mice show reduced neutrophile accumulation in the liver, reduced NF-kappaB activation, and increased nuclear p65 protein expression compared to wild-type mice, phenotypes, overview
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enzyme deletion mutant, enzyme is not required in log phase of growth. Mutation does not affect the binding of strain to macrophages but decreases intracellular survival in macrophages
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enzyme overexpression renders isolated mitochondria far more susceptible to the permeability transition induced by Ca2+ and oxidative stress. Overexpressing cells maintain a lower inner-membrane potential of mitochondria than those of normal cells. Effects are abolished by cyclosporin A. Cyclosporin-D overexpression promotes NO-induced necrosis and inhibits staurosporine-induced apoptosis
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in isoform Pin1-deficient neuronal cell cultures, H2O2 stress-induced phosphoprotein Tau dephosphorylation at Thr231 is significantly lower than in wild-type neurons
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overexpression of wild-type isoform CypB attenuates endoplasmic reticulum stress-induced cell death, whereas overexpression of isomerase activity-defective mutant R62A increases Ca2+ leakage from the endoplasmic reticulum and generation of reactive oxygen species and decreases mitochondrial membrane potential resulting in cell death. siRNA-mediated inhibition of CypB expression renders cells more vulnerable to endoplasmic reticulum stress. CypB interacts with the endoplasmic reticulum stress-related chaperones, Bip and Grp94
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overexpression of mutant FKBP52-FD67DV, but not of wild-type FKBP52, leads to similar midline targeting errors and premature fasciculation
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overexpression of Pin1 reduces wild-type tau stability but increases P301L mutant tau stability
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silencing of Pin1 by siRNA, Pin1 siRNA-transfected neurons show the reduction in perikaryal phosphorylation of NF, siRNA inhibits okadaic acid-induced perikaryal phosphorylation of NF-M/H, immunohistochemic analysis, overview
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disruption of the fkpA gene results in a 47.9fold and 32.1fold decrease in thermotolerance in 5-h and 24-h CS cells, respectively, compared to the parental strain
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enzyme knockout mutant, in mouse pneumonia model no significant difference to wild-type. Deficiency in enzyme does not reduce binding activity of strain to host target proteins but results in enhanced uptake by professional phagocytes
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a mutant lacking the insert-in-flap chaperone domain shoiws 58% of wild-type activity
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a mutant lacking the insert-in-flap chaperone domain shoiws 58% of wild-type activity
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a mutant lacking the insert-in-flap chaperone domain shoiws 58% of wild-type activity
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additional information
enzyme is able to replace the essential homolog Ess1 in Saccharomyces cerevisiae
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enzyme is able to replace the essential homolog Ess1 in Saccharomyces cerevisiae
additional information
overexpression of mutant FKBP52-FD67DV, but not of wild-type FKBP52, leads to similar midline targeting errors and premature fasciculation
