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3.5.1.2: glutaminase

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

Word Map on EC 3.5.1.2

Reaction

L-glutamine
+
H2O
=
L-glutamate
 +
NH3

Synonyms

AnsB, AoGls, GA, GAB, GAC, GahB, GLA, GLNase, GLS, GLS1, GLS2, GlsA, glutaminase, glutaminase 1, glutaminase 2, glutaminase A, glutaminase B, glutaminase C, glutaminase I, glutaminase K, glutaminase L, glutaminase-1, glutaminase-2, glutaminase-B, glutamine amidohydrolase, glutamine aminohydrolase, glutamine deamidating enzyme, K-glutaminase, KAG, KGA, kidney-type glutaminase, kidney-type-glutaminase, L-glutaminase, L-glutamine amidohydrolase, LAG, LGA, liver-type glitaminase, liver-type glutaminase, Mglu, Micrococcus glutaminase Mglu, Micrococcus luteus K-3-type glutaminase, mitochondrial glutaminase, N-PAG, neuroblastoma glutaminase, neuroblastoma PAG, Nit 2, nitrilase 2, omega-amidase, PAG, PDX2, phosphate activated glutaminase, phosphate-activated glutaminase, phosphate-activated L-glutamine amidohydrolase, salt-tolerant glutaminase, YaaE

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.2 glutaminase

Crystallization

Crystallization on EC 3.5.1.2 - glutaminase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
handing-drop vapor diffusion technique, at 18ºC
-
purified recombinant mature C-terminally His6-tagged wild-type enzyme, hanging drop vapor diffusion method, mixing 0.005 ml of 34 mg/ml protein in 20 mM NaHEPES, pH 7.0, with 0.005 ml of reservoir solution containing 1.2 M ammonium dihydrogen phosphate, and 0.1 M sodium citrate, pH 5.6, crystallization of wild-type pro-enzyme by sitting drop vapour diffusion, mixing 0.002 ml of 20 mg/ml pro-enzyme in 20 mM NaHEPES, pH 6.5, with 0.002 ml of reservoir solution containing 0.2 M ammonium citrate, pH 5.1, and 20% w/v PEG-3350, crystallization of mutant A47Q-1 by hanging drop vapour diffusion method, by mixing of 0.005 ml of 20 mg/ml protein in 20 mM ammonium tartrate, pH 6.7, with 0.005 ml of reservoir solution containing 0.2 M ammonium tartrate, pH 6.7, and 20% PEG 3350, and of mutant A47Q-2 by mixing 0.005 ml of 20 mg/ml protein in 20 mM sodium phosphate, pH 6.0, with 0.005 ml reservoir solution containing 0.2 M sodium tartrate, pH 8.6, and 20% w/v PEG 3350, 20°C, X-ray diffraction structure determination and analysis at 1.5-1.75 A resolution
-
molecular modeling of structure and docking with the substrate and potential inhibitors
catalytic domain of isoform KGA in complex with 6-diazo-5-oxo-L-norleucine, hanging drop vapor diffusion method, using 0.1 M Bis-Tris propane (pH 7.2) and 1.8 M LiSO4
phosphate- and L-glutamate-bound GAC, X-ray diffraction structure determination and analysis at 2.85 A and 2.80 A resolution, respectively
-
purified recombinant GAC free and in complex with inhibitor bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide, hanging drop vapor diffusion, mixing of protein in 25 mM HEPES (pH 7.5), 200 mM NaCl, 5% glycerol, and 5 mM beta-ME, with reservoir solution containing 0.3 M magnesium chloride, 0.1 M Tris, pH 8.5, and 12% w/v PEG 4000, X-ray diffraction structure determination and analysis at 2.55 and 2.3 A resolution, respectively
C-terminally truncated enzyme, hanging-drop, vapor-diffusion method at 25°C, X-ray diffraction structure determination and analysis at 2.4 resolution using multiple-wavelength anomalous dispersion, MAD
-
determination of the structures of the intact enzyme in the presence and in the absence of its product L-glutamate and its activator Tris, which activates the enzyme by 6fold, and in the presence of both
enzyme and its fragment containing about 80% of the protein, handing-drop vapour-diffusion method
-
by addition of ammonium sulfate