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1.4.1.4: glutamate dehydrogenase (NADP+)

This is an abbreviated version!
For detailed information about glutamate dehydrogenase (NADP+), go to the full flat file.

Word Map on EC 1.4.1.4

Reaction

L-glutamate
+
H2O
 +
NADP+
=
2-oxoglutarate
 +
NH3
 +
NADPH
 +
H+

Synonyms

APE1386, BpNADPGDH I, BpNADPGDH II, dehydrogenase, glutamate (nicotinamide adenine dinucleotide phosphate), EcGDH, GDH, GDH1, Gdh1p, GDH2, GDH3, Gdh3p, GDH4, GdhA, GDHB, GDHC, GDHI, GDHI', GDHII, GDHP, GluDH, glutamate dehydrogenase, glutamate dehydrogenase 1, glutamate dehydrogenase 2, glutamate dehydrogenase 3, glutamic acid dehydrogenase, glutamic dehydrogenase, GW612_14215, H-form specific BpNADPGDH II, hGDH, hyphal-form specific BpNADPGDH II, L-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, NADP(+)-dependent glutamate dehydrogenase, NADP(H)-dependent glutamate dehydrogenase, NADP(H)-GDH, NADP(H)-specific glutamate dehydrogenase, NADP+ - dependant-glutamate dehydrogenase, NADP+-dependent GDH, NADP+-dependent glutamate dehydrogenase, NADP+-Gdh, NADP-dependent GDH, NADP-dependent GluDH, NADP-dependent glutamate dehydrogenase, NADP-dependent glutamate dehydrogenase 1, NADP-dependent glutamate dehydrogenase 2, NADP-GDH, NADP-GDH 1, NADP-GDH 2, NADP-glutamate dehydrogenase, NADP-linked glutamate dehydrogenase, NADP-specific glutamate dehydrogenase, NADP-specific L-glutamate dehydrogenase, NADP-ylGdh1p, NADPH-dependent GDH, NADPH-dependent glutamate dehydrogenase, OsGDH4, Pcal_1606, RocG, TrGDH, Y-form specific BpNADPGDH I, YALI0F17820g, yeast-form specific BpNADPGDH I, ylGDH1

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.4 glutamate dehydrogenase (NADP+)

Crystallization

Crystallization on EC 1.4.1.4 - glutamate dehydrogenase (NADP+)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol (PEG) 400 as the precipitant
-
to 2.9 A resolution, space group R32, with unit-cell parameters a = b = 173.8, c = 241.5 A, alpha = beta = 90°, gamma = 120°. The crystals exhibit a high solvent content (83.0%) with only one molecule in the asymmetric unit
-
structures of Gdh3 and its complex with 2-oxoglutarate and NADPH. Gdh3 exists as a hexamer, with each subunit containing two domains. The substrate and coenzyme bind in the cleft between the two domains and their binding induces a conformational change
complexed with NADP+ and 2-iminoglutarate. Among six subunits of hexameric GDH-binding NADP+, only four subunits bind 2-iminoglutarate in a closed form, while the other two are in an open form. In the closed form, 2-iminoglutarate is bound to the substrate-binding site with the 2-imino group stacked by the nicotinamide ring of the coenzyme, suggesting a prehydride transfer state
in complex with NADPH and 2-oxoglutarate. The enzyme functions as a hexamer, and each monomer comprises a Rossmann-fold cofactor-binding domain and a substrate-binding domain. In the apo-form, GDH exists as an open state, and upon binding of the substrate and cofactor the protein undergoes a conformation change to a closed state
chimeric protein consisting of domain I from NAD+-dependent GDH of Clostridium symbiosum, residues 1-200, domain II from NADP+-dependent GDH of Escherichia coli, residues 201-404 and the C-terminal helix again from Clostridium symbiosum, residues 405-448 which re-enters domain I. Domain II maintains its structural and functional integrity independent of the hinge and domain I. The enzyme is fully functional and retains the preference for NADP+ cofactor from the parent E. coli domain II
purified GDH in the absence of reactants, hanging drop vapour diffusion method, mixing of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.6, with 15-25% PEG 3350, Tris/HEPES, pH 70-8.0, and 0.2 M NaCl, 18°C, 2 days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modelling
three non-isomorphous crystal forms, all belong to orthorhombic system, homohexamers, one grown from ammonium sulfate, two from L-glutamate, 3.0 A resolution
-
plate-like crystals of monoclinic space group C2 grown by vapour-diffusion using the sitting-drop method, X-ray crystallography to a resolution of 2.7 A
-
purified recombinant detagged GDH2, 0.0025 ml of 16 mg/ml protein in 100 mM Tris, 500 mM NaCl, pH 7.8, mixed with 0.0025 ml of reservoir solution containing 0.2 M magnesium chloride hexahydrate, 0.1 M Tris/HCl pH 8.5, 30% PEG 4000 including 0.01 M spermine tetra HCl droplet concentration and 10 mM glutamate, X-ray diffraction structure determination and analysis at 3.1 A resolution
dialysis against ammonium sulfate solution
-
hanging-drop method of vapour diffusion using an ammonium sulfate and PEG mixture as the precipitant. The crystals belong to the monoclinic system and are in space group C2 with unit-cell dimensions a = 142.7, b = 202.0, c = 125.8 A with beta = 113.1 degrees with a hexamer in the asymmetric unit
cofactor binding domain of glutamate dehydrogenase, sitting-drop vapor diffusion method. X-ray structure of the domain of wild-type enzyme and mutant enzyme R190A/E231A/K193A is solved at 1.43 A
-
quadruple mutant S128R/T158E/N117R/S160E, homohexamer, 2.9 A resolution
-