Purification and characterization of the recombinant CMP-sialic acid synthetase from Neisseria meningitidis

被引：22

作者：

Gilbert, M ^{[1
]}

Watson, DC ^{[1
]}

Wakarchuk, WW ^{[1
]}

机构：

[1] NATL RES COUNCIL CANADA,INST BIOL SCI,OTTAWA,ON K1A 0R6,CANADA

来源：

BIOTECHNOLOGY LETTERS | 1997年 / 19卷 / 05期

关键词：

D O I：

10.1023/A:1018379607492

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

CMP-Sialic acid synthetase from Neisseria meningitidis 406Y was expressed in Escherichia coli K113 pLysS and produced at 360 U/L. The purified CMP-sialic acid synthetase used both N-acetyl-neuraminic acid (K-m = 0.34 mM) and N-glycolyl-neuraminic acid (K-m = 2.6 mM) as substrates. The recombinant synthetase could be used in a coupled reaction with an alpha-2,3-sialyltransferase to sialylate a lactose derivative in a one-reactor synthesis.

引用

页码：417 / 420

页数：4

共 11 条

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