Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Meyer, C.R.; Yirsa, J.; Gott, B.; Preiss, J.
    A kinetic study of site-directed mutants of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 295 in allosteric regulation (1998), Arch. Biochem. Biophys., 352, 247-254.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.27 expression is performed using bacterial strain G6MD3 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.27 G336D a higher activity enzyme form, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme Escherichia coli
2.7.7.27 P295D extremely high activity in the absence of fructose 1,6-bisphosphate, 20fold decreased affinity for AMP than wild-type enzyme Escherichia coli
2.7.7.27 P295D/G336D the double mutant enzyme is more active in the absence of fructose 1,6-bisphosphate, with a higher affinity for fructose 1,6-bisphosphate and a lower apparent affinity for AMP than either single mutated enzyme Escherichia coli
2.7.7.27 P295E extremely high activity in the absence of fructose 1,6-bisphosphate, 10fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme Escherichia coli
2.7.7.27 P295G activity in the absence of fructose 1,6-bisphosphate is similar to wild-type enzyme Escherichia coli
2.7.7.27 P295G 3fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme Escherichia coli
2.7.7.27 P295N 3.4fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme Escherichia coli
2.7.7.27 P295Q 3.8fold decreased affinity for AMP than wild-type enzyme, higher apparent affinity for ATP than wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.27 AMP
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.27 additional information
-
 additional information kinetic parameters Escherichia coli
2.7.7.27 2.2
-
 ATP pH 7.0, 37°C, wild-type enzyme in the absence of fructose 1,6-bisphosphate, comparison of Km of wild-type and mutant enzymes in the presence and absence of fructose 1,6-bisphosphate Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.27 Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.27 ATP + alpha-D-glucose 1-phosphate Escherichia coli
-
 diphosphate + ADP-glucose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.27 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.27 wild-type and mutant enzymes, purification of wild-type and single mutant enzyme usually involves a 5 min/60°C heat treatment step, but the heat treatment step of the double mutant enzyme results in 20% loss of activity Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.27 80 100 mutant enzymes Escherichia coli
2.7.7.27 100
-
 wild-type enzyme Escherichia coli
2.7.7.27 110
-
 double mutant enzymes Escherichia coli

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.27 60
-
 purification of wild-type and single mutant enzyme usually involves a 5 min/60°C heat treatment step, the heat treatment step of the double mutant enzyme results in 20% loss of activity Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.7.27 0.04
-
 AMP pH 7.6, 37°C, wild-type enzyme Escherichia coli
2.7.7.27 0.094
-
 AMP pH 7.0, 37°C, wild-type enzyme, in the presence of a saturating concentration of fructose 1,6-bisphosphate Escherichia coli
2.7.7.27 0.3
-
 AMP pH 7.0, 37°C, mutant enzyme P295G, in the presence of a saturating concentration of fructose 1,6-bisphosphate, Escherichia coli
2.7.7.27 0.34
-
 AMP pH 7.0, 37°C, mutant enzyme P295N, in the presence of a saturating concentration of fructose 1,6-bisphosphate Escherichia coli
2.7.7.27 0.38
-
 AMP pH 7.0, 37°C, mutant enzyme P295Q, in the presence of a saturating concentration of fructose 1,6-bisphosphate Escherichia coli
2.7.7.27 0.95
-
 AMP pH 7.0, 37°C, mutant enzyme G336D, in the presence of a saturating concentration of fructose 1,6-bisphosphate Escherichia coli
2.7.7.27 0.96
-
 AMP pH 7.0, 37°C, mutant enzyme P295E, in the presence of a saturating concentration of fructose 1,6-bisphosphate Escherichia coli
2.7.7.27 2
-
 AMP pH 7.0, 37°C, mutant enzyme P295D, in the presence of a saturating concentration of fructose 1,6-bisphosphate Escherichia coli
2.7.7.27 4.95
-
 AMP pH 7.0, 37°C, double mutant enzyme P295D/G336D Escherichia coli