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

被引:77
作者
Nahalka, Jozef [1 ]
Patoprsty, Vladimir [1 ]
机构
[1] Slovak Acad Sci, Ctr Glyc, Inst Chem, SK-84538 Bratislava, Slovakia
关键词
CMP-SIALIC ACID; ESCHERICHIA-COLI; RECOMBINANT; REGENERATION; PROTEINS; GLYCOPROTEINS; AGGREGATION; ENZYMES; CELLS; GENE;
D O I
10.1039/b822549b
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
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.
引用
收藏
页码:1778 / 1780
页数:3
相关论文
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