フザリウム スポロトリキオイデス菌のペプチジルプロリル異性化酵素の一次構造の決定

抄録

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