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Literature summary for 5.1.3.2 extracted from

  • Dutta, S.; Maiti, N.R.; Bhattacharyya, D.
    Reversible folding of UDP-galactose 4-epimerase from Escherichia coli (1997), Eur. J. Biochem., 244, 407-413.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
UDPgalactose native and renatured enzyme Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
79000
-
native and renatured enzyme, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
denatured by 8 M urea at pH 7.0 to a state having 15% of residual secondary structure. Dilution of the denaturant by 20 mM potassium phosphate, pH 8.5, leads to functional reconstitution of the enzyme. Reactivation follows a socond-order kinetics Escherichia coli

Substrates and Products (Substrate)

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
pH 8.5, 24 h, stable Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
8.5
-
25°C, 24 h, stable Escherichia coli