Abstract：
:Synthesis of the tripeptide Z-Phe-Arg-SerNH2 has been accomplished by a recombinant cysteine protease, cathepsin L1 from liver fluke (Fasciola hepatica), using Z-Phe-Arg-OMe as acyl acceptor and SerNH2 as nucleophile in 0.1 M ammonium acetate pH 9.0-12.5% v/v acetonitrile at 37 degrees C. LC-MS detection indicated tripeptide formation after 10 min, continuing up to 5.5 h. The ester Z-Phe-Arg-OMe was detected throughout the experiment but the hydrolysis product Z-Phe-Arg-OH appeared early and in quite large amounts. We believe that this is the first application of a parasite protease in enzymatic peptide synthesis.
journal_name
Biochimiejournal_title
Biochimieauthors
Ruth DM,McMahon G,O'Fágáin Cdoi
10.1016/j.biochi.2005.06.004keywords:
subject
Has Abstractpub_date
2006-01-01 00:00:00pages
117-20issue
1eissn
0300-9084issn
1638-6183pii
S0300-9084(05)00143-4journal_volume
88pub_type
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