FPGT

FPGT
Identifiers
Aliases	FPGT , GFPP, fucose-1-phosphate guanylyltransferase
External IDs	OMIM: 603609 MGI: 1922790 HomoloGene: 2847 GeneCards: FPGT
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p31.1 Start 74,198,238 bp [1] End 74,234,086 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3|3 H4 Start 154,790,555 bp [2] End 154,799,040 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte Achilles tendon gallbladder secondary oocyte rectum islet of Langerhans jejunal mucosa bronchial epithelial cell corpus epididymis ganglionic eminence Top expressed in secondary oocyte interventricular septum olfactory epithelium islet of Langerhans otolith organ Region I of hippocampus proper utricle left colon medial ganglionic eminence seminal vesicula More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity nucleotide binding transferase activity, transferring phosphorus-containing groups nucleotidyltransferase activity GTP binding catalytic activity fucose-1-phosphate guanylyltransferase activity Cellular component cytoplasm cytosol Biological process fucose metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8790 75540 Ensembl ENSG00000254685 ENSMUSG00000053870 UniProt O14772 G5E8F4 RefSeq (mRNA) NM_003838 NM_001199328 NM_001199329 NM_029330 RefSeq (protein) NP_001186257 NP_001186258 NP_003829 NP_083606 Location (UCSC) Chr 1: 74.2 – 74.23 Mb Chr 3: 154.79 – 154.8 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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. GRCh38: Ensembl release 89: ENSG00000254685 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000053870 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "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.