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Literature summary extracted from

  • Ruzicka, F.J.; Geeganage, S.; Frey, P.A.
    Kinetic mechanism of UDP-hexose synthase, a point variant of hexose-1-phosphate uridylyltransferase from Escherichia coli (1998), Biochemistry, 37, 11385-11392.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.12 expression of mutant H166G in strain CA13, expression of mutant H166A in strain BL21(DE3)pLysS Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.12 H166 A site-directed mutagenesis, 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, highly reduced activity compared to H166G mutant Escherichia coli
2.7.7.12 H166G site-directed mutagenesis Escherichia coli
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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.12 additional information product inhibition study, wild-type and mutants H166G and H166A 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 H166A Escherichia coli
2.7.7.12 additional information
-
 additional information mutant H166G Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.12 Fe2+ contains 0.67 mol per mol of wild-type enzyme, 0.59 mol per mol of mutant H166A enzyme, and 0.7-0.76 mol per mol of mutant H166G enzyme Escherichia coli
2.7.7.12 Zn2+ contains 1.21 mol per mol of wild-type enzyme, 1.33 mol per mol of mutant H166A enzyme, and 0.99-1.16 mol per mol of mutant H166G enzyme 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 mutants H166G and H166A Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose mutant H166G, random equilibrium, intrinsically ordered substrate binding mechanism, ping pong kinetics Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.12 UDP-glucose + 2-methylimidazole kinetic study Escherichia coli uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
-
 r
2.7.7.12 UDP-glucose + 2-methylimidazole mutant H166G, i.e. UDP-hexose synthase Escherichia coli uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate
-
 r
2.7.7.12 UDP-glucose + 4-methylimidazole kinetic study Escherichia coli uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
-
 r
2.7.7.12 UDP-glucose + 4-methylimidazole mutant H166G, i.e. UDP-hexose synthase Escherichia coli uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate
-
 r
2.7.7.12 UDP-glucose + imidazole mutant H166A Escherichia coli uridine 5'-phosphoimidazole + alpha-D-glucose 1-phosphate
-
 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
2.7.7.12 uridine 5'-phospho-2,4,5-trimethylimidazole + alpha-D-glucose 1-phosphate kinetic study Escherichia coli UDP-glucose + 2,4,5-trimethylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-2,4,5-trimethylimidazole + alpha-D-glucose 1-phosphate mutant H166G, i.e. UDP-hexose synthase Escherichia coli UDP-glucose + 2,4,5-trimethylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate kinetic study Escherichia coli UDP-glucose + 2-methylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-2-methylimidazole + alpha-D-glucose 1-phosphate mutant H166G, i.e. UDP-hexose synthase Escherichia coli UDP-glucose + 2-methylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-3-methylimidazole + alpha-D-glucose 1-phosphate kinetic study Escherichia coli UDP-glucose + 3-methylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-3-methylimidazole + alpha-D-glucose 1-phosphate mutant H166G, i.e. UDP-hexose synthase Escherichia coli UDP-glucose + 3-methylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate kinetic study Escherichia coli UDP-glucose + 4-methylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-4-methylimidazole + alpha-D-glucose 1-phosphate mutant H166G, i.e. UDP-hexose synthase Escherichia coli UDP-glucose + 4-methylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-5-methylimidazole + alpha-D-glucose 1-phosphate kinetic study Escherichia coli UDP-glucose + 5-methylimidazole
-
 r
2.7.7.12 uridine 5'-phospho-5-methylimidazole + alpha-D-glucose 1-phosphate mutant H166G, i.e. UDP-hexose synthase Escherichia coli UDP-glucose + 5-methylimidazole
-
 r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.12 27
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.12 0.0167
-
 imidazole mutant H166A, forward reaction with UDP-glucose, pH 8.5, 27°C Escherichia coli
2.7.7.12 0.0217
-
 uridine 5'-phosphoimidazolate mutant H166A, forward reaction with D-glucose 1-phosphate, pH 8.5, 27°C Escherichia coli
2.7.7.12 5.52
-
 imidazole mutant H166G, forward reaction with UDP-glucose, pH 8.5, 27°C Escherichia coli
2.7.7.12 13.5
-
 uridine 5'-phosphoimidazolate mutant H166G, forward reaction with D-glucose 1-phosphate, pH 8.5, 27°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.12 additional information
-
 mutant H166G Escherichia coli
2.7.7.12 8.5
-
 assay at Escherichia coli
2.7.7.12 8.5
-
 both reaction directions Escherichia coli