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Literature summary for 5.1.3.2 extracted from

  • Thoden, J.B.; Gulick, A.M.; Holden, H.M.
    Molecular structures of the S124A, S124T, and S124V site-directed mutants of UDP-galactose 4-epimerase from Escherichia coli (1997), Biochemistry, 36, 10685-10695.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S124A decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations Escherichia coli
S124T decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations Escherichia coli
S124V decrease in activity of the mutant enzymes S124A, S124T, and S124V is due to the loss of a properly positioned hydroxyl group at position 124 and not to major tertiary and quaternary structural pertubations Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P09147
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-galactose
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Escherichia coli UDP-glucose
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