An Approach to the Precise Chemoenzymatic Synthesis of 13C-Labeled Sialyloligosaccharide on an Intact Glycoprotein: A Novel One-Pot [3-13C]-Labeling Method for Sialic Acid Analogues by Control of the Reversible Aldolase Reaction, Enzymatic Synthesis of [3-13C]-NeuAc-α-(2→3)-[U-13C]-Gal-β-(1→4)-GlcNA

@inproceedings{Miyazaki2000AnAT,
  title={An Approach to the Precise Chemoenzymatic Synthesis of 13C-Labeled Sialyloligosaccharide on an Intact Glycoprotein: A Novel One-Pot [3-13C]-Labeling Method for Sialic Acid Analogues by Control of the Reversible Aldolase Reaction, Enzymatic Synthesis of [3-13C]-NeuAc-α-(2→3)-[U-13C]-Gal-β-(1→4)-GlcNA},
  author={Tatsuo Miyazaki and Hajime Sato and and Tohru Sakakibara and Yasuhiro Kajihara},
  year={2000}
}
A one-pot enzymatic 13C-labeling method for the 3-position of sialic acid (NeuAc) analogues has been developed using NeuAc aldolase, lactate dehydrogenase (LDH), alcohol dehydrogenase (ADH), and nucleotide pyrophosphatase (NPP). This method consists of two steps, the first of which is degradation to 2-acetamido-2-deoxy-d-mannose (ManNAc) analogues. This degradation reaction was accelerated by a cofactor regeneration system which converts pyruvic acid into lactic acid using LDH, ADH, and… CONTINUE READING