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Literature summary extracted from

  • Ito, S.; Fushinobu, S.; Jeong, J.J.; Yoshioka, I.; Koga, S.; Shoun, H.; Wakagi, T.
    Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase (2003), J. Mol. Biol., 331, 871-883.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.147 expression in Escherichia coli strain BL21(DE3) Pyrococcus furiosus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.147 enzyme in complex with AMP, sitting drop vapour diffusion method, 10 mg/ml protein in 6 mM ADP-beta-S, 30 mM glucose mixed in equal volumes with reservoir solution containing 1.6 M citrate, pH 6.5, 10 mM DTT, equilibration against 0.075 ml of reservoir solution at 25°C, a few weeks to 1 month, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement, modeling Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.147 C174S site-directed mutagenesis, activity and oligomarization state are similar to the wild-type enzyme Pyrococcus furiosus
2.7.1.147 C94S site-directed mutagenesis, activity is similar to the wild-type enzyme, the mutant enzyme forms no dimers, but monomers Pyrococcus furiosus
2.7.1.147 C94S/C174S site-directed mutagenesis, activity is similar to the wild-type enzyme, the mutant enzyme forms no dimers, but monomers Pyrococcus furiosus
2.7.1.147 D451A site-directed mutagenesis, nearly inactive mutant Pyrococcus furiosus
2.7.1.147 D451N site-directed mutagenesis, nearly inactive mutant Pyrococcus furiosus
2.7.1.147 D451S site-directed mutagenesis, nearly inactive mutant Pyrococcus furiosus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.147 AMP strong competitive inhibition Pyrococcus furiosus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.147 Mg2+ binding site structure Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.147 ADP + D-glucose Pyrococcus furiosus step of the Embden-Meyerhoff pathway AMP + D-glucose 6-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.147 Pyrococcus furiosus Q9V2Z6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.147 recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment at 90°C, ammonium sulfate fractionation, ion exchange chromatography, and gel filtration Pyrococcus furiosus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.147 ADP + D-glucose = AMP + D-glucose 6-phosphate reaction mechanism, the catalytic base Asp451 is essential Pyrococcus furiosus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.147 ADP + D-glucose step of the Embden-Meyerhoff pathway Pyrococcus furiosus AMP + D-glucose 6-phosphate
-
 ?
2.7.1.147 ADP + D-glucose substrate binding site structure, glucose-induced conformational change and domain closure in the enzyme Pyrococcus furiosus AMP + D-glucose 6-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.147 dimer
-
 Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
2.7.1.147 ADP-dependent kinase
-
 Pyrococcus furiosus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.1.147 additional information
-
-
 Pyrococcus furiosus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.147 ADP binding site structure Pyrococcus furiosus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.1.147 0.06
-
 AMP versus ADP Pyrococcus furiosus