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Literature summary for 5.1.3.2 extracted from

  • Thoden, J.B.; Wohlers, T.M.; Fridovich-Keil, J.L.; Holden, H.M.
    Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase (2000), Biochemistry, 39, 5691-5701.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
suitable crystallization conditions are both at room temperature and at 4°C using sparse matrix screen and the hanging drop method of vapor diffusion. The best crystals are observed growing from polyethylene glycol 8000 and potassium chloride and in the presence of 2 mM NAD+. Typical large crystals are ontained from 18-20% polyethylene glycol 8000, 100 mM Hepes, pH 7.5, and 250 mM KCl at room temperature, crystallization of a epimerase/NADH/UDP-glucose ternary complex Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information catalyzes the interconversion of UDP-glucose and UDP-galactose during normal galactose metabolism Homo sapiens ?
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+ the amino acid side chains responsible for anchoring the NAD+ to the protein include Asp33, Asn37, Asp66, Tyr157 and Lys161 Homo sapiens