The primary structure of peptidyl-isomerase a in Fusarium sporotrichioides

Abstract

Peptidyl-prolyl-cis-traps isomerase (PPIase) catalyzes the cis-trans isomerization of prolyl peptide bonds in polypeptides and the foldeng process of proteins. This protein was known to be cyclophilin which has high binding affinity for cyclosporin A, a cyclic undecapeptide of fungal origin with potent immunosuppressive agent. The primary structure of the peptidyl-prolyl isomerase a was determined from analysis of peptides derived by lysyl endopeptidase digestion, Staphylococcus aureus V8 digestion, cyanogen bromide cleavage and N-terminal sequence of the protein. The protein with a calculated molecular mass of 19.7 kDa consisting of 179 amino acids from the established complete sequence. The comparison of the amino acid sequence of peptidylprolyl-isomerase from Fusarium with that from Nucerospora crassa revealed significant degree of amino acid sequence similarity