NANS

NANS
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 1WVO
Identifiers
Aliases	NANS, HEL-S-100, SAS, N-acetylneuraminate synthase, SEMDG
External IDs	MGI: 2149820 HomoloGene: 10343 GeneCards: NANS
EC number	2.5.1.57
Gene ontology Molecular function • N-acetylneuraminate synthase activity • transferase activity • catalytic activity • N-acylneuraminate cytidylyltransferase activity • N-acylneuraminate-9-phosphate synthase activity Cellular component • cytoplasm • cytosol • extracellular exosome Biological process • carbohydrate biosynthetic process • lipopolysaccharide biosynthetic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	54187	94181
Ensembl	ENSG00000095380	ENSMUSG00000028334
UniProt	Q9NR45 Q5TBR0	n/a
RefSeq (mRNA)	NM_018946	NM_053179
RefSeq (protein)	NP_061819.2	n/a
Location (UCSC)	Chr 9: 98.06 – 98.08 Mb	Chr 4: 46.49 – 46.5 Mb
PubMed search	[1]	[2]
Wikidata

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Sialic acid synthase is an enzyme that in humans is encoded by the NANS gene.^[3][4]

This gene encodes an enzyme that functions in the biosynthetic pathways of sialic acids. In vitro, the encoded protein uses N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), respectively. However, it exhibits much higher activity toward the Neu5Ac phosphate product. In insect cells, expression of this gene results in Neu5Ac and KDN production. This gene is related to the E. coli sialic acid synthase gene neuB, and it can partially restore sialic acid synthase activity in an E. coli neuB-negative mutant.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Lawrence SM, Huddleston KA, Pitts LR, Nguyen N, Lee YC, Vann WF, Coleman TA, Betenbaugh MJ (Jul 2000). "Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero- D-galacto-nononic acid biosynthetic ability". J Biol Chem. 275 (23): 17869–77. doi:10.1074/jbc.M000217200. PMID 10749855.
4. "Entrez Gene: NANS N-acetylneuraminic acid synthase (sialic acid synthase)".

Further reading

• Lolas F (1978). "Event-related slow brain potentials, cognitive processes, and alexithymia.". Psychotherapy and psychosomatics. 30 (2): 116–29. doi:10.1159/000287290. PMID 693772.
• Nakata D, Close BE, Colley KJ, et al. (2000). "Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-phosphate synthase activity.". Biochem. Biophys. Res. Commun. 273 (2): 642–8. doi:10.1006/bbrc.2000.2983. PMID 10873658.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Hao J, Balagurumoorthy P, Sarilla S, Sundaramoorthy M (2006). "Cloning, expression, and characterization of sialic acid synthases". Biochem. Biophys. Res. Commun. 338 (3): 1507–14. doi:10.1016/j.bbrc.2005.10.113. PMID 16274664.
• Hamada T, Ito Y, Abe T, et al. (2006). "Solution structure of the antifreeze-like domain of human sialic acid synthase". Protein Sci. 15 (5): 1010–6. doi:10.1110/ps.051700406. PMC 2242509. PMID 16597820.