1.4.1.3: glutamate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about glutamate dehydrogenase [NAD(P)+], go to the full flat file.
Reaction
Synonyms
At5g07440, At5g18170, dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)), dual-coenzyme specific glutamate dehydrogenase, GDH, gdh-1, GDH1, GDH2, GDH3, GdhA, gdhA_1, GDHB, GDHII, GLDH, GLUD1, GLUD2, GluDH, glutamate dehydrogenase, glutamate dehydrogenase 1, glutamate dehydrogenase 2, glutamic acid dehydrogenase, glutamic dehydrogenase, hGDH1, hGDH2, hGLUD1, hGLUD2, housekeeping glutamate dehydrogenase, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, Legdh1, Membrane protein 50, MP50, NAD(P)+-dependent glutamate dehydrogenase, NAD(P)-dependent GDH, NAD(P)-dependent glutamate dehydrogenase, NAD(P)-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, NAD(P)H-utilizing glutamate dehydrogenase, NADH-GDH, NADH-glutamate dehydrogenase, TTC1211, TTC1212, TtGDH
ECTree
1.4.1.3 glutamate dehydrogenase [NAD(P)+]Advanced search results
results (
results (Crystallization
Crystallization on EC 1.4.1.3 - glutamate dehydrogenase [NAD(P)+]
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
homology modeling of the hexameric structure of the GDH3 isoenzyme, it is highly symmetric and is formed by the assembly of two equivalent trimers with a three-fold symmetry
purified isozyme hGDH2, hGDH2 is crystallized in the absence of allosteric regulators or active site ligands, by hanging drop vapour diffusion method, mixing of 0.002 ml of 9.7 mg/ml protein solution with an equal volume of reservoir solution containing 8% PEG 8000, 15% MPD, 0.4 M NaCl and 0.1 M phosphate, pH 7.0, and equilibration against 1.0 ml of reservoir solution at 18°C, method screening and optimization, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement method and modelling using the hexameric human apo-enzyme hGDH1 structure (PDB ID 1L1F) as a search model
hanging-drop method of vapour diffusion using lithium sulfate as the precipitant. The crystals belong to the tetragonal system and are in space group P4(2)2(1)2 with unit-cell dimensions of a = b = 167.2, c = 172.9 A. Consideration of the values of Vm and possible packing of the molecules within the cell suggest that the asymmetric unit contains a trimer
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the crystal structure is determined at 2.2 A resolution and compared with the structure of glutamate dehydrogenase from the mesophile Clostridium symbiosum
hanging drop method of vapour diffusion, crystals belong to space group C2 with a hexamer in the asymmetric unit and have lattice constants a = 141.9 A, b = 197.5 A and c = 125.7 A with beta = 113.6°, the crystal structure of the extremely thermostable glutamate dehydrogenase from Thermococcus litoralis determined at 2.5 A resolution is compared to that from the hyperthermophile Pyrococcus furiosus. The less stable Thermococcus litoralis enzyme has a decreased number of ion pair interactions; modified patterns of hydrogen bonding resulting from isosteric sequence changes; substitutions that decrease packing efficiency; and substitutions which give rise to subtle but distinct shifts in both main-chain and side-chain elements of the structure
hanging-drop vapor-diffusion method at 20°C, the enzyme is crystallized in the presence of both polyethylene glycol 8000 and lithium sulfate. Four types of crystals having different morphologies appeared in the crystallization trials. One type is suitable for X-ray crystal structure analysis. The crystal belongs to the monoclinic space group P2(1) and the unit-cell parameters were a = 112.99, b = 163.70, c = 133.07 A, beta = 113.46°
the active-site cleft of unligated glutamate dehydrogenase from Thermococcus profundus studied by cryogenic X-ray crystal structure analysis and small-angle X-ray scattering
crystals up to a maximum size of 1.2 mm are grown in 3% polyethylene glycol, 120 mM ammonium acetate and 50 mM bis-tris propane (pH 6.5). The enzyme crystallizes in the trigonal space group P3121. The diffraction limit of the crystals is 3.0 A
purified recombinant untagged GDHA and GDHB in complex with each other and leucine, and GDHB in complex with glutamate, hanging drop vapor diffusion method using 0.1 M HEPES-NaOH, pH 7.0, and 0.6 M ammonium phosphate as the reservoir solution, X-ray diffraction structure determination and analysis at 2.6 A and 2.1 A resolution, respectively, molecular replacement
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