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.
Yu
Hai
H
Department of Chemistry, University of California, Davis, 95616, USA.
Chen
Xi
X
D002384:Catalysis; D002473:Cell Wall / Q000737:chemistry; D004187:Disaccharides / Q000138:chemical synthesis*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015394:Molecular Structure; D009438:Neuraminic Acids / Q000138:chemical synthesis*; D007652:Oxo-Acid-Lyases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012799:Sialyltransferases / Q000737:chemistry / Q000378:metabolism*; D013302:Streptomyces / Q000737:chemistry
D004187:Disaccharides; D009438:Neuraminic Acids; D011994:Recombinant Proteins; C517696:beta-D-galp-(1-9)-D-KDN; D012799:Sialyltransferases; D007652:Oxo-Acid-Lyases; C018728:N-acetylneuraminate lyase