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Information on EC 5.2.1.8 - peptidylprolyl isomerase and Organism(s) Lupinus luteus and UniProt Accession O49886

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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:
Lupinus luteus
UNIPROT: O49886
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The taxonomic range for the selected organisms is: Lupinus luteus
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
-
-
-
-
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
-
-
-
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40 kDa thylakoid lumen PPIase
-
-
-
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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
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-
-
-
Cyclophilin B
-
-
-
-
Cyclophilin C
-
-
-
-
Cyclophilin cyp2
-
-
-
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Cyclophilin homolog
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-
-
-
Cyclophilin ScCypA
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-
-
-
Cyclophilin ScCypB
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-
-
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Cyclophilin-10
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-
-
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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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-
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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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-
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CYP-S1
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-
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Cyp3 PPIase
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-
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CyPA
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-
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CyPB
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-
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Estrogen receptor binding cyclophilin
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-
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FF1 antigen
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-
-
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FKBP
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-
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FKBP-12
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-
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FKBP-12.6
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-
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FKBP-13
-
-
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FKBP-15
-
-
-
-
FKBP-19
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-
-
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FKBP-21
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-
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FKBP-22
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-
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FKBP-23
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-
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FKBP-25
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-
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FKBP-36
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-
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FKBP-51
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-
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FKBP-70
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-
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FKBP22
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-
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FKBP52 protein
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-
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FKBP54
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-
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-
FKBP59
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FKBP65
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FKBP65RS
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-
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HBI
-
-
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Histidine rich protein
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-
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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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-
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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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-
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MtFK
-
-
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Nucleolar proline isomerase
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-
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-
p17.7
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-
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-
P31
-
-
-
-
P54
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-
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p59 protein
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-
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Par14
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-
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Parvulin
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-
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Parvulin 14
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-
-
-
Peptide bond isomerase
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-
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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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Peptidyl-prolyl cis-trans isomerase surA
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Peptidyl-prolyl cis/trans isomerase EPVH
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-
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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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PPIase
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PPIase Pin1
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PPIase Pin4
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-
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Proline rotamase
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Proteins, cyclophilins
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-
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Proteins, specific or class, cyclophilins
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Rapamycin-binding protein
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Rapamycin-selective 25 kDa immunophilin
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-
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Rotamase
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-
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Rotamase Pin1
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Rotamase Pin4
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-
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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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-
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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
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CYPH_LUPLU
172
0
18287
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18000
x * 18000, SDS-PAGE of recombinant enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 18000, SDS-PAGE of recombinant enzyme
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nuc, K.; Lesniewicz, K.; Nuc, P.; S?omski, R.
Yellow lupine cyclophilin interacts with nucleic acids
Protein Pept. Lett.
15
719-723
2008
Lupinus luteus (O49886), Lupinus luteus
Manually annotated by BRENDA team