Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3)

Org Biomol Chem. 2009 May 7;7(9):1778-80. doi: 10.1039/b822549b. Epub 2009 Mar 23.

Abstract

Active inclusion bodies of polyphosphate kinase 3 and cytidine 5'-monophosphate kinase were combined with whole cells that co-express sialic acid aldolase and CMP-sialic acid synthetase. The biocatalytic mixture was used for the synthesis of CMP-sialic acid, which was then converted to 3'-sialyllactose by whole cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis
  • Cytidine Monophosphate N-Acetylneuraminic Acid / chemistry
  • Cytidine Monophosphate N-Acetylneuraminic Acid / metabolism*
  • Molecular Structure
  • Nucleoside-Diphosphate Kinase / metabolism
  • Oligosaccharides / chemistry
  • Oligosaccharides / metabolism
  • Phosphotransferases (Phosphate Group Acceptor) / metabolism*
  • Rhodobacteraceae / enzymology*
  • Substrate Specificity

Substances

  • 3'-sialyllactose
  • Oligosaccharides
  • Cytidine Monophosphate N-Acetylneuraminic Acid
  • Phosphotransferases (Phosphate Group Acceptor)
  • polyphosphate kinase
  • Nucleoside-Diphosphate Kinase