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Literature summary extracted from

  • Arabshahi, A.; Ruzicka, F.J.; Geeganage, S.; Frey, P.A.
    Standard free energies for uridylyl group transfer by hexose-1-P uridylyltransferase and UDP-hexose synthase and for the hydrolysis of uridine 5'-phosphoimidazolate (1996), Biochemistry, 35, 3426-3428.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.12 expression of wild-type and mutant H166G in strain BL21(DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.12 H166G point mutation leads to shift of the enzyme activity to UDP-hexose synthase activity, formation of uridine 5'-phosphoimidazolate and alpha-D-glucose 1-phosphate from UDP-glucose and imidazole Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.12 additional information
-
additional information kinetics Escherichia coli
2.7.7.12 additional information
-
additional information mutant H166G Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.12 Escherichia coli
-
native mutant H166G
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.12 recombinant from overexpressing strain BL21(DE3) Escherichia coli
2.7.7.12 wild-type and mutant H166G Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.12 UDP-glucose + alpha-D-galactose 1-phosphate
-
Escherichia coli alpha-D-glucose 1-phosphate + UDP-galactose
-
r
2.7.7.12 UDP-glucose + imidazole mutant H166G, i.e. UDP-hexose synthase Escherichia coli uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
r
2.7.7.12 UDP-glucose + imidazole equilibrium study and constants Escherichia coli uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
r