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Results 1 - 5 of 5
EC Number Crystallization (Commentary) Reference
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3- 289263, 289265, 289268, 289269
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3by hanging-drop vapor diffusion method at room temperature, to 1.85 A resolution, Lys-227 is the pyridoxal-5'-phosphate binding residue near the pyridoxal-5'-phosphate nitrogen, but Asp-132 is also strictly conserved and at a similar distance from the pyridinium nitrogen, Tyr-226 donates a hydrogen bond to the phosphate of pyridoxal-5'-phosphate, Trp-256 donates a hydrogen bond to the phosphate through the indole N1-hydrogen 658027
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3crystals of recombinant kynureninase that diffracted to 2.0 A are obtained, and the atomic structure of the PLP-bound holoenzyme is determined by molecular replacement using the Pseudomonas fluorescens structure as the phasing model 685134
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3performed using the hanging-drop vapor diffusion technique 658027
Show all pathways known for 3.7.1.3Display the word mapDisplay the reaction diagram Show all sequences 3.7.1.3the wild type enzyme is cocrystallized with 3-hydroxyhippuric acid, using the modified microbatch under oil technique at 25?C, with 0.05 M MgCl2, 0.1 M Tris (pH 8.0), and 25% (w/v) PEG 3000 699466
Results 1 - 5 of 5