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Literature summary for 2.7.7.27 extracted from

  • Figueroa, C.M.; Esper, M.C.; Bertolo, A.; Demonte, A.M.; Aleanzi, M.; Iglesias, A.A.; Ballicora, M.A.
    Understanding the allosteric trigger for the fructose-1,6-bisphosphate regulation of the ADP-glucose pyrophosphorylase from Escherichia coli (2011), Biochimie, 93, 1816-1823.
    View publication on PubMed
Search for more literature for 2.7.7.27

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modeling of enzyme. Binding of ATP correlates with conformational changes of a loop facing the ATP substrate, going from an open to a closed substrate-bound form Escherichia coli

Protein Variants

Protein Variants Comment Organism
W113A mutation does not change apparent affinities for the substrates, but mutant becomes insensitive to activation by fructose-1,6-bisphosphate. The mutant enzymes still binds fructose-1,6-bisphosphate, with similar affinity as the wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
 alpha-D-glucose 1-phosphate wild-type, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.21
-
 alpha-D-glucose 1-phosphate wild-type, pH 8.0, 37°C Escherichia coli
0.32
-
 ATP wild-type, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.33
-
 alpha-D-glucose 1-phosphate mutant W113A, pH 8.0, 37°C Escherichia coli
0.41
-
 alpha-D-glucose 1-phosphate mutant Q74A, pH 8.0, 37°C Escherichia coli
0.41
-
 alpha-D-glucose 1-phosphate mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
0.47
-
 alpha-D-glucose 1-phosphate mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
2.5
-
 ATP mutant W113A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
5.8
-
 ATP mutant W113A, pH 8.0, 37°C Escherichia coli
7.6
-
 ATP mutant Q74A, pH 8.0, 37°C Escherichia coli
9.8
-
 ATP mutant Q74A, presence of 2 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
11
-
 ATP wild-type, pH 8.0, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.61
-
 mutant W113A, presence of 0.5 mM AMP plus 2.5 mM fructose 1,6-bisphosphate , pH 8.0, 37°C Escherichia coli
0.63
-
 mutant W113A, presence of 0.5 mM AMP, pH 8.0, 37°C Escherichia coli
0.72
-
 wild-type, presence of 0.5 mM AMP, pH 8.0, 37°C Escherichia coli
0.82
-
 mutant Q74A, presence of 0.5 mM AMP plus 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
1.05
-
 mutant Q74A, presence of 0.5 mM AMP, pH 8.0, 37°C Escherichia coli
1.08
-
 wild-type, pH 8.0, 37°C Escherichia coli
1.12
-
 mutant W113A, presence of 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
1.45
-
 mutant W113A, pH 8.0, 37°C Escherichia coli
1.6
-
 mutant Q74A, presence of 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
1.93
-
 mutant Q74A, pH 8.0, 37°C Escherichia coli
3.6
-
 wild-type, presence of 0.5 mM AMP plus 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C Escherichia coli
47.6
-
 wild-type, presence of 2.5 mM fructose 1,6-bisphosphate, pH 8.0, 37°C 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
-
 ?
additional information enzyme displays a regulatory mechanism where the interaction with the allosteric activator triggers conformational changes at the level of loops containing residues Trp113 and Gln74 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
ADP-Glc PPase
-
 Escherichia coli