FPGT

Fucose-1-phosphate guanylyltransferase, also known as FPGT, is a human gene.cite web | title = Entrez Gene: FPGT fucose-1-phosphate guanylyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8790| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: FPGT fucose-1-phosphate guanylyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8790| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Quirk S, Seley-Radtke KL |title=Purification, crystallization and preliminary X-ray characterization of the human GTP fucose pyrophosphorylase. |journal=Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |volume=62 |issue= Pt 4 |pages= 392-4 |year= 2006 |pmid= 16582493 |doi= 10.1107/S1744309106008529
*cite journal | author=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 | author=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 | author=Gerhard DS, Wagner L, Feingold EA, "et al." |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
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |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
*cite journal | author=Pastuszak I, Ketchum C, Hermanson G, "et al." |title=GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30165-74 |year= 1998 |pmid= 9804772 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |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=
*cite journal | author=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=

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