USE OF ESCHERICHIA-COLI POLYPHOSPHATE KINASE FOR OLIGOSACCHARIDE SYNTHESIS

The Escherichia coil polyphosphate kinase (PPK) has been known to cata lyze the reversible transfer of phosphate molecules between ATP and po lyphosphate (poly(P)). It has also been found that the PPK catalyzes t he kination of not only ADP but also other nucleoside diphosphates (ND Ps) using poly(P) as a phosphate donor, yielding nucleotide triphospha tes (NTPs). We used the PPK and poly(P) in place of pyruvate kinase an d phosphoenol pyruvate for NTP regeneration followed by synthesis of s ugar nucleotides in a cyclic synthesis system for oligosaccharides. It was confirmed that the PPK efficiently catalyzed the UTP regeneration in the cyclic system of N-acetyllactosamine synthesis. This novel act ivity of PPK enables us to perform the practical synthesis of oligosac charides.