Glycosyltransferase

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'''Galactosyltransferase''' (AGT) is a GT which catalyzes the transfer of galactose during the synthesis of polysaccharides<ref>PMID:18393823</ref>.<br />
'''Galactosyltransferase''' (AGT) is a GT which catalyzes the transfer of galactose during the synthesis of polysaccharides<ref>PMID:18393823</ref>.<br />
'''Fucosylglycoprotein 3-AGT''' (GTB) or '''histo-blood group ABO system transferase''' is the basis of the blood ABO system. It involves 3 carbohydrate antigens: A, B and H. <br />
'''Fucosylglycoprotein 3-AGT''' (GTB) or '''histo-blood group ABO system transferase''' is the basis of the blood ABO system. It involves 3 carbohydrate antigens: A, B and H. <br />
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'''Flavonoid GT''' glycosylates flavonoids<ref>PMID:23144555</ref>. For details on flavonoid GT see [[Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)]].
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'''Flavonoid GT''' glycosylates flavonoids (plant metabolites with two phenyl rings and one heterocyclic ring)<ref>PMID:23144555</ref>. For details on flavonoid GT see [[Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT)]].
== Relevance ==
== Relevance ==

Revision as of 09:31, 15 March 2016

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Contents

Function

Glycosyltransferase (GT) are enzymes which catalyze the transfer of monosaccharide to alcohol, carbohydrate, protein or inorganic phosphate[1].
Galactosyltransferase (AGT) is a GT which catalyzes the transfer of galactose during the synthesis of polysaccharides[2].
Fucosylglycoprotein 3-AGT (GTB) or histo-blood group ABO system transferase is the basis of the blood ABO system. It involves 3 carbohydrate antigens: A, B and H.
Flavonoid GT glycosylates flavonoids (plant metabolites with two phenyl rings and one heterocyclic ring)[3]. For details on flavonoid GT see Vitis vinifera Flavonoid 3-O-Glucosyltransferase (Vv3GT).

Relevance

Individuals with blood type A, B and AB has glycosyltransferase activitiy which converts antigen H to A or B. Individuals with blood type O lack this activity. For details see Human ABO(H) Blood Group Glycosyltransferases.

Disease

Mutations in mannose GT can cause muscular dystrophy and neuronal migration disorder[4].

Structural highlights

The active site of cyclodextrin GT contains three catalytic residues[5].

3D structures of glycosyltransferase

Updated on 15-March-2016

References

  1. Williams GJ, Thorson JS. Natural product glycosyltransferases: properties and applications. Adv Enzymol Relat Areas Mol Biol. 2009;76:55-119. PMID:18990828
  2. Qasba PK, Ramakrishnan B, Boeggeman E. Structure and function of beta -1,4-galactosyltransferase. Curr Drug Targets. 2008 Apr;9(4):292-309. PMID:18393823
  3. Jadhav SK, Patel KA, Dholakia BB, Khan BM. Structural characterization of a flavonoid glycosyltransferase from Withania somnifera. Bioinformation. 2012;8(19):943-9. doi: 10.6026/97320630008943. Epub 2012 Oct 1. PMID:23144555 doi:http://dx.doi.org/10.6026/97320630008943
  4. Yoshida A, Kobayashi K, Manya H, Taniguchi K, Kano H, Mizuno M, Inazu T, Mitsuhashi H, Takahashi S, Takeuchi M, Herrmann R, Straub V, Talim B, Voit T, Topaloglu H, Toda T, Endo T. Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1. Dev Cell. 2001 Nov;1(5):717-24. PMID:11709191
  5. Knegtel RM, Strokopytov B, Penninga D, Faber OG, Rozeboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW. Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products. J Biol Chem. 1995 Dec 8;270(49):29256-64. PMID:7493956

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