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Literature summary for 2.7.7.27 extracted from

  • Hill, B.L.; Wong, J.; May, B.M.; Huerta, F.B.; Manley, T.E.; Sullivan, P.R.; Olsen, K.W.; Ballicora, M.A.
    Conserved residues of the Pro103-Arg115 loop are involved in triggering the allosteric response of the Escherichia coli ADP-glucose pyrophosphorylase (2015), Protein Sci., 24, 714-728.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
P103A mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate Escherichia coli
Q106A mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate Escherichia coli
R107A mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate Escherichia coli
R115A mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate Escherichia coli
W113A mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate Escherichia coli
Y114A mutation in loop Pro103-Arg115, mutant protein displays altered kinetic profiles, primarily a lack of response to fructose-1,6-bisphosphate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.023
-
alpha-D-glucose 1-phosphate wild-type, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.12
-
alpha-D-glucose 1-phosphate mutant Q106A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.12
-
alpha-D-glucose 1-phosphate mutant R107A, S0.5 value, Hill coefficient 1.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.143
-
alpha-D-glucose 1-phosphate mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.17
-
alpha-D-glucose 1-phosphate mutant P103A, S0.5 value, Hill coefficient 1.4, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.17
-
ATP wild-type, S0.5 value, Hill coefficient 2.0, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.22
-
alpha-D-glucose 1-phosphate mutant P103A, S0.5 value, Hill coefficient 1.1, pH 8.0, 37°C Escherichia coli
0.25
-
alpha-D-glucose 1-phosphate mutant Q106A, S0.5 value, Hill coefficient 1.6, pH 8.0, 37°C Escherichia coli
0.26
-
alpha-D-glucose 1-phosphate mutant R107A, S0.5 value, Hill coefficient 0.9, pH 8.0, 37°C Escherichia coli
0.27
-
alpha-D-glucose 1-phosphate mutant Y114A, S0.5 value, Hill coefficient 0.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.28
-
alpha-D-glucose 1-phosphate mutant R115A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C Escherichia coli
0.34
-
alpha-D-glucose 1-phosphate mutant W113A, S0.5 value, Hill coefficient 1.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.37
-
alpha-D-glucose 1-phosphate wild-type, S0.5 value, Hill coefficient 1.5, pH 8.0, 37°C Escherichia coli
0.43
-
alpha-D-glucose 1-phosphate mutant Y114A, S0.5 value, Hill coefficient 0.3, pH 8.0, 37°C Escherichia coli
0.46
-
alpha-D-glucose 1-phosphate mutant W113A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C Escherichia coli
0.81
-
ATP mutant P103A, S0.5 value, Hill coefficient 1.5, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.89
-
ATP mutant P103A, S0.5 value, Hill coefficient 1.9, pH 8.0, 37°C Escherichia coli
1.3
-
ATP mutant R115A, S0.5 value, Hill coefficient 1.7, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
1.63
-
ATP mutant R107A, S0.5 value, Hill coefficient 2.3, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
2.3
-
ATP mutant Y114A, S0.5 value, Hill coefficient 1.9, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
2.5
-
ATP mutant Q106A, S0.5 value, Hill coefficient 1.7, pH 8.0, 37°C Escherichia coli
2.5
-
ATP mutant R107A, S0.5 value, Hill coefficient 2.1, pH 8.0, 37°C Escherichia coli
2.5
-
ATP mutant Y114A, S0.5 value, Hill coefficient 2.0, pH 8.0, 37°C Escherichia coli
2.5
-
ATP wild-type, S0.5 value, Hill coefficient 2.4, pH 8.0, 37°C Escherichia coli
3
-
ATP mutant R115A, S0.5 value, Hill coefficient 2.1, pH 8.0, 37°C Escherichia coli
3.1
-
ATP mutant W113A, S0.5 value, Hill coefficient 1.1, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
3.5
-
ATP mutant W113A, S0.5 value, Hill coefficient 1.2, pH 8.0, 37°C Escherichia coli
4.4
-
ATP mutant Q106A, S0.5 value, Hill coefficient 1.2, presence of 1.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More a Pro103-Arg115 loop is part of an activation path. It has strongly correlated movements with regions of the enzyme associated with regulation and ATP binding, and the optimal network pathways linking ATP and the activator binding Lys39 mainly involve residues of this loop. The loop is a distinct insertional element present only in allosterically regulated sugar nucleotide diphosphorylases Escherichia coli