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Literature summary extracted from

  • Frueauf, J.B.; Ballicora, M.A.; Preiss, J.
    Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli (2001), J. Biol. Chem., 276, 46319-46325.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.27 D-fructose 1,6-bisphosphate
-
 Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.27 expression of wild-type and D142E plasmids in Escherichia coli strain BL21(DE3), expression of D142N and D142A plasmids in Escherichia coli strain AC70R1-504 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.27 D142A Km values are not significantly different in comparison to the wild-type enzyme, no significant changes for fructose 1,6-bisphosphate activation, Ki value of AMP 3fold increases in comparison to the wild-type enzyme Escherichia coli
2.7.7.27 D142E 47fold increase of Km value of glucose 1-phosphate and 11.5fold increase of Km value of ATP in comparison to the wild-type enzyme, activation by fructose 1,6-bisphosphate increases, no significant changes for AMP-inhibition in comparison to the wild-type enzyme Escherichia coli
2.7.7.27 D142N Km values are not significantly different in comparison to the wild-type enzyme, Ki value of AMP 25fold increases in comparison to the 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 0.018
-
 alpha-D-glucose 1-phosphate pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes Escherichia coli
2.7.7.27 0.26
-
 ATP pH 7.6, 37°C, wild-type enzyme, comparison of Km of wild-type and mutant enzymes 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 major regulated step in the bacterial glycogen biosynthesis pathway diphosphate + ADP-glucose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.27 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
-
 ?
2.7.7.27 ATP + alpha-D-glucose 1-phosphate major regulated step in the bacterial glycogen biosynthesis pathway Escherichia coli diphosphate + ADP-glucose
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.27 55
-
 5 min 80% remaining activity of the wild-type enzyme, 98% remaining activity of the mutant enzyme D142A, 96% remaining activity of the mutant enzyme D142E, 52% remaining activity of the mutant enzyme D142N Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.7.27 0.06
-
 AMP pH 7.6, 37°C, mutant enzyme D142E Escherichia coli
2.7.7.27 0.13
-
 AMP pH 7.6, 37°C, mutant enzyme D142A Escherichia coli
2.7.7.27 1
-
 AMP pH 7.6, 37°C, mutant enzyme D142N Escherichia coli