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Results 1 - 6 of 6
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.12apo enzyme, diffraction of third crystals at 2 A resolution at -174°C, crystals belong to space group P2(1) with unit-cell parameters a = 60.56 A, b = 106.40 A, c =82.78 A, beta = 96.50°, technique: 1 microlitre of 10 mg/ml protein solution to 1 microlitre reservoir solution (38% pentaerytritol propoxylate (5/4 PO/OH) and 200 mM KCl pH 9) one week at 4°C, generation of first crystals by hanging-drop vapour diffusion (Index HT screening kit), generation of second crystals by microseeding: reservoir solution contained crushed first crystals, generation of third crystals by Repeated Seeding Technique: reservoir solution contained crushed second crystals
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.12crystal structures at up to 2.1 A resolution of NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866. Crystals of the selenomethionyl free enzyme of human NMPRTase (F132M I151M double mutant) are grown with the sitting drop vapor diffusion method at 22°C. Crystals of wild-type human NMPRTase in complex with NMN are obtained at 22°C by sitting drop vapor diffusion
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.12crystal structures at up to 2.1 A resolution of NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866. Crystals of wild-type murine NMPRTase free enzyme are obtained by sitting drop vapor diffusion at 4°C
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.12crystal structures of the enzyme in the free form and bound to nicotinamide and 5-phospho-alpha-D-ribose 1-diphosphate at the resolution of 2.0 A to 2.2 A are essentially identical to that of the complex with nicotinamide mononucleotide, except for some variations that can facilitate the substitution reaction by fixing the nucleophile and the leaving group for the requisite inversion of configuration at the C1’-carbon of the ribose ring. In the active site near the C1’-atom of the bound 5-phospho-alpha-D-ribose 1-diphosphate or nicotinamide mononucleotide, there is neither negatively charged group nor waterproof environment necessary to support the feasibility of a ribo-oxocarbocation intermediate inherent in the SN1 mechanism
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.12crystallization of recombinant human NMPRTase in the free form, sitting-drop vapour-diffusion method, hanging-drop vapour-diffusion method, crystal quality is improved by successive use of the microseeding technique. The resultant crystals diffract to 2.0 A resolution. These crystals belongs to space group P2(1), with unit-cell parameters a = 60.56, b = 106.40, c = 82.78 A
Display the word mapDisplay the reaction diagram Show all sequences 2.4.2.12hanging drop vapor diffusion method, crystallization of apoenzyme and complex with either nicotinamide mononucleotide or the NAmPRTase inhibitor FK-866
Results 1 - 6 of 6