Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.2.1.8 - peptidylprolyl isomerase

for references in articles please use BRENDA:EC5.2.1.8
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
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
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
peptidylproline (omega=180) = peptidylproline (omega=0)
show the reaction diagram