Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.1.3.2 extracted from

  • Bhattacharyya, D.
    Reversible folding of UDP-galactose-4-epimerase from yeast Kluyveromyces fragilis (1993), Biochemistry, 32, 9726-9734.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
UDPgalactose native and renatured enzyme Kluyveromyces marxianus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
158000
-
gel filtration Kluyveromyces marxianus

Organism

Organism UniProt Comment Textmining
Kluyveromyces marxianus
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
denaturation in presence of 8 M urea. Dilution of the denaturant by sodium phosphate buffer, 20 mM, pH 7.0, containing 1 mM NAD+ recovers the activity to the extent of 80-100% Kluyveromyces marxianus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-galactose
-
Kluyveromyces marxianus UDP-glucose
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20
-
pH 7.0, 4 h stable, native enzyme Kluyveromyces marxianus

Cofactor

Cofactor Comment Organism Structure
NAD+ contains one molecule of NAD+ per dimer Kluyveromyces marxianus