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

来源：

ORGANIC & BIOMOLECULAR CHEMISTRY | 2009年 / 7卷 / 09期

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

页码：1778 / 1780

页数：3

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