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6.3.2.3: glutathione synthase

This is an abbreviated version!
For detailed information about glutathione synthase, go to the full flat file.

Word Map on EC 6.3.2.3

Reaction

ATP
+
gamma-L-glutamyl-L-cysteine
 +
glycine
=
ADP
 +
phosphate
 +
glutathione

Synonyms

Asuc_1947, bifunctional glutathione synthetase, bifunctional GSH synthetase, bifunctional L-glutathione synthetase, gamma -glutamate-cysteine ligase-glutathione synthetase, gamma-GCS, gamma-GCS-GS, gamma-glutamate-cysteine ligase/glutathione synthetase, gamma-glutamylcysteine synthetase-glutathione synthetase, GCL, GCSGS, ghF, glutamate cysteine ligase, glutathione biosynthesis bifunctional protein GshAB, Glutathione synthase, Glutathione synthetase, Glutathione synthetase (tripeptide), GS, GSH synthase, GSH synthetase, GSH-S, GSH2, gshAB, GSHase, gshB, GshF, GshFAp, GshFAs, GSHII, GSHS, GSHS1, GSS, hGS, L-glutathione synthetase, More, Phytochelatin synthetase, StGCL-GS, Synthetase, glutathione, TAGS1, TaGS2, TbGS, ZmGS

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.3 glutathione synthase

Crystallization

Crystallization on EC 6.3.2.3 - glutathione synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.0 A resolution
-
mutant enzymes replaced with Val at the basal position of the flexible loop (P227V, G240V, and P227V/G240V) are identical with wild-type enzyme in their crystal structures, except the loop region
-
structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 A resolution
the crystal structure of the loopless mutant, in which the loop is replaced by 3 Gly residues, is identical with that of the wild-type enzyme
-
under optimal catalytic condition pH 7.5
-
analysis of the dimeric enzyme, PDB ID 2HGS
computational structure modeling of wild-type and mutant enzymes using crystal structure data at 2.1 A resolution, interactions of actie site residues Glu144, Asn146, Lys305, and Lys364, and ligands ADP2-, SO42-, and Mg2+
purified recombinant enzyme, 20 mg/ml protein by hanging-drop method, from reservoir solution containing containing 10% w/v PEG 20K, 5% v/v tacsimate and 0.1 M HEPES, pH 7.5, 2-5 days, X-ray diffraction structure determination and analysis at 3.5 A resolution. Better crystals by vapor diffusion experiments to the without-oil microbatch method, method development, mixing of 40 mg/ml protein with an equal volume of solution containing 14% w/v PEG 20000, 0.2 M HEPES pH 7.5, 10% v/v tacsimate, X-ray diffraction structure determination and analysis at 2.34 A resolution, molecular replacement
-
crystallization by vapour-diffusion hanging-drop method of the free enzyme or the enzyme liganded to substrate gamma-glutamylcysteine and non-hydrolyzable ATP-substrate-analogue AMP-PNP, 17 mg/ml enzyme in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM DTT, plus equal volume of reservoir solution: for crystals of free enzyme with 1.97 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400 at 22°C, or for the liganded enzyme with 3 mM AMP-PNP, 10 mM MgCl2, 3 mM gamma-glutamylcysteine against a well solution of 2.2 M ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, 2% PEG 400, 5 mM TCEP, 40 mM MgCl2, at 22°C, X-ray diffraction structure determination and analysis at 2.3 A and 1.8 A, respectively
structure modeling
-
hanging drop vapour diffusion method
-