| FPGT | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | FPGT, GFPP, fucose-1-phosphate guanylyltransferase | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 603609 MGI: 1922790 HomoloGene: 2847 GeneCards: FPGT | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Fucose-1-phosphate guanylyltransferase is an enzyme that in humans is encoded by the FPGT gene.[5][6]
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.[6]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000254685 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000053870 - Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD (Dec 1998). "GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme". J Biol Chem. 273 (46): 30165–74. doi:10.1074/jbc.273.46.30165. PMID 9804772.
- 1 2 "Entrez Gene: FPGT fucose-1-phosphate guanylyltransferase".
Further reading
- Quirk S, Seley-Radtke KL (2006). "Purification, crystallization and preliminary X-ray characterization of the human GTP fucose pyrophosphorylase". Acta Crystallographica Section F. 62 (Pt 4): 392–4. doi:10.1107/S1744309106008529. PMC 2222559. 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:10.1021/bi051288d. PMID 16185085.
- Quirk S, Seley KL (2005). "Substrate discrimination by the human GTP fucose pyrophosphorylase". Biochemistry. 44 (32): 10854–63. doi:10.1021/bi0503605. 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:10.1101/gr.2596504. PMC 528928. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- 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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.