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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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.
mechanism for regulation of isoform cyclosporin A activity via oxidation of its thiol groups at C122 and C126, oxidized enzyme is inactive, whereas the reduced enzyme is an efficient isomerase
mechanism for regulation of isoform cyclosporin A activity via oxidation of its thiol groups at C122 and C126, oxidized enzyme is inactive, whereas the reduced enzyme is an efficient isomerase
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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
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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
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