4.6 Article

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

Journal

ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 7, Issue 9, Pages 1778-1780

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/b822549b

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Funding

  1. Slovak Research and Development Agency [APVV-51-040205]

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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.

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