2.7.2.11: glutamate 5-kinase

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For detailed information about glutamate 5-kinase, go to the full flat file.

Reaction

Synonyms

ATP-L-glutamate 5-phosphotransferase, ATP:gamma-L-glutamate phosphotransferase, G5K, gamma-GK, gamma-glutamate kinase, gamma-glutamyl kinase, gamma-glutamylphosphate kinase, GK, GKA, glutamate kinase, glutamate-5-kinase, GPK, kinase (phosphorylating), glutamate, kinase, glutamate (phosphorylating), PRO1, proB, scGK

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.2 Phosphotransferases with a carboxy group as acceptor

                2.7.2.11 glutamate 5-kinase

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Results	in table
6	Activating Compound
34385	AA Sequence
6	Application
1	CAS Registry Number
16	Cloned(Commentary)
2	Cofactor
2	Crystallization (Commentary)
11	General Information
40	IC50 Value
53	Inhibitors
2	kcat/KM [mM/s]
15	Ki Value [mM]
20	KM Value [mM]
1	Localization
12	Metals/Ions
12	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
38	Organism
12	Pathway
52	PDB ID
6	pH Optimum
2	pH Range
1	pH Stability
61	Protein Variants
15	Purification (Commentary)
1	Reaction
1	Reaction Type
34	Reference
8	Source Tissue
11	Specific Activity [micromol/min/mg]
2	Storage Stability
51	Substrates and Products (Substrate)
11	Subunits
34	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
2	Temperature Stability [°C]
2	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.2.11 - glutamate 5-kinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

-

660594

in about 4-5 months, using the hanging drop vapour diffusion method, complexed with glutamate and sulfate, or with L-glutamate 5-phosphate, sulfate and 5-oxoproline, at 2.9 A and 2.5 A resolution, belongs to the space groups P41212 or P21, respectively. Dimer of dimers architecture, each subunit contains a 257 residue AAK domain, typical of acylphosphate-forming enzymes, with characteristic alpha3beta8alpha4 sandwich topology, each subunit contains a 93 residue C-terminal PUA domain, typical of RNA-modifying enzymes, which presents the characteristic beta5beta4 sandwich fold and three alpha helices

Escherichia coli

P0A7B5

681421