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Literature summary for 2.7.7.27 extracted from

  • Bejar, C.M.; Jin, X.; Ballicora, M.A.; Preiss, J.
    Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases (2006), J. Biol. Chem., 281, 40473-40484.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
D-fructose 1,6-diphosphate 50% of maximal activation at 0.059 for wild-type Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
homology model of enzyme strucutre complexed with ADP-glucose Escherichia coli

Protein Variants

Protein Variants Comment Organism
D239A residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
D239E residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
D239N residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
D276A residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
D276E residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
D276N residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
E194A residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
E194D residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
E194Q residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
F240A residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
F240M residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
K195Q residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
S212A residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
S212T residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
S212V residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
S212Y residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
W274A residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
W274F residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
W274L residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli
Y216F residue in close proximity to the glucose moiety of ADP-glucose substrate. Significant decrease in affinity for glucose 1-phosphate, kinetic analysis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
alpha-D-glucose 1-phosphate wild-type, pH 8.0, 37°C Escherichia coli
0.05
-
alpha-D-glucose 1-phosphate mutant W274F, pH 8.0, 37°C Escherichia coli
0.09
-
alpha-D-glucose 1-phosphate mutant S212Y, pH 8.0, 37°C Escherichia coli
0.122
-
alpha-D-glucose 1-phosphate mutant F240M, pH 8.0, 37°C Escherichia coli
0.16
-
ATP mutant D239A, pH 8.0, 37°C Escherichia coli
0.169
-
alpha-D-glucose 1-phosphate mutant D239E, pH 8.0, 37°C Escherichia coli
0.17
-
ATP mutant E194Q, pH 8.0, 37°C Escherichia coli
0.19
-
ATP mutant K195Q, pH 8.0, 37°C Escherichia coli
0.204
-
alpha-D-glucose 1-phosphate mutant F240A, pH 8.0, 37°C Escherichia coli
0.24
-
alpha-D-glucose 1-phosphate mutant S212A, pH 8.0, 37°C Escherichia coli
0.264
-
alpha-D-glucose 1-phosphate mutant D239N, pH 8.0, 37°C Escherichia coli
0.28
-
ATP mutant W274F, pH 8.0, 37°C Escherichia coli
0.35
-
ATP mutant Y216F, pH 8.0, 37°C Escherichia coli
0.367
-
alpha-D-glucose 1-phosphate mutant W274A, pH 8.0, 37°C Escherichia coli
0.38
-
ATP mutant S212V, pH 8.0, 37°C Escherichia coli
0.41
-
alpha-D-glucose 1-phosphate mutant D276E, pH 8.0, 37°C Escherichia coli
0.41
-
ATP mutant S212T, pH 8.0, 37°C Escherichia coli
0.43
-
ATP mutant S212Y, pH 8.0, 37°C Escherichia coli
0.48
-
ATP mutant W274L, pH 8.0, 37°C Escherichia coli
0.49
-
ATP mutant E194D, pH 8.0, 37°C Escherichia coli
0.524
-
alpha-D-glucose 1-phosphate mutant D239A, pH 8.0, 37°C Escherichia coli
0.525
-
alpha-D-glucose 1-phosphate mutant W274L, pH 8.0, 37°C Escherichia coli
0.56
-
ATP mutant D239N, pH 8.0, 37°C Escherichia coli
0.59
-
ATP wild-type, pH 8.0, 37°C Escherichia coli
0.68
-
ATP mutant S212A, pH 8.0, 37°C Escherichia coli
0.785
-
alpha-D-glucose 1-phosphate mutant Y216F, pH 8.0, 37°C Escherichia coli
0.96
-
ATP mutant D239E, pH 8.0, 37°C Escherichia coli
1.04
-
ATP mutant W274A, pH 8.0, 37°C Escherichia coli
1.14
-
ATP mutant F240A, pH 8.0, 37°C Escherichia coli
1.2
-
ATP mutant E194A, pH 8.0, 37°C Escherichia coli
1.44
-
alpha-D-glucose 1-phosphate mutant E194Q, pH 8.0, 37°C Escherichia coli
1.45
-
alpha-D-glucose 1-phosphate mutant D276N, pH 8.0, 37°C Escherichia coli
1.7
-
alpha-D-glucose 1-phosphate mutant D276A, pH 8.0, 37°C Escherichia coli
1.98
-
ATP mutant F240M, pH 8.0, 37°C Escherichia coli
2.03
-
ATP mutant D276A, pH 8.0, 37°C Escherichia coli
2.3
-
ATP mutant D276N, pH 8.0, 37°C Escherichia coli
2.81
-
alpha-D-glucose 1-phosphate mutant E194A, pH 8.0, 37°C Escherichia coli
4.66
-
alpha-D-glucose 1-phosphate mutant S212T, pH 8.0, 37°C Escherichia coli
4.77
-
ATP mutant D276E, pH 8.0, 37°C Escherichia coli
6.42
-
alpha-D-glucose 1-phosphate mutant S212V, pH 8.0, 37°C Escherichia coli
6.59
-
alpha-D-glucose 1-phosphate mutant E194D, pH 8.0, 37°C Escherichia coli
16.7
-
alpha-D-glucose 1-phosphate mutant K195Q, pH 8.0, 37°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Km value for wild-type 2.6 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6V1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + alpha-D-glucose 1-phosphate
-
Escherichia coli diphosphate + ADP-glucose
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
5 min, 85% residual activity for wild-type Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.36
-
ATP mutant D276A, pH 8.0, 37°C Escherichia coli
0.37
-
ATP mutant D276N, pH 8.0, 37°C Escherichia coli
0.52 0.7 ATP mutant E194Q, pH 8.0, 37°C Escherichia coli
1.6
-
ATP mutant S212Y, pH 8.0, 37°C Escherichia coli
15.4
-
ATP mutant E194A, pH 8.0, 37°C Escherichia coli
22.4
-
ATP mutant S212V, pH 8.0, 37°C Escherichia coli
27
-
ATP mutant D276E, pH 8.0, 37°C Escherichia coli
29
-
ATP mutant Y216F, pH 8.0, 37°C Escherichia coli
32.7
-
ATP mutant D239A, pH 8.0, 37°C Escherichia coli
80.7
-
ATP mutant E194Q, pH 8.0, 37°C Escherichia coli
92.7
-
ATP mutant E194D, pH 8.0, 37°C Escherichia coli
104
-
ATP mutant E194D, pH 8.0, 37°C Escherichia coli
112.7
-
ATP mutant D276E, pH 8.0, 37°C Escherichia coli
169
-
ATP mutant D239N, pH 8.0, 37°C Escherichia coli
171.7
-
ATP mutant F240A, pH 8.0, 37°C Escherichia coli
179
-
ATP mutant S212T, pH 8.0, 37°C Escherichia coli
193.3
-
ATP mutant K195Q, pH 8.0, 37°C Escherichia coli
247.5
-
ATP mutant W274L, pH 8.0, 37°C Escherichia coli
266
-
ATP mutant W274F, pH 8.0, 37°C Escherichia coli
347.7
-
ATP mutant D239E, pH 8.0, 37°C Escherichia coli
370
-
ATP wild-type, pH 8.0, 37°C Escherichia coli
371.2
-
ATP mutant S212A, pH 8.0, 37°C Escherichia coli
384
-
ATP mutant W274A, pH 8.0, 37°C Escherichia coli
487
-
ATP mutant F240M, pH 8.0, 37°C Escherichia coli