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Literature summary for 5.1.3.2 extracted from

  • Vanhooke, J.L.; Frey, P.A.
    Characterization and activation of naturally occuring abortive complexes of UDP-galactose 4-epimerase from Escherichia coli (1994), J. Biol. Chem., 269, 31596-31504.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
NADH NADH associated with the purified enzyme is a component of the inactive, abortive complexes, enzyme-NADH-uridine nucleotide, that contain tightly bound uridine nucleotides in place of the epimerization intermediate UDP-4-keto-alpha-D-hexoglucopyranose. These complexes are produced in vivo in the course of bacterial growth Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
NAD+ NAD+ is very tightly but noncovalently bound in the active site, NAD+ is reduced to NADH in the course of catalysis. NADH associated with the purified enzyme is a component of the inactive, abortive complexes, enzyme-NADH-uridine nucleotide, that contain tightly bound uridine nucleotides in place of the epimerization intermediate UDP-4-keto-alpha-D-hexoglucopyranose. These complexes are produced in vivo in the course of bacterial growth Escherichia coli