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Literature summary for 2.4.1.255 extracted from

  • Lazarus, M.B.; Jiang, J.; Gloster, T.M.; Zandberg, W.F.; Whitworth, G.E.; Vocadlo, D.J.; Walker, S.
    Structural snapshots of the reaction coordinate for O-GlcNAc transferase (2012), Nat. Chem. Biol., 8, 966-968.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
UDP-N-acetyl-5-deoxy-5-thio-alpha-D-glucosamine effective inhibitor Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O15294
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is not able to transfer UDP-glucose or UDP-2-dehydro-alpha-D-glucose to peptide and protein substrates Homo sapiens ?
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-serine UDP-N-acetyl-5-deoxy-5-thio-alpha-D-glucosamine is a very poor (3200times slower) donor substrate compared to UDP-N-acetyl-D-glucosamine Homo sapiens ?
-
?
UDP-N-acetyl-D-glucosamine + [protein]-L-serine the enzyme transfers N-acetylglucosamine from the sugar donor UDP-GlcNAc onto specific serine or threonine residues of nucleocytoplasmic proteins with inversion of configuration at the anomeric center Homo sapiens UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine
-
?

Synonyms

Synonyms Comment Organism
O-GlcNAc transferase
-
Homo sapiens
O-linked beta-N-acetylglucosamine transferase
-
Homo sapiens
OGT
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Homo sapiens