FPGT
From Wikipedia, the free encyclopedia
Fucose-1-phosphate guanylyltransferase
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Identifiers | ||||||||||||||
Symbol(s) | FPGT; GFPP | |||||||||||||
External IDs | OMIM: 603609 MGI: 1922790 HomoloGene: 2847 | |||||||||||||
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Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 8790 | 75540 | ||||||||||||
Ensembl | n/a | ENSMUSG00000053870 | ||||||||||||
Refseq | NM_003838 (mRNA) NP_003829 (protein) |
XM_001005515 (mRNA) XP_001005515 (protein) |
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Location | n/a | Chr 3: 155.02 - 155.03 Mb | ||||||||||||
Pubmed search | [1] | [2] |
Fucose-1-phosphate guanylyltransferase, also known as FPGT, is a human gene.[1]
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.[1]
[edit] References
[edit] Further reading
- Quirk S, Seley-Radtke KL (2006). "Purification, crystallization and preliminary X-ray characterization of the human GTP fucose pyrophosphorylase.". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (Pt 4): 392-4. doi: . PMID 16582493.
- Quirk S, Seley KL (2005). "Identification of catalytic amino acids in the human GTP fucose pyrophosphorylase active site.". Biochemistry 44 (39): 13172-8. doi: . PMID 16185085.
- Quirk S, Seley KL (2005). "Substrate discrimination by the human GTP fucose pyrophosphorylase.". Biochemistry 44 (32): 10854-63. doi: . PMID 16086588.
- 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: . PMID 15489334.
- 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: . PMID 12477932.
- Pastuszak I, Ketchum C, Hermanson G, et al. (1998). "GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme.". J. Biol. Chem. 273 (46): 30165-74. PMID 9804772.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.