Design, synthesis and catalytic activity of a serine protease synthetic model (Journal article)
Stavrakoudis, A./ Demetropoulos, I. N./ Sakarellos, C./ Sakarellos-Daitsiotis, M./ Tsikaris, V.
The design, synthesis and catalytic properties of a cyclic branched peptide carrier that possesses the catalytic triad residues of the serine proteases is reported. The synthesis of the peptide model was totally completed on solid support using three different orthogonal amino protecting groups. Hydrolytic activity measurements against Suc-Ala-Ala-Ala-pNA substrate showed that it is hydrolysed by the peptide model to a small extent. Despite this small hydrolytic activity, it is the first time, to our knowledge, that hydrolysis of such a substrate is reported by an enzyme model compound. Contrary, this enzyme model peptide showed considerable activity against the Boc-Ala-pNP substrate (k(cat)=0.414 min(-1) and K-m=0.228 mm). These results suggest that the designed carrier brings in appropriate contact the catalytic triad residues (Ser, His, Asp) resulting in the obtained hydrolytic activity.
|Institution and School/Department of submitter:||Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας|
|Keywords:||catalytic triad residues,cyclic branched peptide,cyclization on solid support,enzymatic properties of serine protease model,proline cyclic hexapeptide,serine protease model,peptide-synthesis,cyclic-peptides,chymotrypsin,reevaluation,enzymes|
|Link:||<Go to ISI>://000071627900048|
|Publisher:||Kluwer Academic Publishers|
|Appears in Collections:||Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)|
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