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Literature summary for 5.1.3.2 extracted from

  • Brahma, A.; Bhattacharyya, D.
    UDP-galactose 4-epimerase from Kluyveromyces fragilis. Evidence for independent mutarotation site (2004), Eur. J. Biochem., 271, 58-68.
    View publication on PubMed

General Stability

General Stability Organism
when trypsinized in the presence of 2.5 mM 5'-UMP, the mutarotase activity is lost in a time-dependent manner without affecting the epimerase activity. Proteolysis under identical conditions in the presence of 6.7 mM galactose or fructose leads to reversal of this protection - epimerase activity is completely lost whereas mutarotase activity is 90% protected Kluyveromyces marxianus

Inhibitors

Inhibitors Comment Organism Structure
UDP 5.0 mM, 25% inhibition Kluyveromyces marxianus
UMP 5.0 mM, 44% inhibition Kluyveromyces marxianus
UTP 5.0 mM, 13% inhibition Kluyveromyces marxianus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
2 * 75000, SDS-PAGE Kluyveromyces marxianus

Organism

Organism UniProt Comment Textmining
Kluyveromyces marxianus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Kluyveromyces marxianus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
73
-
-
Kluyveromyces marxianus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the epimerase shows associated mutarotase activity distinct from the constitutively formed mutarotase activity. Both activities exist in two functionally independent domains Kluyveromyces marxianus ?
-
?
UDP-galactose
-
Kluyveromyces marxianus UDP-glucose
-
?

Subunits

Subunits Comment Organism
dimer 2 * 75000, SDS-PAGE Kluyveromyces marxianus