FPGT: Difference between revisions

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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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.<ref name="entrez">{{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 = }}</ref>
| 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.<ref name="entrez">{{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 = }}</ref>
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{{PBB_Further_reading  
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| citations =  
| citations =  
*{{cite journal  | vauthors=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  | pmc=2222559 }}
*{{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=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=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 }}

Latest revision as of 15:30, 8 October 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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.[2]

References

  1. 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.
  2. 2.0 2.1 "Entrez Gene: FPGT fucose-1-phosphate guanylyltransferase".

Further reading