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

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

Organic & biomolecular chemistry (2009-07-11)
Jozef Nahálka, Vladimír Pätoprstý
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Cytidine-5′-monophospho-N-acetylneuraminic acid sodium salt, ≥85% (HPLC)
Sigma-Aldrich
Sialic Acid Aldolase from Escherichia coli K12, recombinant, expressed in E. coli BL21, ≥3.0 units/mg protein