FKBP-type peptidyl-prolyl cis-trans isomerases (PPIases) are a class of enzymes that play a crucial role in protein folding by catalyzing the cis-trans isomerization of proline residues in polypeptides. These enzymes are also known as immunophilins due to their ability to bind immunosuppressive drugs like FK506 (tacrolimus) and rapamycin. The recombinant expression of these enzymes in Escherichia coli (E. coli) has been a significant area of research due to their potential applications in biotechnology and medicine.
FKBP-type PPIases are characterized by their FK506-binding domain, which is responsible for their isomerase activity. This domain facilitates the conversion of proline residues between their cis and trans conformations, a process essential for proper protein folding and function. The isomerase activity of these enzymes is crucial for various cellular processes, including signal transduction, protein trafficking, and stress responses .
The recombinant expression of FKBP-type PPIases in E. coli involves the insertion of the gene encoding the enzyme into an expression vector, which is then introduced into the bacterial cells. This allows for the production of large quantities of the enzyme, which can be purified and studied in detail. The use of E. coli as a host organism is advantageous due to its rapid growth, well-characterized genetics, and ease of manipulation .
The recombinant FKBP-type PPIases expressed in E. coli have several important applications: