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Literature summary extracted from

  • Perez-Arellano, I.; Carmona-Alvarez, F.; Gallego, J.; Cervera, J.
    Molecular mechanisms modulating glutamate kinase activity. Identification of the proline feedback inhibitor binding site (2010), J. Mol. Biol., 404, 890-901.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.11 D107A mutant shows 40fold increased IC50 (L-proline) Escherichia coli
2.7.2.11 D137A mutation hampers proline binding and glutamate binding, IC50 (L-proline) 142fold increased compared to wild-type Escherichia coli
2.7.2.11 E135A mutation of Glu135 and Lys145 only produce relatively small changes in proline activity, IC50 (L-proline) comparable to wild-type Escherichia coli
2.7.2.11 E143A mutant shows an 38fold augmented IC0.5 (L-proline) while kinetic parameters of glutamate and ATP are scarcely changed, IC50 (L-proline) 38fold increased compared to wild-type Escherichia coli
2.7.2.11 E143A/K145A mutant shows an enhanced affinity for L-glutamate and increased IC50 (L-proline) compared to wild-type Escherichia coli
2.7.2.11 I53A decreased kinetic parameters, IC50 (L-proline) increased 5fold compared to wild-type Escherichia coli
2.7.2.11 I69E mutation produces a very strong (170fold) decrease on proline activity with no other consequence on the kinetic parameters of the enzyme Escherichia coli
2.7.2.11 K145A mutant shows an enhanced affinity for L-glutamate and increased IC50 (L-proline) compared to wild-type Escherichia coli
2.7.2.11 additional information 2-amino-acid insertion (Val and Asn) in front of Glu143: insertion mutant exhibits a dramatic reduction in catalytic ability (the velocity at infinite concentration of substrates is 5% relative to wild-type), IC50 (L-proline) is enhanced compared to wild-type Escherichia coli
2.7.2.11 N134D mutation hampers proline binding and glutamate binding, IC50 (L-proline) 76fold increased compared to wild-type Escherichia coli
2.7.2.11 Q100A mutant shows drastically reduced catalytic rate and reduced affinity for glutamate, IC50 (L-proline) 3fold decreased compared to wild-type Escherichia coli
2.7.2.11 Q80A mutant shows drastically reduced catalytic rate and reduced affinity for glutamate, IC50 (L-proline) 3fold decreased compared to wild-type Escherichia coli
2.7.2.11 R118A mutant shows increased affinity for glutamate and reduced L-proline affinity (63fold increased IC50) Escherichia coli
2.7.2.11 R25S/E30K/I193A mutant behaves as a dimer in gel filtration experiments, kinetically indistinguishable from wild-type, IC50 (L-proline) comparable to wild-type Escherichia coli
2.7.2.11 S50A mutant exhibits a greatly reduced catalytic rate but has a small effect on apparent affinities for glutamate or ATP, IC50 (L-proline) 3fold increased compared to wild-type Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.11 L-proline
-
 Escherichia coli

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.11 ATP + L-glutamate
-
 Escherichia coli ADP + L-glutamate 5-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.2.11 dimer functional unit of the Escherichia coli enzyme is dimeric and contains an intermolecular hydrogen-bond network that interconnects the active-center cavities of the monomers and is important for substrate binding Escherichia coli
2.7.2.11 tetramer glutamte kinase crystalizes as a tetramer Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.2.11 glutamate kinase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.11 37
-
 assay at Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.2.11 0.05
-
 mutant Q100A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 0.05
-
 mutant Q80A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 0.14
-
 mutant E135A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 0.15
-
 wild-type, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 0.18
-
 mutant R25S/E30K,I193A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 0.5
-
 mutant S50A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 1.2
-
 mutant I53A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 1.3
-
 mutant K145A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 5.7
-
 mutant E143A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 6.1
-
 mutant D107A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 9.4
-
 mutant R118A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 11.5
-
 mutant N134D, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 21.4
-
 mutant D137A, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 26
-
 mutant I69E, pH not specified in the publication, 37°C Escherichia coli L-proline
2.7.2.11 96
-
 mutant E143A/K145A, pH not specified in the publication, 37°C Escherichia coli L-proline