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Results 1 - 4 of 4
EC Number Crystallization (Commentary)
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. Residues Leu14, Val15, Ala60, Leu92 and Pro97 surround the hydrophobic bicycle of the nucleotide, while the amine groups of the latter interact with Glu88. The ribose ring belonging to the substrate is bound to protein residues Asn116 and Ser117. The magnesium ion is chelated by Asp118 and Asp226, and the diphosphate group makes electrostatic interactions with residues Arg21 and Lys31, which belong to the GGXGXRLXPLX5PK diphosphorylase signature
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. The human active site is site very similar to the Leishmania donovani one. Leishmania donovani GDP-mannose diphosphorylase makes more interactions with its substrate than the human enzyme does
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13enzyme in apo form, in complex with substrates mannose-1-phosphate, or with GTP, or bound to the end product GDP-Mannose and Mg2+, sitting drop vapour diffusion method, for apoenzyme: mixing of equal volumes of 20 mg/ml protein in 10 mM Tris, pH 8.0, 150 mM NaCl with reservoir solution containing 35% v/v 2-methyl-2,4-pentanediol, 0.1 M phosphate citrate, pH 7.5, for enzyme complexes: preincubation of 12.5 or 25 mg/ml protein in 10 mM HEPES, pH 7.5, 100 mM NaCl, 10 mM MgCl2, with a 16:1 alpha-D-mannose 1-phosphate or a 8:1 GTP and GDP-Man molar excess of ligand for 30 min at room temperature, protein to well solution ratio of 3:1, the well solution containing 30-35% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 4.6, 20 mM MgCl2, or in a 2:1 ratio with weel solution containing 30% 2-methyl-2,4-pentanediol, 0.1 M sodium acetate, pH 5.0, 20 mM MgCl2, X-ray diffraction structure determination and analysis at 2.1-2.95 A resolution
Show all pathways known for 2.7.7.13Display the word mapDisplay the reaction diagram Show all sequences 2.7.7.13ligand-free enzyme, sitting drop vapor diffusion method, using 0.1 M bis-Tris pH 6.5, 25% (w/v) PEG 3350, 0.2 M lithium sulfate. Enzyme bound to GTP and D-mannose 1-phosphate, sitting drop vapor diffusion method, using 0.1 M magnesium formate, 15% (w/v) PEG 3350
Results 1 - 4 of 4