Enzymatic synthesis of sialylation substrates powered by a novel polyphosphate kinase (PPK3).
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.
Nahálka
Jozef
J
Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Dúbravská cesta 9, SK-84538, Bratislava, Slovak Republic. nahalka@savba.sk
Pätoprstý
Vladimír
V
D055162:Biocatalysis; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D009701:Nucleoside-Diphosphate Kinase / Q000378:metabolism; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000378:metabolism*; D041902:Rhodobacteraceae / Q000201:enzymology*; D013379:Substrate Specificity
C421467:3'-sialyllactose; D009844:Oligosaccharides; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid; D017856:Phosphotransferases (Phosphate Group Acceptor); C022424:polyphosphate kinase; D009701:Nucleoside-Diphosphate Kinase