Cloning and Expression of the HumanN-Acetylneuraminic Acid Phosphate Synthase Gene with 2-Keto-3-deoxy-d-glycero- d-galacto-nononic Acid Biosynthetic Ability

Sialic acids participate in many important biological recognition events, yet eukaryotic sialic acid biosynthetic genes are not well characterized. In this study, we have identified a novel human gene based on homology to the Escherichia colisialic acid synthase gene (neuB). The human gene is ubiqui...

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Published in:The Journal of biological chemistry 2000-06, Vol.275 (23), p.17869-17877
Main Authors: Lawrence, Shawn M., Huddleston, Kathleen A., Pitts, Lee R., Nguyen, Nam, Lee, Yuan C., Vann, Willie F., Coleman, Timothy A., Betenbaugh, Michael J.
Format: Article
Language:English
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Summary:Sialic acids participate in many important biological recognition events, yet eukaryotic sialic acid biosynthetic genes are not well characterized. In this study, we have identified a novel human gene based on homology to the Escherichia colisialic acid synthase gene (neuB). The human gene is ubiquitously expressed and encodes a 40-kDa enzyme. The gene partially restores sialic acid synthase activity in a neuB-negative mutant of E. coli and results inN-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-d-glycero-d-galacto-nononic acid (KDN) production in insect cells upon recombinant baculovirus infection. In vitro the human enzyme usesN-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively, but exhibits much higher activity toward the Neu5Ac phosphate product.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M000217200