Design, synthesis and catalytic activity of a serine protease synthetic model

 
This item is provided by the institution :
University of Ioannina
Repository :
Repository of UOI Olympias
see the original item page
in the repository's web site and access all digital files if the item*
share



1997 (EN)
Design, synthesis and catalytic activity of a serine protease synthetic model (EN)

Stavrakoudis, A. (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)
Stavrakoudis, A. (EN)

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. (EN)

catalytic triad residues (EN)

Πανεπιστήμιο Ιωαννίνων (EL)
University of Ioannina (EN)

Letters in Peptide Science (EN)

1997

<Go to ISI>://000071627900048

Kluwer Academic Publishers (EN)



*Institutions are responsible for keeping their URLs functional (digital file, item page in repository site)