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Information on EC 5.2.1.8 - peptidylprolyl isomerase

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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:
UNIPROT: Q6UX04
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Word Map
The enzyme appears in 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
Cyclophilin
-
peptidyl-prolyl isomerase
-
SDCCAG-10
-
spliceosome-associated protein CWC27 homolog
-
12 kDa FKBP
-
-
-
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12.6 kDa FKBP
-
-
-
-
13 kDa FKBP
-
-
-
-
15 kDa FKBP
-
-
-
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19 kDa FK506-binding protein
-
-
-
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22 kDa FK506-binding protein
-
-
-
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25 kDa FKBP
-
-
-
-
27 kDa membrane protein
-
-
-
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36 kDa FK506 binding protein
-
-
-
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40 kDa thylakoid lumen PPIase
-
-
-
-
40 kDa thylakoid lumen rotamase
-
-
-
-
51 kDa FK506-binding protein
-
-
-
-
52 kDa FK506 binding protein
-
-
-
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54 kDa progesterone receptor-associated immunophilin
-
-
-
-
65 kDa FK506-binding protein
-
-
-
-
CGI-124
-
-
-
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Chl-Mip
-
-
-
-
CPH
-
-
-
-
Cyclophilin
-
-
-
-
Cyclophilin 18
-
-
-
-
Cyclophilin 33
-
-
-
-
Cyclophilin A
-
-
-
-
Cyclophilin B
-
-
-
-
Cyclophilin C
-
-
-
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Cyclophilin cyp2
-
-
-
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Cyclophilin homolog
-
-
-
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Cyclophilin ScCypA
-
-
-
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Cyclophilin ScCypB
-
-
-
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Cyclophilin-10
-
-
-
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Cyclophilin-11
-
-
-
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Cyclophilin-40
-
-
-
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Cyclophilin-60
-
-
-
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Cyclophilin-like protein Cyp-60
-
-
-
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Cyclophilin-related protein
-
-
-
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Cyclosporin A-binding protein
-
-
-
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CYP-40
-
-
-
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CYP-S1
-
-
-
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Cyp3 PPIase
-
-
-
-
CyPA
-
-
-
-
CyPB
-
-
-
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Estrogen receptor binding cyclophilin
-
-
-
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FF1 antigen
-
-
-
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FKBP
-
-
-
-
FKBP-12
-
-
-
-
FKBP-12.6
-
-
-
-
FKBP-13
-
-
-
-
FKBP-15
-
-
-
-
FKBP-19
-
-
-
-
FKBP-21
-
-
-
-
FKBP-22
-
-
-
-
FKBP-23
-
-
-
-
FKBP-25
-
-
-
-
FKBP-36
-
-
-
-
FKBP-51
-
-
-
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FKBP-70
-
-
-
-
FKBP22
-
-
-
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FKBP52 protein
-
-
-
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FKBP54
-
-
-
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FKBP59
-
-
-
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FKBP65
-
-
-
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FKBP65RS
-
-
-
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HBI
-
-
-
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Histidine rich protein
-
-
-
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hPar14
-
-
-
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HSP binding immunophilin
-
-
-
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HSP90-binding immunophilin
-
-
-
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Immunophilin FKBP12
-
-
-
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Immunophilin FKBP12.6
-
-
-
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Immunophilin FKBP36
-
-
-
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Immunophilin FKBP65
-
-
-
-
Isomerase, peptidylprolyl cis-trans
-
-
-
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Macrolide binding protein
-
-
-
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Macrophage infectivity potentiator
-
-
-
-
MtFK
-
-
-
-
Nucleolar proline isomerase
-
-
-
-
p17.7
-
-
-
-
P31
-
-
-
-
P54
-
-
-
-
p59 protein
-
-
-
-
Par14
-
-
-
-
Parvulin
-
-
-
-
Parvulin 14
-
-
-
-
Peptide bond isomerase
-
-
-
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Peptidyl-prolyl cis-trans isomerase
-
-
-
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Peptidyl-prolyl cis-trans isomerase plp
-
-
-
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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
-
-
-
-
Planta-induced rust protein 28
-
-
-
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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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Rapamycin-binding protein
-
-
-
-
Rapamycin-selective 25 kDa immunophilin
-
-
-
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Rotamase
-
-
-
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Rotamase Pin1
-
-
-
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Rotamase Pin4
-
-
-
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Rotamase plp
-
-
-
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S-cyclophilin
-
-
-
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S1205-06
-
-
-
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SCYLP
-
-
-
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SmCYP A
-
-
-
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SmCYP B
-
-
-
-
Smp17.7
-
-
-
-
SP18
-
-
-
-
WHP
-
-
-
-
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
-
-
-
?
succinyl-Ala-Gly-(cis)-Pro-Phe-4-nitroanilide
succinyl-Ala-Gly-(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
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CWC27_HUMAN
472
0
53847
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 53800, calculated for full-length protein, x * 17000, N-terminal fragment
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M NaI
structure of a relatively protease-resistant N-terminal fragment containing the PPIase domain, t 2.0 A resolution. Residues Arg56, Phe61, Ile62, Gln64, Ala102, Asn103, Phe114, Glu122, Leu123 and His127 in beta-strands 3, 4 and 6, as well as in the extended loop connecting beta-strands 6 and 7, form the proline-binding pocket
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
melting temperature, peptidyl-prolyl cis-trans isomerase domain
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Gold DE3 cells
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Davis, T.L.; Walker, J.R.; Campagna-Slater, V.; Finerty, P.J.; Paramanathan, R.; Bernstein, G.; MacKenzie, F.; Tempel, W.; Ouyang, H.; Lee, W.H.; Eisenmesser, E.Z.; Dhe-Paganon, S.
Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases
PLoS Biol.
8
e1000439
2010
Homo sapiens (O43447), Homo sapiens (P23284), Homo sapiens (P30405), Homo sapiens (P45877), Homo sapiens (P62937), Homo sapiens (Q08752), Homo sapiens (Q13427), Homo sapiens (Q6UX04), Homo sapiens (Q9UNP9), Homo sapiens
Manually annotated by BRENDA team
Ulrich, A.; Wahl, M.C.
Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27
Acta Crystallogr. Sect. D
70
3110-3123
2014
Homo sapiens (Q6UX04), Homo sapiens, Thermochaetoides thermophila (G0RY38), Thermochaetoides thermophila DSM 1495 (G0RY38)
Manually annotated by BRENDA team