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Literature summary for 2.4.1.87 extracted from

  • Gomez, H.; Lluch, J.; Masgrau, L.
    Substrate-assisted and nucleophilically assisted catalysis in bovine alpha1,3-galactosyltransferase. Mechanistic implications for retaining glycosyltransferases (2013), J. Am. Chem. Soc., 135, 7053-7063.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E317A/E317Q site-directed mutagenesis, substrate binding compared to wild-type Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
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-
-

Synonyms

Synonyms Comment Organism
alpha1,3-galactosyltransferase
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Bos taurus
alpha1,3-GalT
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Bos taurus

General Information

General Information Comment Organism
evolution the enzyme is a family 6 glycosyltransferase, family members have a nucleophilic residue (Glu317) situated close to the anomeric carbon Bos taurus
additional information reaction mechanism: substrate-assisted mechanism for retaining glycosyltransferases consisting of the stabilization of the developing negative charge on the beta-phosphate by the hydrogen of the attacking hydroxyl group of the acceptor molecule. This interaction is impaired in the alpha1,3-GalT reactants, which explains why Glu317 is required to nucleophilically assist initial catalysis by pushing leaving-group departure. The presence of Glu317 opens the door to the possibility of a double-displacement mechanism in GT6 family. In alpha1,3-GalT the substrate-assisted catalysis might be necessary in both mechanisms, because the nucleophilic strength of Glu317 is reduced by the interactions it makes to ensure proper acceptor binding. The same effect might be found in the absence of the acceptor when Glu317 interacts with water molecules, quantum mechanics/molecular mechanics dynamic simulations analysis, overview Bos taurus