Information on EC 5.2.1.8 - Peptidylprolyl isomerase and Organism(s) Homo sapiens and UniProt Accession P62942

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Homo sapiens
UNIPROT: P62942


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.2.1.8
-
RECOMMENDED NAME
GeneOntology No.
Peptidylprolyl isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
peptidylproline (omega=180) = peptidylproline (omega=0)
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cis-trans-isomerization
-
-
SYSTEMATIC NAME
IUBMB Comments
Peptidylproline cis-trans-isomerase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
95076-93-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform FKBP12
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme belongs to the FK506-binding protein (FKBP) family whose members are peptidyl-prolyl cis-trans isomerases with the enzymatic function attributed to the FKBP domain. Six members of this family localize to the mammalian endoplasmic reticulum. Four of them, FKBP22 (encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65 (FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. All FKBP-EFs contain an endoplasmic reticulum retention signal at the C-terminus
malfunction
physiological function
additional information
-
active site Cys113
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(trans)-Pro190 of protein phosphatase 2A
(cis)-Pro190 of protein phosphatase 2A
show the reaction diagram
-
-
-
-
?
acetyl-Ala-Ala-(cis)-Pro-Ala-Lys-NH2
acetyl-Ala-Ala-(trans)-Pro-Ala-Lys-NH2
show the reaction diagram
-
-
-
?
acetyl-Ala-Ala-Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
acetyl-Ala-Ala-Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
show the reaction diagram
-
-
-
?
Ala-Ala-(cis)-Pro-Ala
Ala-Ala-(trans)-Pro-Ala
show the reaction diagram
-
-
-
?
Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
-
?
Ala-Ser(PO3H2)-(cis)-Pro
Ala-Ser(PO3H2)-(trans)-Pro
show the reaction diagram
-
-
-
?
Ala-Ser(PO3H2)-(cis)-Pro-Arg
Ala-Ser(PO3H2)-(trans)-Pro-Arg
show the reaction diagram
-
-
-
?
amyloidbeta precursor protein
?
show the reaction diagram
-
interaction with Thr688
-
-
?
barstar C40A/C82A/P27A
?
show the reaction diagram
-
the mutant of barstar lacks complications arising from oxidation of Cys in wild-type or isomerization affecting the peptidyl-Pro27 bond. Refolding is comprised by several kinetically detectable folding phases. The slowest phase in refolding, the trans to cis isomerization of the Tyr47-Pro48 peptide bond being in cis conformation in the native state
-
?
cis-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
trans-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
?
D-Glyceraldehyde 3-phosphate
Glycerone phosphate
show the reaction diagram
-
-
-
-
GFPRALPAWARPDYNPPLVE
?
show the reaction diagram
-
a synthetic peptide, named PepD2, corresponding to residues 304-323 of NS5A
-
-
?
hepatitis C virus NS5A protein
?
show the reaction diagram
interleukin-2 tyrosine kinase
?
show the reaction diagram
-
catalytic activity of interleukin-2 tyrosine kinase is inhibited by peptidylprolyl isomerase activity of cyclophilin A. Proline-dependent conformational switch within the interleukin-2 tyrosine kinase SH2 domain regulates substrate recognition and mediates regulatory interactions with the active site of cyclophilin A
-
?
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
show the reaction diagram
Phe-Phe-L-pSer-Pro-Arg-pNA
?
show the reaction diagram
-
-
-
-
?
phosphorylated pro-apoptotic Bcl-2-associated X protein
?
show the reaction diagram
protein tau
?
show the reaction diagram
-
interaction with Thr231 of tau in Alzheimer's disease
-
-
?
RNA polymerase II
?
show the reaction diagram
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
Ser(PO3H2)-(cis)-Pro-Arg
Ser(PO3H2)-(trans)-Pro-Arg
show the reaction diagram
-
-
-
?
Ser(PO3H2)-(cis)-Pro-Arg-NH-4-nitroanilide
Ser(PO3H2)-(trans)-Pro-Arg-NH-4-nitroanilide
show the reaction diagram
-
-
-
?
serine/threonine protein kinase B
?
show the reaction diagram
Suc-Ala-Ala-(trans)-Pro-Lys-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Lys-p-nitroanilide
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-methylcoumarylamide
Suc-Ala-Ala-(cis)-Pro-Phe-methylcoumarylamide
show the reaction diagram
-
-
-
-
?
Suc-Ala-Ala-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Ala-(cis)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
-
?
suc-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
suc-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
-
?
Suc-Ala-Glu-(trans)-Pro-Phe-p-nitroanilide
Suc-Ala-Glu-(cis)-Pro-Phe-p-nitroanilide
show the reaction diagram
-
-
-
-
?
Suc-Ala-Glu-Pro-Phe-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
Suc-Ala-Glu-Pro-Phe-7-amido-4-methylcoumarin
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-(cis)-Pro-Phe-NH-4-nitroanilide
succinyl-Ala-(trans)-Pro-Phe-NH-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe-NH-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-NH-4-nitroanilide
show the reaction diagram
-
-
-
?
succinyl-Ala-Ala-(trans)-Pro-Arg-p-nitroanilide
succinyl-Ala-Ala-(cis)-Pro-Arg-p-nitroanilide
show the reaction diagram
-
-
-
r
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Gly-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Gly-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
-
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
Succinyl-Ala-Val-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Val-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Succinyl-Arg-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Arg-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Succinyl-Leu-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Leu-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Succinyl-Phe-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Phe-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Succinyl-Ser-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ser-Leu-(trans)-Pro-Phe 4-nitroanilide
show the reaction diagram
-
-
-
-
Trp-Phe-Tyr-pSer-Pro-Arg-4-nitroanilide
?
show the reaction diagram
-
-
-
-
?
Trp-Phe-Tyr-Ser(PO3H2)-(cis)-Pro-Arg-4-nitroanilide
Trp-Phe-Tyr-Ser(PO3H2)-(trans)-Pro-Arg-4-nitroanilide
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
amyloidbeta precursor protein
?
show the reaction diagram
-
interaction with Thr688
-
-
?
hepatitis C virus NS5A protein
?
show the reaction diagram
-
nonstructural 5A protein, NS5A, from the JFH1 hepatitis C virus strain. Mutations in this domain are linked to cyclosporin A resistance
-
-
?
interleukin-2 tyrosine kinase
?
show the reaction diagram
-
catalytic activity of interleukin-2 tyrosine kinase is inhibited by peptidylprolyl isomerase activity of cyclophilin A. Proline-dependent conformational switch within the interleukin-2 tyrosine kinase SH2 domain regulates substrate recognition and mediates regulatory interactions with the active site of cyclophilin A
-
?
peptidylproline (omega=180)
peptidylproline (omega=0)
show the reaction diagram
-
-
-
-
?
phosphorylated pro-apoptotic Bcl-2-associated X protein
?
show the reaction diagram
-
Pin1 prevents activation of Bax, prevents Bax cleavage by calpain, and prevents Bax translocation to mitochondria
-
-
?
protein tau
?
show the reaction diagram
-
interaction with Thr231 of tau in Alzheimer's disease
-
-
?
RNA polymerase II
?
show the reaction diagram
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
serine/threonine protein kinase B
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1,2-dimethyl-1H-indol-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate
-
-
(1R)-1,3-diphenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-cyclohexyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-naphthalen-2-yl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-1-[3-(diethenylcarbamoyl)phenyl]-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
inhibition of FKBP12 cis-trans peptidylprolyl isomerase activity, but no activity in splenocyte mitogenesis assay for immunosuppression
(1R)-3-(1,3-benzodioxol-5-yl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-(3,4-dimethoxyphenyl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-cyclohexyl-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1R)-3-cyclohexyl-1-phenylpropyl 1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
(1R)-3-phenyl-1-[3-(phenylcarbonyl)phenyl]propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
inhibition of FKBP12 cis-trans peptidylprolyl isomerase activity, but no activity in splenocyte mitogenesis assay for immunosuppression
(1R,5S)-1-(phenylsulfonyl)bicyclo[3.3.1]nonan-3-one
-
-
(1R,5S)-1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
(1S)-1,3-diphenylpropyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
(1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
(1S)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethylbutanoyl)piperidine-2-carboxylate
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-iodophenyl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-methylphenyl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(3',4,5'-trihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)[2-hydroxy-5-(trifluoromethyl)phenyl]methanone
-
-
(2,5-dimethyl-1-benzofuran-3-yl)[4-hydroxy-4'-(trifluoromethoxy)-1,1'-biphenyl-3-yl]methanone
-
-
(2-butyl-1-benzothiophen-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
-
(24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21)-tetrone
-
-
(3S,26aR)-19,19-dimethyl-3-(2-phenylethyl)-12,13,14,15,18,19,24,25,26,26a-decahydro-3H,10H-4,8-(metheno)pyrido[2,1-c][1,9,17,4]trioxazacyclotricosine-1,16,20,21(11H,23H)-tetrone
-
-
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanone
-
-
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanone
-
-
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
-
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanethione
-
-
(5'-fluoro-2',4-dimethoxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
-
(5-bromo-2-hydroxyphenyl)(2,5-dimethyl-1-benzofuran-3-yl)methanone
-
-
(E)-2-(2-hydroxy-2-isobutylethy 1idene)-1-meth ylcyclopentane-(L)-tyrosylcarboxamide
-
-
1-(1H-imidazol-2-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(2-phenylethyl)-4-pyridin-3-ylbutyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
1-(3-hydroxyphenoxy)bicyclo[3.3.1]nonan-3-one
-
-
1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(pyridin-3-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
1-benzyl-2-pyridin-3-ylethyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
1-benzyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
1-phenyl-3-pyridin-3-ylpropyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
-
15,15-dimethyltetradecahydropyrido[2,1-c][1,9,4]dioxazacyclononadecine-1,12,16,17(3H,19H)-tetrone
-
-
2-(4-((2R)-2-[(1R,3R,5R)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl)-2,6-dioxopiperidin-1-yl)acetamide
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
2-oxo-2-[(1R,10S)-5-phenoxy-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-1-(3,4,5-trimethoxyphenyl)ethanone
-
2-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-2-oxo-1-(3,4,5-trimethoxyphenyl)ethanone
-
3,5-dichloro-N-(3-[(2-naphthylacetyl)amino]phenyl)benzamide
-
-
3,5-dichloro-N-[3-([[(2,4-dibromophenyl)amino]carbonyl]amino)phenyl]benzamide
-
-
3,5-dichloro-N-[3-([[(3,5-dichlorophenyl)amino]carbonyl]amino)phenyl]benzamide
-
-
3,5-dichloro-N-[3-[(3,3-diphenylpropanoyl)amino]phenyl]benzamide
-
-
3,5-dichloro-N-[3-[([[4-(trifluoromethyl)phenyl]amino]carbonyl)amino]phenyl]benzamide
-
-
3-(3,4,5-trimethoxyphenyl)propyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
3-(3,4,5-trimethoxyphenyl)propyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
3-phenyl-1-(2-pyridin-3-ylethyl)propyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
3-phenylpropyl 1-(2-hydroxy-3,3-dimethylpentanoyl)piperidine-2-carboxylate
-
-
4-phenyl-1-(2-pyridin-3-ylethyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(4-ethyl butanoate)
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(ethyl ethanoate)
-
competitive inhibition. Evaluation of cytotoxicity against cell lines L-929 fibroblasts and K-562 leukemic cells. Compound is able to significantly speed nerve regeneration in a rat sciatic nerve neurotomy model
5-hydroxy-1,4-naphthoquinone
-
i.e. juglone, 0.0057 mM, complete inactivation within 150 min, irreversible inhibition of the parvulin family of peptidyl-prolyl cis/trans isomerases, specific inhibition allows selective inactivation of these enzymes in presence of other peptidylprolyl isomerases, the inactivated parvulin contains two juglone molecules that are covalently bound to the side chains of Cys41 and Cys69, partial unfolding of the active site of the parvulins is thought to be the cause of the deterioration of peptidylprolyl isomerase activity
5-methoxy-1',3'dihydro-3H-spiro[1-benzofuran-2,2'-indene]-3-one
-
-
5-methoxy-2',3'-dihydro-3H-spiro[1-benzofuran-2,1'-indene]-3-one
-
-
5-methoxy-3H-spiro[1-benzofuran-2,1'-cyclopent[3]en]-3-one
-
-
Ac-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.127 mM
Ac-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-Yaa-Zaa-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(2-thienyl)Ala-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-cyclohexylAla-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
Ac-Phe-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
-
acetyl-Ala-Ala-D-Ser(PO3H2)-Pro-Leu-NH-4-nitroanilide
-
IC50: 0.001 mM
acetyl-Ala-Ala-D-Ser-Pro-Leu-NH-4-nitroanilide
-
IC50: 0.085 mM
acetyl-Ala-Pro-Phe-4-(trimethylammonium)anilide
-
IC50: 7 mM
acetyl-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.77 mM
Ala-Pro
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1R)-1-methoxy-3-methylbut-2-en-1-yl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxy-3-methylbutyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxyethyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
cyclic CRYPEVEIC
-
the cyclic peptide is specific for the active site of the PPIase domain
cyclo(Arg-Arg-Arg-D-pThr-Pip-Nal-Arg-Arg-Gln)
-
-
cyclo(Arg-Arg-Arg-D-Thr-Pip-Nal-Arg-Arg-Gln)
-
-
cyclo(D-Ala-Gln-Glu-Mpa-Mal-Ile-Gln)
-
-
cyclo(D-Ala-Gly-D-pThr-Pip-Nal-Orn-Gln)
-
-
cyclo(D-Ala-Ile-D-pSer-Pro-Nal-Orn-Gln)
-
-
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)
-
-
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)-Lys-SH
-
-
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
-
-
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-Gln)
-
-
cycloheximide
-
-
cyclosporin A
D-Ser(PO3H2)-Pro
-
1 mM, 20% inhibition
diethyl 2,2'-(1,3,6,8-tetraoxo-1,3,6,8-tetrahydrobenzo[lmn][3,8]phenanthroline-2,7-diyl)diacetate
-
-
diethyl 2,2'-(1,3,8,10-tetraoxo-1,3,8,10-tetrahydroisoquinolino[4',5',6':6,5,10]anthra[2,1,9-def]isoquinoline-2,9-diyl)diacetate
-
-
dipentamethylene thiuram monosulfide
-
-
ethyl (2S)-1-(4,4-dimethyl-2-oxohexanoyl)piperidine-2-carboxylate
-
-
ethyl (2S)-1-[(2-methoxycyclohexyl)(oxo)acetyl]piperidine-2-carboxylate
-
-
ethyl (2S)-1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
ethyl 1-(4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-(4-methyl-2-oxopentanethioyl)piperidine-2-carboxylate
-
-
ethyl 1-(4-methyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-(5-ethoxy-4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
ethyl 1-[(1-methoxycyclohexyl)(oxo)acetyl]pyrrolidine-2-carboxylate
-
-
ethyl 1-[(3-methoxytetrahydro-2H-pyran-2-yl)(oxo)acetyl]piperidine-2-carboxylate
-
-
FK506
-
-
juglone
linear CRYPEVEIC
-
-
methyl N-([(1R,2E)-2-[(2S)-2-hydroxy-4-methylpentylidene]-1-methylcyclopentyl]carbonyl)-L-tyrosinate
-
-
N,N''-(4,6-dibromo-1,3-phenylene)bis[3-(4-iodophenyl)urea]
-
-
N,N'-1,3-phenylenebis(3,5-dichlorobenzamide)
-
-
Phe-Ser(PO3H2)-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
-
IC50: 0.004 mM
Phe-Ser-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
-
IC50: 0.097 mM
QAEGPK
peptide corresponding to peptide QAEGP487KR at the N-terminus of the enzyme's isomerase domain. Peptide binds to the active site, but the enzyme does not catalyze its isomerization
Ser(PO3H2)-Pro
-
; IC50: 2.0 mM
Ser-Pro
-
-
Ser-PSI[CS-N]-Pro
-
-
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.138 mM
Suc-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
-
transition-state analogue of peptidylprolyl isomerase activity of cyclophilin Cyp-18, Kd value 0.02 mM. Selectively inhibits Cyp-18, but not enzyme isoform FKBP12
succinyl-Ala-Ala-Pro-NH2
-
IC50: 14 mM
succinyl-Ala-Ala-Pro-Phe-4-carboxymethylanilide
-
IC50: 4.4 mM
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.54 mM
succinyl-Ala-Pro-Phe-4-aminoanilide
-
IC50: 5.8 mM
succinyl-Ala-Pro-Phe-4-carboxmethylanilide
-
IC50: 0.7 mM
succinyl-Ala-Pro-Phe-4-nitroanilide
-
IC50: 0.17 mM
succinyl-Pro-Phe-4-nitroanilide
-
IC50: 1.09 mM
[(1S,2R,3S,6R,7aR)-2-(benzylcarbamoyl)-6-methoxy-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
[(1S,2R,3S,6S,7aR)-2-(benzylcarbamoyl)-6-fluoro-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-(pentafluorophenyl)hexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-phenylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
[(1S,2R,3S,7aR)-2-[(1,3-benzodioxol-5-ylmethyl)carbamoyl]-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
[3-[(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)carbonyl]-2-methyl-1-benzofuran-5-yl]acetonitrile
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
stimulation
additional information
-
GM-CSF-induced activation of Erk1/2, which phosphorylated Thr167 of the pro-apoptotic Bcl-2-associated X protein, Bax, facilitates de novo interaction of Bax with the prolyl isomerase Pin1
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
Ala-Gly-PSI[CS-N]-Pro-Phe 4-nitroanilide
-
-
0.17 - 0.7
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
1.247
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
0.585
succinyl-Ala-Lys-Pro-Phe 4-nitroanilide
-
-
additional information
additional information
-
kinetic analysis of Pin1, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.7 - 140
N-succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide
1480 - 14600
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00222
(1,2-dimethyl-1H-indol-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
pH and temperature not specified in the publication
0.00001
(1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate
-
-
0.01
(1R)-1,3-diphenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.007
(1R)-1-cyclohexyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.004 - 0.01
(1R)-1-naphthalen-2-yl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.009
(1R)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.000005
(1R)-1-[3-(diethenylcarbamoyl)phenyl]-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.009
(1R)-3-(1,3-benzodioxol-5-yl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.002 - 0.006
(1R)-3-(3,4-dimethoxyphenyl)-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.01
(1R)-3-cyclohexyl-1-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.02
(1R)-3-cyclohexyl-1-phenylpropyl 1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
0.000005
(1R)-3-phenyl-1-[3-(phenylcarbonyl)phenyl]propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.00016
(1S)-1,3-diphenylpropyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
0.000007
(1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.0002
(1S)-1-phenyl-3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethylbutanoyl)piperidine-2-carboxylate
-
-
0.001
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-iodophenyl)methanone
-
pH and temperature not specified in the publication
0.0074
(2,5-dimethyl-1-benzofuran-3-yl)(2-hydroxy-5-methylphenyl)methanone
-
pH and temperature not specified in the publication
0.0041
(2,5-dimethyl-1-benzofuran-3-yl)[2-hydroxy-5-(trifluoromethyl)phenyl]methanone
-
pH and temperature not specified in the publication
0.0072
(2,5-dimethyl-1-benzofuran-3-yl)[4-hydroxy-4'-(trifluoromethoxy)-1,1'-biphenyl-3-yl]methanone
-
pH and temperature not specified in the publication
0.00366
(2-butyl-1-benzothiophen-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
-
pH and temperature not specified in the publication
0.0001
(24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21)-tetrone
-
-
0.000001
(3S,26aR)-19,19-dimethyl-3-(2-phenylethyl)-12,13,14,15,18,19,24,25,26,26a-decahydro-3H,10H-4,8-(metheno)pyrido[2,1-c][1,9,17,4]trioxazacyclotricosine-1,16,20,21(11H,23H)-tetrone
-
-
0.0021
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanone
-
pH and temperature not specified in the publication
0.0037
(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanone
-
pH and temperature not specified in the publication
0.0018
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0006
(5'-fluoro-2',4-dihydroxybiphenyl-3-yl)(2-methyl-1-benzothiophen-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0029
(5'-fluoro-2',4-dimethoxybiphenyl-3-yl)(2-methyl-1-benzofuran-3-yl)methanethione
-
pH and temperature not specified in the publication
0.0026
(5-bromo-2-hydroxyphenyl)(2,5-dimethyl-1-benzofuran-3-yl)methanone
-
pH and temperature not specified in the publication
0.0086
(E)-2-(2-hydroxy-2-isobutylethy 1idene)-1-meth ylcyclopentane-(L)-tyrosylcarboxamide
-
0C, pH 8.0
0.00005
1-(2-phenylethyl)-4-pyridin-3-ylbutyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.0167
1-(3-hydroxyphenoxy)bicyclo[3.3.1]nonan-3-one
-
-
0.0092
1-(phenylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.0079
1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
-
-
0.000084
1-benzyl-2-pyridin-3-ylethyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
0.055
1-benzyl-3-phenylpropyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.000059
1-phenyl-3-pyridin-3-ylpropyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.0083
1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
pH 8.0
0.03
15,15-dimethyltetradecahydropyrido[2,1-c][1,9,4]dioxazacyclononadecine-1,12,16,17(3H,19H)-tetrone
-
-
0.0012
2-oxo-2-[(1R,10S)-5-phenoxy-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-1-(3,4,5-trimethoxyphenyl)ethanone
pH 8.0
0.0081
2-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-2-oxo-1-(3,4,5-trimethoxyphenyl)ethanone
pH 8.0
0.000012
3-(3,4,5-trimethoxyphenyl)propyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.012
3-(3,4,5-trimethoxyphenyl)propyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.00023
3-(3,4,5-trimethoxyphenyl)propyl 1-(benzylsulfonyl)piperidine-2-carboxylate
-
-
0.00006
3-phenyl-1-(2-pyridin-3-ylethyl)propyl 1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]-D-prolinate
-
-
0.0023
3-phenylpropyl 1-(2-hydroxy-3,3-dimethylpentanoyl)piperidine-2-carboxylate
-
-
0.00009
4-phenyl-1-(2-pyridin-3-ylethyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.000019
4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate
-
-
0.258
Ac-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
0.0012
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
0.183
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
0.0048
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
0.0183
Ac-Phe-D-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
0.547
Ac-Phe-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
-
pH 7.8, 10C
19
Ala-Pro
-
-
0.000068
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1R)-1-methoxy-3-methylbut-2-en-1-yl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.0000028
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxy-3-methylbutyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.000081
benzyl (2S)-1-[[(1S,2R,5R)-1-hydroxy-5-[(1S)-1-methoxyethyl]-2-methylcyclohexyl](oxo)acetyl]piperidine-2-carboxylate
-
-
0.0002 - 0.00052
cyclic CRYPEVEIC
0.0034
cycloheximide
-
-
0.00066
ethyl (2S)-1-(4,4-dimethyl-2-oxohexanoyl)piperidine-2-carboxylate
-
-
0.001
ethyl (2S)-1-[(2-methoxycyclohexyl)(oxo)acetyl]piperidine-2-carboxylate
-
-
0.002
ethyl (2S)-1-[cyclohexyl(oxo)acetyl]piperidine-2-carboxylate
-
-
0.002
ethyl 1-(4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.0043
ethyl 1-(4-methyl-2-oxopentanethioyl)piperidine-2-carboxylate
-
-
0.002
ethyl 1-(4-methyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.001
ethyl 1-(5-ethoxy-4,4-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
-
-
0.008
ethyl 1-[(1-methoxycyclohexyl)(oxo)acetyl]pyrrolidine-2-carboxylate
-
-
0.004
ethyl 1-[(3-methoxytetrahydro-2H-pyran-2-yl)(oxo)acetyl]piperidine-2-carboxylate
-
-
0.044
linear CRYPEVEIC
-
using succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide as substrate, in 50 mM HEPES, 0.1 M NaCl, 5 mM NaN3, pH 7.4, at 22C
1
Ser(PO3H2)-Pro
-
-
27
Ser-Pro
-
-
0.009
[(1S,2R,3S,6R,7aR)-2-(benzylcarbamoyl)-6-methoxy-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
0.026
[(1S,2R,3S,6S,7aR)-2-(benzylcarbamoyl)-6-fluoro-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
0.016
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-(pentafluorophenyl)hexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
0.015
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
0.044
[(1S,2R,3S,7aR)-2-(benzylcarbamoyl)-3-phenylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
0.032
[(1S,2R,3S,7aR)-2-[(1,3-benzodioxol-5-ylmethyl)carbamoyl]-3-naphthalen-2-ylhexahydro-1H-pyrrolizin-1-yl]methyl dihydrogen phosphate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0485
(1R,5S)-1-(phenylsulfonyl)bicyclo[3.3.1]nonan-3-one
Homo sapiens
-
-
0.0092
(1R,5S)-1-(phenylthio)bicyclo[3.3.1]nonan-3-one
Homo sapiens
-
-
0.01
(2,5-dimethyl-1-benzofuran-3-yl)(3',4,5'-trihydroxy-1,1'-biphenyl-3-yl)methanone
Homo sapiens
-
above, pH and temperature not specified in the publication
0.00167
(2,5-dimethyl-1-benzofuran-3-yl)(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)methanone
Homo sapiens
-
pH and temperature not specified in the publication
0.0275
1-(1H-imidazol-2-ylthio)bicyclo[3.3.1]nonan-3-one
Homo sapiens
-
-
0.0079
1-(pyridin-3-ylthio)bicyclo[3.3.1]nonan-3-one
Homo sapiens
-
-
0.0216
2-(4-((2R)-2-[(1R,3R,5R)-3,5-dimethyl-2-oxocyclohexyl]-2-hydroxyethyl)-2,6-dioxopiperidin-1-yl)acetamide
Homo sapiens
-
-
0.00088
3,5-dichloro-N-(3-[(2-naphthylacetyl)amino]phenyl)benzamide
Homo sapiens
-
-
0.00062
3,5-dichloro-N-[3-([[(2,4-dibromophenyl)amino]carbonyl]amino)phenyl]benzamide
Homo sapiens
-
-
0.00069
3,5-dichloro-N-[3-([[(3,5-dichlorophenyl)amino]carbonyl]amino)phenyl]benzamide
Homo sapiens
-
-
0.00087
3,5-dichloro-N-[3-[(3,3-diphenylpropanoyl)amino]phenyl]benzamide
Homo sapiens
-
-
0.0009 - 4
3,5-dichloro-N-[3-[([[4-(trifluoromethyl)phenyl]amino]carbonyl)amino]phenyl]benzamide
Homo sapiens
-
-
0.0036
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione
Homo sapiens
-
-
0.0223
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(4-ethyl butanoate)
Homo sapiens
-
-
0.0044
4-[2-(3,5-dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]-2,6-piperidinedione-1-(ethyl ethanoate)
Homo sapiens
-
-
0.1
5-methoxy-1',3'dihydro-3H-spiro[1-benzofuran-2,2'-indene]-3-one
Homo sapiens
-
-
0.077
5-methoxy-2',3'-dihydro-3H-spiro[1-benzofuran-2,1'-indene]-3-one
Homo sapiens
-
-
0.065
5-methoxy-3H-spiro[1-benzofuran-2,1'-cyclopent[3]en]-3-one
Homo sapiens
-
-
0.215
Ac-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
Homo sapiens
-
10C
1
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
Homo sapiens
-
pH 7.8, 10C
8
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-(t-butyl)Phe-Thr(PO3H2)-Yaa-Zaa-Gln-NH2
Homo sapiens
-
pH 7.8, 10C
15
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(2-thienyl)Ala-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
Homo sapiens
-
pH 7.8, 10C
15
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-(3-benzothienyl)Ala-Thr(PO3H2)-piperidine-2-carboxylic acid-beta-(2-naphthyl)Ala-Gln-NH2
Homo sapiens
-
pH 7.8, 10C
7
Ac-Lys(Nepsilon-biotinoyl)-Ala-Ala-beta-cyclohexylAla-Thr(PO3H2)-(methyl)Ala-beta-(2-naphthyl)Ala-Gln-NH2
Homo sapiens
-
pH 7.8, 10C
0.001
acetyl-Ala-Ala-D-Ser(PO3H2)-Pro-Leu-NH-4-nitroanilide
Homo sapiens
-
IC50: 0.001 mM
0.085
acetyl-Ala-Ala-D-Ser-Pro-Leu-NH-4-nitroanilide
Homo sapiens
-
IC50: 0.085 mM
7
acetyl-Ala-Pro-Phe-4-(trimethylammonium)anilide
Homo sapiens
-
IC50: 7 mM
0.77
acetyl-Ala-Pro-Phe-4-nitroanilide
Homo sapiens
-
IC50: 0.77 mM
30
Ala-Pro
Homo sapiens
-
IC50: 30 mM
0.0011
cyclo(Arg-Arg-Arg-D-pThr-Pip-Nal-Arg-Arg-Gln)
Homo sapiens
-
-
0.3
cyclo(Arg-Arg-Arg-D-Thr-Pip-Nal-Arg-Arg-Gln)
Homo sapiens
-
above
0.063
cyclo(D-Ala-Gln-Glu-Mpa-Mal-Ile-Gln)
Homo sapiens
-
-
0.000043
cyclo(D-Ala-Gly-D-pThr-Pip-Nal-Orn-Gln)
Homo sapiens
-
-
0.0011
cyclo(D-Ala-Ile-D-pSer-Pro-Nal-Orn-Gln)
Homo sapiens
-
-
0.00031
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)
Homo sapiens
-
-
0.000032
cyclo(D-Ala-Sar-D-pThr-Pip-Nal-Tyr-Gln)-Lys-SH
Homo sapiens
-
-
0.0025
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
Homo sapiens
-
-
0.00022
cyclo(D-Arg-D-Arg-D-pThr-Pip-Nal-Arg-Gln)
Homo sapiens
-
-
0.3
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-D-Arg-D-Arg-D-Arg-Gln)
Homo sapiens
-
above
0.3
cyclo(D-Arg-D-Arg-D-Thr-Pip-Nal-Arg-Gln)
Homo sapiens
-
above
0.00000265
cyclosporin A
Homo sapiens
-
-
0.0086
methyl N-([(1R,2E)-2-[(2S)-2-hydroxy-4-methylpentylidene]-1-methylcyclopentyl]carbonyl)-L-tyrosinate
Homo sapiens
-
-
0.00059
N,N''-(4,6-dibromo-1,3-phenylene)bis[3-(4-iodophenyl)urea]
Homo sapiens
-
-
0.00093
N,N'-1,3-phenylenebis(3,5-dichlorobenzamide)
Homo sapiens
-
-
0.004
Phe-Ser(PO3H2)-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
Homo sapiens
-
IC50: 0.004 mM
0.097
Phe-Ser-PSI[CS-N]-Pro-Phe-NH-4-nitroanilide
Homo sapiens
-
IC50: 0.097 mM
2
Ser(PO3H2)-Pro
Homo sapiens
-
IC50: 2.0 mM
0.54
Suc-Ala-Ala-Pro-Phe-4-nitroanilide
Homo sapiens
-
10C
0.015
Suc-Ala-GlyPSI(PO2Et-N)Pro-Phe-4-nitroanilide
Homo sapiens
-
10C
14
succinyl-Ala-Ala-Pro-NH2
Homo sapiens
-
IC50: 14 mM
4.4
succinyl-Ala-Ala-Pro-Phe-4-carboxymethylanilide
Homo sapiens
-
IC50: 4.4 mM
0.54
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
Homo sapiens
-
IC50: 0.54 mM
5.8
succinyl-Ala-Pro-Phe-4-aminoanilide
Homo sapiens
-
IC50: 5.8 mM
0.7
succinyl-Ala-Pro-Phe-4-carboxmethylanilide
Homo sapiens
-
IC50: 0.7 mM
0.17
succinyl-Ala-Pro-Phe-4-nitroanilide
Homo sapiens
-
IC50: 0.17 mM
1.09
succinyl-Pro-Phe-4-nitroanilide
Homo sapiens
-
IC50: 1.09 mM
0.0045
[3-[(5'-fluoro-2',4-dihydroxy-1,1'-biphenyl-3-yl)carbonyl]-2-methyl-1-benzofuran-5-yl]acetonitrile
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
primary cortical culture
Manually annotated by BRENDA team
-
primary
Manually annotated by BRENDA team
-
foetal brain
Manually annotated by BRENDA team
-
a Hodkin's lymphoma cell line
Manually annotated by BRENDA team
-
enzyme isoform Pin1 is necessary for activation-dependent mRNA stabilization, accumulation, and protein secretion of cytokine GM-CSF. Pin1 mediates the association of the AU-rich element-binding protein, AUF1, with GM-CSF mRNA
Manually annotated by BRENDA team
-
co-localization of cyclophilin B and channel protein TRPV6 in the syncytiotropoblast layer, with small amounts of both in microvilli apical membrane
Manually annotated by BRENDA team
-
neuroblastoma cell, overexpression of isoform Pin1 decreases levels of the inhibitor of apoptosis protein, Survivin. Pin1 and Survivin partially co-localize in interphase and mitotic cells and form a complex. Pin1 silencing leads to an increase in Survivin levels
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
and/or organelles, isoforms CyP2 and CyP3
Manually annotated by BRENDA team
-
cyclophilin H is a component of the human U4/U5 small nuclear ribonucleoprotein particle, interacting with homologous sequences in the proteins U4/U6-60K and hPr18 during Pre-mRNA splicing
-
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
x * 14000, about, SDS-PAGE
17000
-
x * 17000, SDS-PAGE
17737
-
x * 17737, calculation from amino acid sequence
18000
-
x * 18000, about
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
phosphorylated at Ser19 in vivo and in vitro. In human HeLa cells the protein is most likely modified by casein kinase 2
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.65 A resolution. The N-terminus of one isomerase domain is bound in the active site of a neighbouring isomerase molecule in a manner analogous to the substrate. This sequence binds to the active site of the enzyme, but cannot be turned over
2.0 A resolution, space group P3121; recombinant enzyme
crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide, hanging drop vapour diffusion method
-
crystal structure of cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
-
crystal structure of cyclophilin A complexed with a binding site peptide from HIV-1 capsid protein
-
crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]4,4-dimethylthreonine cyclosporin A
-
crystallization of cyclophilin-tetrapeptide and cyclophilin-cyclosporin complexes
-
hanging drop vapor diffusion method, using 25% (w/v) PEG MME 550, 0.1 M zinc acetate, 0.1 M MES at pH 6.5
in complex with inhibitor 1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
in complex with inhibitor 4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate. Fluorine atoms of inhibitor participate in discrete interactions with the Phe36 phenyl ring and the Tyr26 hydroxyl group of enzyme, with the latter resembling a moderate-to-weak hydrogen bond
-
in complex with inhibitors (1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate, (1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate, (24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21H)-tetrone
-
mutant K125A/E126A is crystallized by the hanging drop vapor diffusion method, using 2 M NH4SO4, 0.2 M NaCl, 0.1 M HEPES, pH 7.5
mutant P9Q/R13F/K17V/R18F in complex with 1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
-
purified recombinant detagged wild-type and selenomethionine-labeled FKBP22, hanging drop vapor diffusion method, mixing of 0.002 ml of 3 mg/ml protein in 1 mM Tris/HCl, pH 7.2, and 0.05 mM CaCl2, with 0.001 ml of reservoir solution containing 0.1 M MES, 25% 1,2-propanediol, and 11-12% PEG 20000, pH 7.0-7.2, 1-2 weeks, X-ray diffraction structure determination and analysis at 1.9 A and 2.46 A resolution, respectively
recombinant enzyme expressed in Escherichia coli
-
recombinant protein, overall structure and analysis of cyclosporin A binding site
-
sitting drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M NaI
sitting drop vapor diffusion method, using 34% (w/v) PEG 8K, 0.2 M NH4SO4, and 0.1 M bis-Tris, pH 6.0
solution structure of protein determined by NMR spectroscopy
structure of human cyclophilin and its binding site for cyclophilin A determined by X-ray crystallography and NMR spectroscopy
-
X-ray structure of a decameric cyclophilin-cyclosporin crystal complex
-
X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 isoforms: CyP1, CyP2, CyP3
-
glutathione-Sepharose 4B column chromatography
-
glutathione-Sepharose column chromatography and S-Sepharose column chromatography
-
Ni-NTA resin column chromatography and Superdex 200 gel filtration
recombinant enzyme and mutant P16S
-
recombinant GST-tagged enzyme from Escherichia coli
-
recombinant His6-tagged wild-type and selenomethionine-labeled FKBP22 from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography, tag cleavage by enterokinase, anion exchanchromatography, and dialysis
recombinant MBP-Pin1 fusion protein from Escherichia coli strain BL21(DE3) by amylose affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 isoforms expressed in Escherichia coli
-
co-expression with TRPV6 channel protein in Xenopus laevis oocytes
-
expressed in COS-1 cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21 Gold DE3 cells
expressed in Escherichia coli JM105 cells
-
expression in 293-T cells
-
expression in Escherichia coli
expression in T47D cell, MCF-7 cell, MDA-231 cell
-
expression of GST-tagged Pin1
-
expression of MBP-Pin1 fusion protein in Escherichia coli strain BL21(DE3)
-
gene FKBP14, expression of His6-tagged wild-type and selenomethionine-labeled FKBP22 in Escherichia coli strains BL21(DE3) and B834(DE3), respectively
neutral isoelectric form
-
Par14, sequence comparisons, expression of GST-tagged enzyme in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes
-
wild-type and mutant enzymes W121A, H54Q, R55A, F60A, Q111A, F133A, and H126Q, expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Pin1 expression is enhanced in transformed T-cell lines C8166-45, MT4, and JPX9 expressing oncoprotein Tax from human T-cell leukemia virus type 1
-
Pin1 expression is increased by NS5B protein
-
the enzyme is upregulated in cancer cells
-
the overexpression of Pin1 in Hep-G2 cells markedly enhances insulin-induced IRS-1 phosphorylation and its downstream events: phosphatidylinositol 3-kinase binding with IRS-1andAkt phosphorylation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A16S
-
site-directed mutagenesis, dominant-negative Pin1 point mutation
C113D
-
mutation does not compromise isoform Pin1 function in vivo nor does it abolish catalytic activity. C113 may not be the catalytic nucleophile
C115A
-
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
-
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
-
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
-
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
-
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
-
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
-
dramatic reduction of peptidylprolyl isomerase activity and 400fold reduction of protein phosphatase 2A activation
F133A
-
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
-
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
-
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
-
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
H157A
-
mutant supports viability in yeast complementation assay
H157F
-
mutant supports viability in yeast complementation assay
H157L
-
mutant supports viability in yeast complementation assay
H157N
-
mutant supports viability in yeast complementation assay
H157S
-
mutant supports viability in yeast complementation assay
H47Q
-
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
H59A
-
mutant supports viability in yeast complementation assay
H59F
-
mutant supports viability in yeast complementation assay but displays significantly reduced growth in yeast compared to wild-type Pin1
H59L
-
mutant is not viable
H59L/H157A
-
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
-
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
-
mutant supports viability in yeast complementation assay, mutation H157L rescues mutant H59L
H59L/H157S
-
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
H59N
-
mutant supports viability in yeast complementation assay
H59S
-
mutant supports viability in yeast complementation assay
P16S
-
10fold decrease in ratio kcat/Km at 10C. Mutant is extremely sensitive to guanidinium-HCl and shows increased susceptibility to urea. Folding time of the mutant is extended
P9Q/R13F/K17V/R18F
-
mutant designed for crytallizability, crystal structure in complex with 1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
Q111A
-
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
-
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
R68/69A
-
catalytically inactive
R68A/R69A
-
decrease in both kcat and Km value
S16A/Y23A
-
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
-
mutation in WW domain. Mutation diminishes binding to brain-specifc protein BNIP-H
S19A
-
mutation abolishes phosphorylation and alters the subcellular localization from predominantly nuclear to significantly cytoplasmic
S19E
-
mutant enzyme is localized around the nuclear envelope, but does not penetrate into the nucleoplasm, in vitro DNA-binding affinity is strongly reduced
V55R
-
site-directed mutagenesis, the mutation increases the PPIase activity by a factor of 11
W121A
-
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/K63A
-
catalytically inactive
Y82K
-
site-directed mutagenesis, the mutation decreases the PPIase activity by a factor of 7
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
high-throughput screening method for isoform FKBP12 binding based on the decrease of a fluorescence signal generated by a small molecule fluorescent FKBP12 ligand bound to the protein and measured in the presence of inhibitor
medicine
pharmacology