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Literature summary for 2.7.7.12 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
Search for more literature for 2.7.7.12

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
H166G site-directed mutagenesis Escherichia coli
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Escherichia coli
additional information
-
 additional information mutant H166A Escherichia coli
additional information
-
 additional information mutant H166G Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
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
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

Organism UniProt Comment Textmining
Escherichia coli
-
 native mutant H166G
-

Purification (Commentary)

Purification (Comment) Organism
recombinant mutants H166G and H166A Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
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)

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

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

Turnover Number [1/s]

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

pH Optimum

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