Peptidyl‐prolyl cis‐trans isomerase from Bacillus subtilis A prokaryotic enzyme that is highly sensitive to cyclosporin A

FEBS Letters

Marahiel, Mohamed A.¹  Brune, Kay²  Bang, Holger²  Herrler, Michael¹  Fischer, Gunter³ 

[1] Philips-Universität Marburg, Fachbereich Chemie/Biochemie, W-3550 Marburg, Germany;Institut für Pharmakologie und Toxikologie, Universität Erlangen-Nürnberg, W-8520 Erlangen, Germany;Max-Planck Gesellschaft zur Förderung der Wissenschaften c.V. Halle, O-4050 Halle, Germany

关键词: Basillus subtilis;    Peptidyl-prolyl cis-trans isomerase;    Cyclosporin A;   

DOI  :  10.1016/0014-5793(92)80779-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cyclophylins are members of a class of proteins with peptidyl-protyl cis-trans isomerase activity. These enzymes bind the immunosuppressive agent, cyclosporin A (CsA), which acts as a competitive inhibitor. The peptidyl-prolyl cis-trans isomerase from Bacillus subtilis (PPlase) was purified to homogeneity in a 4-step purification procedure, which resulted in a 100-fold protein purification with a yield of 5%, Coomassie blue-stained SDS-PAGE revealed a single band of about 18 kDa. PPlase activity was determined using synthetic peptides as substrates in a 2-step reaction coupled to chymotrypsin. Treatment of Bacillus subtilis PPlase by CsA revealed an inhibition constant of K ₁=175 nM, which differs from cyclophilin of enterobacteria such as E. coli or Salmonella typhimurium and is in the range of human enzymes.

【 授权许可】

Unknown