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Literature summary for 1.1.1.22 extracted from

  • Sommer, B.J.; Barycki, J.J.; Simpson, M.A.
    Characterization of human UDP-glucose dehydrogenase. CYS-276 is required for the second of two successive oxidations (2004), J. Biol. Chem., 279, 23590-23596.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

Protein Variants

Protein Variants Comment Organism
C276S no enzymic activity, affinity for NAD+ similar to wild-type, retains predominantly hexameric structure Homo sapiens
K279A no enzymic activity, affinity for NAD+ similar to wild-type, almost exclusively found as dimer Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.011
-
UDP-glucose pH 7.4, 22°C Homo sapiens
0.355
-
NAD+ pH 7.4, 22°C Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
345000
-
gel filtration, dynamic light scattering Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O60701 recombinant His-tagged enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucose + 2 NAD+ + H2O
-
Homo sapiens UDP-glucuronate + 2 NADH + 2 H+
-
?

Subunits

Subunits Comment Organism
hexamer 6 x 57000, SDS-PAGE Homo sapiens
More significant amount of dimeric and monomeric species can be detected Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens