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EC Number Crystallization (Commentary) Reference
Show all pathways known for 4.1.2.50Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.50crystal structures of wild-type apo 6-carboxytetrahydropterin synthase and of a C27A mutant complexed with sepiapterin to 2.3 and 2.5 A resolution, respectively. The structures are highly conserved at the active site and the Zn2+ binding site. Residues Trp51 and Phe55, that are not found in mammalian 6-pyruvoyltetrahydropterin synthase keep the substrate bound by stacking it with their side chains. Replacement of these two residues by site-directed mutagenesis to the residues Met and Leu, which are only found in mammalian 6-pyruvoyltetrahydropterin synthase, converted the enzyme to the mammalian 6-pyruvoyltetrahydropterin synthase activity 726593
Show all pathways known for 4.1.2.50Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.50hanging drop vapor diffusion method, using 5% (v/v) 2-methyl-1,3-propanediol, 0.04 M CaCl2, 0.1 M sodium acetate (pH 4.5) 748175
Show all pathways known for 4.1.2.50Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.50purified recomb inant QueD, hanging-drop vapor-diffusion method, mixing of 800 nl of protein solution containing 10 mg/ml protein and of 800 nl crystallization solution containing 25% PEG 600, 100 mM NaCl and sodium citrate buffer, pH 5.5, at 18°C, X-ray diffraction structure determination and analysis at 3.6 A resolution 717029
Results 1 - 3 of 3