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Literature summary for 2.4.1.17 extracted from

  • Takaoka, Y.; Ohta, M.; Takeuchi, A.; Miura, K.; Matsuo, M.; Sakaeda, T.; Sugano, A.; Nishio, H.
    Ligand orientation governs conjugation capacity of UDP-glucuronosyltransferase 1A1 (2010), J. Biochem., 148, 25-28.
    View publication on PubMed
Search for more literature for 2.4.1.17

Protein Variants

Protein Variants Comment Organism
F83L mutant of isoform UGT1A1, comparison of the substrate hydroxyl orientation with the values for in vitro conjugation capacity Homo sapiens
G71R mutant of isoform UGT1A1, comparison of the substrate hydroxyl orientation with the values for in vitro conjugation capacity Homo sapiens
I294T mutant of isoform UGT1A1, comparison of the substrate hydroxyl orientation with the values for in vitro conjugation capacity Homo sapiens
N400D mutant of isoform UGT1A1, comparison of the substrate hydroxyl orientation with the values for in vitro conjugation capacity Homo sapiens
R336L mutant of isoform UGT1A1, comparison of the substrate hydroxyl orientation with the values for in vitro conjugation capacity Homo sapiens
W461R mutant of isoform UGT1A1, comparison of the substrate hydroxyl orientation with the values for in vitro conjugation capacity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bilirubin + UDP-glucuronate
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 Homo sapiens bilirubin D-glucuronate + UDP
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 ?
additional information the orientation of the substrate correlates with the conjugation capacity in in vitro experiments. As glucuronidation is an intermolecular rearrangement reaction, the conjugation reaction proceeds only when the hydroxyl group of the substrate is oriented towards the coenzyme, which allows the proton transfer to occur Homo sapiens ?
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 ?