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Information on EC 5.2.1.8 - peptidylprolyl isomerase and Organism(s) Schistosoma mansoni and UniProt Accession Q26548

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EC Tree
IUBMB Comments
The first type of this enzyme found 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.
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This record set is specific for:
Schistosoma mansoni
UNIPROT: Q26548
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Word Map
The taxonomic range for the selected organisms is: Schistosoma mansoni
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyclophilin, cyclophilin a, fkbp12, ppiase, fkbp51, trigger factor, fkbp52, fk506-binding protein, peptidyl-prolyl isomerase, cyclophilin b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12 kDa FKBP
-
-
-
-
12.6 kDa FKBP
-
-
-
-
13 kDa FKBP
-
-
-
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15 kDa FKBP
-
-
-
-
19 kDa FK506-binding protein
-
-
-
-
22 kDa FK506-binding protein
-
-
-
-
25 kDa FKBP
-
-
-
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27 kDa membrane protein
-
-
-
-
36 kDa FK506 binding protein
-
-
-
-
40 kDa thylakoid lumen PPIase
-
-
-
-
40 kDa thylakoid lumen rotamase
-
-
-
-
51 kDa FK506-binding protein
-
-
-
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52 kDa FK506 binding protein
-
-
-
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54 kDa progesterone receptor-associated immunophilin
-
-
-
-
65 kDa FK506-binding protein
-
-
-
-
CGI-124
-
-
-
-
Chl-Mip
-
-
-
-
CPH
-
-
-
-
Cyclophilin
-
-
-
-
Cyclophilin 18
-
-
-
-
Cyclophilin 33
-
-
-
-
Cyclophilin A
-
-
-
-
Cyclophilin B
-
-
-
-
Cyclophilin C
-
-
-
-
Cyclophilin cyp2
-
-
-
-
Cyclophilin homolog
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-
-
-
Cyclophilin ScCypA
-
-
-
-
Cyclophilin ScCypB
-
-
-
-
Cyclophilin-10
-
-
-
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Cyclophilin-11
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-
-
-
Cyclophilin-40
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-
-
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Cyclophilin-60
-
-
-
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Cyclophilin-like protein Cyp-60
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-
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Cyclophilin-related protein
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-
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Cyclosporin A-binding protein
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-
-
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CYP-40
-
-
-
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CYP-S1
-
-
-
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Cyp3 PPIase
-
-
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CyPA
-
-
-
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CyPB
-
-
-
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Estrogen receptor binding cyclophilin
-
-
-
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FF1 antigen
-
-
-
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FKBP
-
-
-
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FKBP-12
-
-
-
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FKBP-12.6
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-
-
-
FKBP-13
-
-
-
-
FKBP-15
-
-
-
-
FKBP-19
-
-
-
-
FKBP-21
-
-
-
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FKBP-22
-
-
-
-
FKBP-23
-
-
-
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FKBP-25
-
-
-
-
FKBP-36
-
-
-
-
FKBP-51
-
-
-
-
FKBP-70
-
-
-
-
FKBP22
-
-
-
-
FKBP52 protein
-
-
-
-
FKBP54
-
-
-
-
FKBP59
-
-
-
-
FKBP65
-
-
-
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FKBP65RS
-
-
-
-
HBI
-
-
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Histidine rich protein
-
-
-
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hPar14
-
-
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HSP binding immunophilin
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-
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HSP90-binding immunophilin
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-
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Immunophilin FKBP12
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-
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Immunophilin FKBP12.6
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-
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Immunophilin FKBP36
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-
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Immunophilin FKBP65
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-
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Isomerase, peptidylprolyl cis-trans
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-
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Macrolide binding protein
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-
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Macrophage infectivity potentiator
-
-
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MtFK
-
-
-
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Nucleolar proline isomerase
-
-
-
-
p17.7
-
-
-
-
P31
-
-
-
-
P54
-
-
-
-
p59 protein
-
-
-
-
Par14
-
-
-
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Parvulin
-
-
-
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Parvulin 14
-
-
-
-
Peptide bond isomerase
-
-
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Peptidyl-prolyl cis-trans isomerase
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-
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Peptidyl-prolyl cis-trans isomerase plp
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-
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Peptidyl-prolyl cis-trans isomerase surA
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Peptidyl-prolyl cis/trans isomerase EPVH
-
-
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Peptidylprolyl cis-trans isomerase
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PfCyP
-
-
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Planta-induced rust protein 28
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-
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PPIase
-
-
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PPIase Pin1
-
-
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PPIase Pin4
-
-
-
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Proline rotamase
-
-
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Proteins, cyclophilins
-
-
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Proteins, specific or class, cyclophilins
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-
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Rapamycin-binding protein
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-
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Rapamycin-selective 25 kDa immunophilin
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-
-
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Rotamase
-
-
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Rotamase Pin1
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-
-
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Rotamase Pin4
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-
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Rotamase plp
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-
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S-cyclophilin
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-
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S1205-06
-
-
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SCYLP
-
-
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SmCYP A
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-
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SmCYP B
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-
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Smp17.7
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-
-
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SP18
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-
-
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WHP
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-
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-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000014
cyclosporin A
Schistosoma mansoni
10°C, pH 7.9
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cyclophilin A
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPIE_SCHMA
273
0
30905
Swiss-Prot
other Location (Reliability: 2)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in reduced and oxidized state at 1.5 and 1.8 A resolution. Oxidized enzyme contains a disulfide bridge between C-terminal cysteines C122 and C126
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme form SmCYP A ans SmCYP B expressed in bacterial cells as histidine-binding fusion proteins and as maltose-binding fusion proteins and also as nonfused proteins. Expression in Sf9 insect cells in their natural forms
-
overexpression as a fusion protein with Schistosoma japonicum EC 2.5.1.18 in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bulgi, F.; Khattab, A.; Vigneti, E.; Butler, R.; Cioli, D.; Klinkert, M.Q.
Expression cloning and biochemical characterizations of recombinant cyclophilin proteins from Schistosoma manoni
Protein Expr. Purif.
12
340-346
1998
Schistosoma mansoni
Manually annotated by BRENDA team
Kiang, D.; El Ghazalie, N.E.; Medhat, A.M.; Abdel-Fattah, M.; Karim, A.M.; LoVerde, P.T.
Identification and characterization of Schistosoma mansoni p17.7, a cyclophilin
Mol. Biochem. Parasitol.
76
73-82
1996
Schistosoma mansoni
Manually annotated by BRENDA team
Gourlay, L.J.; Angelucci, F.; Baiocco, P.; Boumis, G.; Brunori, M.; Bellelli, A.; Miele, A.E.
The three-dimensional structure of two redox states of cyclophilin A from Schistosoma mansoni. Evidence for redox regulation of peptidyl-prolyl cis-trans isomerase activity
J. Biol. Chem.
282
24851-24857
2007
Schistosoma mansoni (Q26548), Schistosoma mansoni
Manually annotated by BRENDA team