| 释义 |
- References
- Further reading
{{Other uses|Nans (disambiguation){{!}}Nans}}{{Infobox_gene}}Sialic acid synthase is an enzyme that in humans is encoded by the NANS gene.[1][2]{{PBB_Summary
| section_title =
| summary_text = 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.[2]
}}References1. ^{{cite journal | vauthors = Lawrence SM, Huddleston KA, Pitts LR, Nguyen N, Lee YC, Vann WF, Coleman TA, Betenbaugh MJ | title = 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 | journal = J Biol Chem | volume = 275 | issue = 23 | pages = 17869–77 |date=Jul 2000 | pmid = 10749855 | pmc = | doi = 10.1074/jbc.M000217200 }}
2. ^1 {{cite web | title = Entrez Gene: NANS N-acetylneuraminic acid synthase (sialic acid synthase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54187| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal | author=Lolas F |title=Event-related slow brain potentials, cognitive processes, and alexithymia. |journal=Psychotherapy and Psychosomatics |volume=30 |issue= 2 |pages= 116–29 |year= 1978 |pmid= 693772 |doi=10.1159/000287290 }}
- {{cite journal |vauthors=Nakata D, Close BE, Colley KJ, etal |title=Molecular cloning and expression of the mouse N-acetylneuraminic acid 9-phosphate synthase which does not have deaminoneuraminic acid (KDN) 9-phosphate synthase activity. |journal=Biochem. Biophys. Res. Commun. |volume=273 |issue= 2 |pages= 642–8 |year= 2000 |pmid= 10873658 |doi= 10.1006/bbrc.2000.2983 }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
- {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
- {{cite journal |vauthors=Humphray SJ, Oliver K, Hunt AR, etal |title=DNA sequence and analysis of human chromosome 9 |journal=Nature |volume=429 |issue= 6990 |pages= 369–74 |year= 2004 |pmid= 15164053 |doi= 10.1038/nature02465 | pmc=2734081 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
- {{cite journal | vauthors=Hao J, Balagurumoorthy P, Sarilla S, Sundaramoorthy M |title=Cloning, expression, and characterization of sialic acid synthases |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue= 3 |pages= 1507–14 |year= 2006 |pmid= 16274664 |doi= 10.1016/j.bbrc.2005.10.113 }}
- {{cite journal |vauthors=Hamada T, Ito Y, Abe T, etal |title=Solution structure of the antifreeze-like domain of human sialic acid synthase |journal=Protein Sci. |volume=15 |issue= 5 |pages= 1010–6 |year= 2006 |pmid= 16597820 |doi= 10.1110/ps.051700406 | pmc=2242509 }}
{{refend}}{{PDB Gallery|geneid=54187}}{{gene-9-stub}} 1 : Human proteins |