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Literature summary for 5.1.3.2 extracted from

  • Liu, Y.; Vanhooke, J.L.; Frey, P.A.
    UDP-galactose 4-epimerase: NAD+ content and a charge-transfer band associated with the substrate-induced conformational transition (1996), Biochemistry, 35, 7615-7620.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
purified enzyme dimer consists of a mixture of catalytically active subunits designated enzyme-NAD+ and inactive, abortive complexes designated enzyme-NADH-uridine nucleotide, in which the uridine nucleotide may be UDPglucose, UDPgalactose, or UDP. The abortive complexes are transformed into active enzyme-NAD+ by denaturation of the purified enzyme at 4°C in 6 M guanidine hydrochloride buffered at pH 7.0 in the presence of 0.126 mM NAD+ for 3 h, followed by dilution of guanidine hydrochloride to 0.18 M and of NAD+ to 0.076 mM for 2 h. The renatured enzyme is fully active and contains negligible amounts of NADH and uridine nucleotides Escherichia coli

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
NAD+ contains firmly bound NAD+ Escherichia coli