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PMID: 11886840 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Expression of a functional Drosophila melanogaster N-acetylneuraminic acid (Neu5Ac) phosphate synthase gene: evidence for endogenous sialic acid biosynthetic ability in insects.

Glycobiology ·Vol. 12 ·No. 2 ·2002-02-00 ·Pages 73-83

Kim K, Lawrence SM, Park J, Pitts L, Vann WF, Betenbaugh MJ, Palter KB

Abstract

In this study, we report the first cloning and characterization of a N-acetylneuraminic acid phosphate synthase gene from Drosophila melanogaster, an insect in the protostome lineage. The gene is ubiquitously expressed at all stages of Drosophila development and in Schneider cells. Similar to the human homologue, the gene encodes an enzyme with dual substrate specificity that can use either N-acetylmannosamine 6-phosphate or mannose 6-phosphate to generate phosphorylated forms of both the sialic acids, N-acetylneuraminic acid and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid, respectively, when expressed in either bacterial or baculoviral expression systems. The identification of a functional sialic acid synthase in Drosophila indicates that insects have the biosynthetic capability to produce sialic acids endogenously. Although sialylation is widely distributed in organisms of the deuterstome lineage, genetic evidence concerning the presence or absence of sialic acid metabolism in organisms of the protostome lineage has been lacking. Homology searches of the Drosophila genome identified putative orthologues of other genes required for sialylation of glycoconjugates.

MeSH Terms
Amino Acid Sequence Animals Baculoviridae/enzymology,genetics Base Sequence Cloning, Molecular Consensus Sequence DNA Primers/chemistry Drosophila melanogaster/enzymology Escherichia coli/enzymology,genetics Gene Expression Regulation, Enzymologic/physiology Molecular Sequence Data Oxo-Acid-Lyases/genetics,metabolism Polymerase Chain Reaction Recombinant Proteins/chemistry,metabolism Sequence Homology, Amino Acid Sialic Acids/biosynthesis Substrate Specificity
Chemicals
DNA Primers Recombinant Proteins Sialic Acids N-acylneuraminate-9-phosphate synthase Oxo-Acid-Lyases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Kim Kildong
Department of Biology, Temple University, Philadelphia, PA 19122, USA.
Lawrence Shawn M
Park Jung
Pitts Lee
Vann Willie F
Betenbaugh Michael J
Palter Karen B
Article Info
Journal
Glycobiology
Abbr.
Glycobiology
ISSN
0959-6658
Published
2002-02-00
Pages
73-83
Language
English
Region
England
NLM ID
9104124
Subset
IM
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