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Literature summary for 2.7.2.11 extracted from

  • Perez-Arellano, I.; Gil-Ortiz, F.; Cervera, J.; Rubio, V.
    Glutamate-5-kinase from Escherichia coli: gene cloning, overexpression, purification and crystallization of the recombinant enzyme and preliminary X-ray studies (2004), Acta Crystallogr. Sect. D, 60, 2091-2094.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
cloned in pET22 and overexpressed in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method at 21°C in the presence of ADP, MgCl2 and L-glutamate using 1.6 M MgSO4, 0.1 M KCl in 0.1 M MES pH 6.5 as crystallization solution. The tetragonal bipyramid-shaped crystals diffract to 2.5 A resolution using synchrotron radiation. The crystals belong to space group P4(1)(3)2(1)2, with unit-cell parameters a = b = 101.1, c = 178.6 A, and contain two monomers in the asymmetric unit, with 58% solvent content Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-glutamate Escherichia coli enzyme catalyzes the first step of proline biosynthesis ADP + L-glutamate 5-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamate enzyme catalyzes the first step of proline biosynthesis Escherichia coli ADP + L-glutamate 5-phosphate
-
 ?

Synonyms

Synonyms Comment Organism
G5K
-
 Escherichia coli