| 释义 |
- References
- Further reading
{{Underlinked|date=May 2016}}{{Infobox_gene}}Fucose-1-phosphate guanylyltransferase is an enzyme that in humans is encoded by the FPGT gene.[1][2]L-fucose is a key sugar in glycoproteins and other complex carbohydrates since it may be involved in many of the functional roles of these macromolecules, such as in cell–cell recognition. The fucosyl donor for these fucosylated oligosaccharides is GDP-beta-L-fucose. There are two alternate pathways for the biosynthesis of GDP-fucose; the major pathway converts GDP-alpha-D-mannose to GDP-beta-L-fucose. The protein encoded by this gene participates in an alternate pathway that is present in certain mammalian tissues, such as liver and kidney, and appears to function as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids. This pathway involves the phosphorylation of L-fucose to form beta-L-fucose-1-phosphate, and then condensation of the beta-L-fucose-1-phosphate with GTP by fucose-1-phosphate guanylyltransferase to form GDP-beta-L-fucose.[3] References1. ^{{cite journal | vauthors = Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD | title = GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme | journal = J Biol Chem | volume = 273 | issue = 46 | pages = 30165–74 |date=Dec 1998 | pmid = 9804772 | pmc = | doi =10.1074/jbc.273.46.30165 }}
2. ^{{cite web | title = Entrez Gene: FPGT fucose-1-phosphate guanylyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8790| accessdate = }}
3. ^{{cite web | title = Entrez Gene: FPGT fucose-1-phosphate guanylyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8790| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal | vauthors=Quirk S, Seley-Radtke KL |title=Purification, crystallization and preliminary X-ray characterization of the human GTP fucose pyrophosphorylase. |journal=Acta Crystallographica Section F |volume=62 |issue= Pt 4 |pages= 392–4 |year= 2006 |pmid= 16582493 |doi= 10.1107/S1744309106008529 | pmc=2222559 }}
- {{cite journal | vauthors=Quirk S, Seley KL |title=Identification of catalytic amino acids in the human GTP fucose pyrophosphorylase active site. |journal=Biochemistry |volume=44 |issue= 39 |pages= 13172–8 |year= 2005 |pmid= 16185085 |doi= 10.1021/bi051288d }}
- {{cite journal | vauthors=Quirk S, Seley KL |title=Substrate discrimination by the human GTP fucose pyrophosphorylase. |journal=Biochemistry |volume=44 |issue= 32 |pages= 10854–63 |year= 2005 |pmid= 16086588 |doi= 10.1021/bi0503605 }}
- {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |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 |display-authors=etal}}
- {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal}}
- {{cite journal | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
- {{cite journal | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
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