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Publication Abstract from PubMed

Serine proteinase catalyzed peptide splicing was demonstrated in both, one and two-peptide-chain (C- and N-terminal peptide chains linked by a disulfide bridge) trypsin inhibitor SFTI-1 analogues. In the second series, peptide splicing, with catalytic amount of proteinase, was observed only when formation of acyl-enzyme intermediate was preceded by the hydrolysis of the substrate Lys-Ser peptide bond. Here we presented that at an equimolar amount of the proteinase, splicing occurred in all two-peptide-chain analogues. This conclusion was supported by high resolution crystal structures of selected analogues in complex with trypsin. We showed that the process followed a direct transpeptidation mechanism. It means that the acyl-enzyme intermediate was formed and was immediately utilized for a new peptide bond formation, and products associated with the hydrolysis of acyl-enzyme were not observed. The demonstrated peptide splicing was a sequence- not structure-specific.

Investigation of serine proteinase catalyzed peptide splicing in analogues of sunflower trypsin inhibitor 1 (SFTI-1).,Karna N, Malicki S, Debowski D, Golik P, Gitlin A, Grudnik P, Wladyka B, Brzozowski K, Dubin G, Rolka K, Legowska A Chembiochem. 2015 Jul 25. doi: 10.1002/cbic.201500296. PMID:26212347^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.