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2.3.2.2: gamma-glutamyltransferase

This is an abbreviated version!
For detailed information about gamma-glutamyltransferase, go to the full flat file.

Word Map on EC 2.3.2.2

Reaction

a (5-L-glutamyl)-peptide
+
an amino acid
=
a peptide
 +
a 5-L-glutamyl amino acid

Synonyms

(5-L-glutamyl) peptide: amino-acid 5-glutamyl transferase, alpha-glutamyl transpeptidase, AngammaGT, AsGGT1, At1g69820, At4g29210, At4g39640, At4g39650, BaGGT, BaGGT42, BaGGT469, BlGGT, BlGGT13, BsGGT168, Cgl0954, eqGGT, gamma glutamyl transferase, gamma-glutamyl peptidyltransferase, gamma-glutamyl transferase, gamma-glutamyl transferase 1, gamma-glutamyl transferase 5, gamma-glutamyl transferase/transpeptidase, gamma-glutamyl transferases, gamma-glutamyl transpeptidase, gamma-glutamyl transpeptidase 1, gamma-glutamyl transpeptidase 4, gamma-glutamyl transpeptidase-1, gamma-glutamyl-transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-GPT, gamma-GT, gamma-GTase, gamma-GTP, gammaGT, GGT, GGT A, GGT I, GGT-1, GGT1, GGT2, GGT3, GGT4, GGT5, ggtB, GGTII protein, GGTLA1, glutamyl transpeptidase, glutamyltransferase, gamma-, HGGT, L-gamma-glutamyl transpeptidase, L-gamma-glutamyltransferase, L-glutamyltransferase, More, PnGGT, SBLGGT, VvGGT3

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.2 gamma-glutamyltransferase

Crystallization

Crystallization on EC 2.3.2.2 - gamma-glutamyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with L-glutamate, hanging drop vapor diffusion method, using poly(ethylene glycol) 4000, 100 mM MES buffer (pH 7.0), 600 mM NaCl, and 5% (v/v) Jeffamine M-600
ammonium sulfate precipitation from 20 mM Tris-HCl, pH 8.0, 14.2 mg/ml protein, refrigerator, 1 week
-
ammonium sulfate precipitation, hanging-drop vapor diffusion method, crystal structure of gamma-glutamyltransferase at 1.95 A resolution and structure of the gamma-glutamyl-enzyme intermediate trapped by flash cooling the GGT crystal soaked in glutathione solution and the structure of GGT in complex with L-glutamate
ammonium sulfate precipitation, hanging-drop vapor diffusion method, crystal structure of the T391A mutant gamma-glutamyltranspeptidase that lacks autocatalytic processing ability refined at 2.55 A resolution
in complex with azaserine and acivicin, at 1.65 A resolution. Both inhibitors bind to the substrate-binding pocketand form a covalent bond with the Ogamma atom of residue T391. The two amido nitrogen atoms of Gly483 and Gly484, which form the oxyanion hole, interact with the inhibitors directly or via a water molecule. In the azaserine complex the carbon atom that forms a covalent bond with Thr391 is sp3-hybridized
purified recombinant deglycosylated hGGT1 mutant V272A with bound inhibitor DON, mixing of 0.002 ml of 4.3 mg/ml protein in 50 mM HEPES, pH 8.0, 0.5 mM EDTA, 0.02% sodium azide, and 2 mM DON, with 0.0017 ml of H2O, and 0.002 ml of reservoir solution containing 20-25% PEG 3350, 0.1 M Na-cacodylate, pH 6.0, and 0.1 M ammonium chloride, microseeding with apo-hGGT1 crystals, room temperature, 1-2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, modeling using the apo-form crystals of hGGT1 (PDB ID 4Z9O) as template
ammonium sulfate precipitation, refrigerator, 2 weeks
-
purified recombinant wild-type PnGGT enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml of 3-5 mg/ml protein in 0.1 M HEPES, pH 7.0, with 0.001 ml reservoir solution containing 16% PEG 8000, 15% PEG 400, 0.1 M HEPES, pH 7.0, 50 mM glycylglycine, and equilibration against 0.5 ml of reservoir solution, 20°C, 1 week, method optimization, X-ray diffraction structure determination and analysis at 1.57-1.70 A resolution, molecular replacement method using the structure of Escherichia coli GGT (EcGGT, PDB ID 2DG5) as the template, modeling