Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.3.2.2: glutamate-cysteine ligase

This is an abbreviated version!
For detailed information about glutamate-cysteine ligase, go to the full flat file.

Word Map on EC 6.3.2.2

Reaction

ATP
+
L-glutamate
 +
L-cysteine
=
ADP
 +
phosphate
 +
gamma-L-glutamyl-L-cysteine

Synonyms

Ace-GCL, Asuc_1947, AtGCL, bifunctional glutathione synthetase, bifunctional GSH synthetase, bifunctional L-glutathione synthetase, gamma -GCS, gamma-ECL, Gamma-ECS, gamma-GC, gamma-GCS, gamma-GCS-GS, gamma-glutamate-cysteine ligase-glutathione synthetase, gamma-glutamate-cysteine ligase/glutathione synthetase, gamma-glutaminylcysteine synthetase, gamma-glutamycysteine synthetase, gamma-glutamyl-cysteine ligase, gamma-Glutamyl-L-cysteine synthetase, gamma-glutamylcysteine ligase, gamma-glutamylcysteine synthase, gamma-Glutamylcysteine synthetase, gamma-glutamylcysteine synthetase-glutathione synthetase, gamma-Glutamylcysteinyl-synthetase, gammaGCS, GCL, GCLC, Gclc-X2, GCLM, GCS, GCSGS, ghF, GLCL, GLCLC, GLCLR, glutamate cysteine ligase, glutamate cysteine ligase gene, glutamate-cysteine ligase, glutamate-cysteine-ligase, glutamate–cysteine ligase, glutathione biosynthesis bifunctional protein GshAB, GSH1, GshA, gshAB, GshF, GshFAp, GshFAs, GSHI, I79_022778, L-glutamate L-cysteine ligase, More, PAD2, PhGshA II, PSHAa0937, StGCL-GS, Synthetase, gamma-glutamylcysteine

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.2 glutamate-cysteine ligase

Crystallization

Crystallization on EC 6.3.2.2 - glutamate-cysteine ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure at 2.1 A resolution
22.6 mg/ml purified enzyme, wild-type or mutant, hanging drop vapour diffusion method, equal volume of protein and reservoir solution, reservoir solution: 3.9 M sodium formate, pH 7.4, equilibration with reservoir solution at 293K, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
sitting-drop vapor diffusion method, crystal structure of unliganded enzyme and enzyme complexed with a sulfoximine-based transition-state analog inhibitor at resolutions of 2.5 and 2.1 A, respectively. In the crystal structure of the complex, the bound inhibitor is phosphorylated at the sulfoximido nitrogen and is coordinated to three Mg2+ ions
-
homology model of the catalytic subunit of human glutamate cysteine ligase. Examination of the model suggests that post-translational modifications of cysteine residues may be involved in the regulation of enzymatic activity
-
structure of the GCL-glutathione complex to 2.5 A resolution indicates that the inhibitor occupies both the glutamate- and the presumed cysteine-binding site and disrupts the previously observed Mg2+-coordination in the ATP-binding site. The structure of the complex with mechanism-based inhibitor L-buthionine-S-sulfoximine to 2.2 A resolution confirms that L-buthionine-S-sulfoximine is phosphorylated on the sulfoximine nitrogen to generate the inhibitory species and reveals contacts that likely contribute to transition state stabilization
structures of glutamate cysteine ligase in the presence of glutamate and MgCl2, to 2.1 A resolution, and in complex with glutamate, MgCl2, and ADP to 2.7 A resolution. Structures reveal an unusual binding pocket for the alpha-carboxylate of the glutamate substrate and an ATP-independent Mg2+ coordination site, clarifying the Mg2+-dependence of the enzymatic reaction