Carboxypeptidase A-catalyzed dipeptide synthesis in organic media.
The carboxypeptidase A-catalyzed syntheses of dipeptides from L-amino acids (Phe, Tyr, Trp, Leu and Ile) were studied in various water-miscible (acetone, acetonitrile, ethanol, methanol and 1,4-dioxane) organic solvents. The highest yield (43%) was achieved in acetonitrile with L-Phe as substrate, after a 24-h incubation. The optimal conditions of Phe-Phe synthesis in acetonitrile were determined. For maximal conversion 1.2 mM L-Phe, 1.4 mg ml-1 enzyme and about 10% water are needed in buffered aqueous acetonitrile (pH 5.5) at 30 degrees C.
Vértesi
A
A
Department of Biochemistry, József Attila University, Szeged, Hungary.
Simon
L M
LM
D000097:Acetonitriles; D001671:Biochemistry / Q000379:methods*; D002268:Carboxypeptidases / Q000737:chemistry* / Q000378:metabolism*; D043422:Carboxypeptidases A; D004151:Dipeptides / Q000138:chemical synthesis* / Q000378:metabolism; D010649:Phenylalanine / Q000737:chemistry; D012997:Solvents
D000097:Acetonitriles; D004151:Dipeptides; D012997:Solvents; D010649:Phenylalanine; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; C032159:acetonitrile