Aldolase-catalyzed synthesis of beta-D-galp-(1-->9)-D-KDN: a novel acceptor for sialyltransferases.

[reaction: see text] beta-D-Galp-(1-->9)-D-KDN, a disaccharide component of the cell wall of Streptomyces sp. MB-8, was synthesized from beta-D-Galp-(1-->6)-D-Manp and pyruvate using a sialic acid aldolase. The obtained KDN-containing compound was a novel acceptor for bacterial sialyltransferases. Unusual alpha2,3- and alpha2,6-linked sialyltrisaccharides and a tetrasaccharide were synthesized using a one-pot two-enzyme system containing a Neisseria meningitidis CMP-sialic acid synthetase and a Pasteurella multocida sialyltransferase or a Photobacterium damsela alpha2,6-sialyltransferase.