期刊
BIOORGANIC & MEDICINAL CHEMISTRY
卷 16, 期 22, 页码 9830-9836出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2008.09.056
关键词
Neisseria meningitidis; D-A5P; KDOP; Lipopolysaccharide biosynthesis
资金
- Massey University Research Fund
- Royal Society of New Zealand Marsden Fund [MAU008]
3-Deoxy-D-manno-octulosonate 8-phosphate (KDO8P) synthase catalyses the condensation reaction between phosphoenolpyruvate and D-arabinose 5-phosphate (D-A5P) in a key step in lipopolysaccharide biosynthesis in Gram-negative bacteria. The KDO8P synthase from Neisseria meningitidis was cloned into Escherichia coli, overexpressed and purified. A variety of D-A5P stereoisomers were tested as substrates, of these only D-A5P and L-X5P were substrates. The Asn59Ala mutant of N. meningitidis KDO8P synthase was constructed and this mutant retained less than 1% of the wild-type activity. These results are consistent with a catalytic mechanism for this enzyme in which the C2 and C3 hydroxyl groups of D-A5P and Asn59 are critical. (C) 2008 Elsevier Ltd. All rights reserved.
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