N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela alpha2,6-sialyltransferase.

Photobacterium damsela alpha2,6-sialyltransferase was cloned as N- and C- His-tagged fusion proteins with different lengths (16-497 aa or 113-497 aa). Expression and activity assays indicated that the N-terminal 112 amino acid residues of the protein were not required for its alpha2,6-sialyltransferase activity. Among four truncated forms tested, N-His-tagged Delta15Pd2,6ST(N) containing 16-497 amino acid residues had the highest expression level.

The Hd0053 gene of Haemophilus ducreyi encodes an alpha2,3-sialyltransferase.

Haemophilus ducreyi is a Gram-negative bacterium that causes chancroid, a sexually transmitted genital ulcer disease. Different lipooligosaccharide (LOS) structures have been identified from H. ducreyi strain 35000, including those sialylated glycoforms.

Cytidine 5'-monophosphate (CMP)-induced structural changes in a multifunctional sialyltransferase from Pasteurella multocida.

Sialyltransferases catalyze reactions that transfer a sialic acid from CMP-sialic acid to an acceptor (a structure terminated with galactose, N-acetylgalactosamine, or sialic acid). They are key enzymes that catalyze the synthesis of sialic acid-containing oligosaccharides, polysaccharides, and glycoconjugates that play pivotal roles in many critical physiological and pathological processes. The structures of a truncated multifunctional Pasteurella multocida sialyltransferase (Delta24PmST1), in the absence and presence of CMP, have been determined by X-ray crystallography at 1.