Archaeal peptidyl prolyl cis-trans isomerases (PPIases).

@article{Maruyama2000ArchaealPP,
  title={Archaeal peptidyl prolyl cis-trans isomerases (PPIases).},
  author={Takahiro Maruyama and Masahiro Furutani},
  journal={Frontiers in bioscience : a journal and virtual library},
  year={2000},
  volume={5},
  pages={
          D821-36
        }
}
PPIases are ubiquitous in living organisms. While 3 families of PPIases, cyclophilin (CyP), FK506 binding protein (FKBP) and parvulin (Pvn), have been studied in detail in Eukarya and Bacteria (eubacteria), little is known about archaeal PPIases. Among 2 cyclophilins found in Archaea, only Halobacterium cyclophilin (HcCyP19) has been characterized. It is a cyclosporin A (CsA) sensitive CyP with a MW of 19.4kDa. The PPIase activity and CsA sensitivity of this CyP is higher at higher salt… CONTINUE READING
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