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EC Number Crystallization (Commentary) Reference
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1- 347696, 347707, 347712
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1atomistic simulations study. The diffusion of camphor along the pathway near the substrate recognition site is thermodynamically preferred. The diffusion near the substrate recognition site is triggered by a transition from a heterogeneous collection of closed ligand-bound conformers to the basin comprising the open conformations of cytochrome P450cam. The accompanying conformational change includesthe retraction of the F and G helices and the disorder of the B' helix 746482
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1camphor-free or camphor-bound P450cam mutant C334A in the absence of substrate and at high and low K+ concentration, protein in 50 mM Tris, pH 7.4, with or without 2-4 mM camphor, mixed with crystallization solution containing 50 mM Tris, pH 7.4, and 12-22% PEG 8000 with and without 200 mM K+, sitting drop vapour diffusion method, 6°C, X-ray diffraction structure determination and analysis at 1.50-1.79 A resolution 711234
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1docking simulations for binding of 3-chloroindole, the wild-type does not accommodate 3-chloroindole in the active site, whereas all the mutants do. The mutants did not differ significantly in the Fe-N, Fe-C-2 or Fe-C-3 distances for 3-chloroindole 744434
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1double electron-electron resonance studies. The geometry of the complex is nearly identical for the open and closed states of P450cam. Putaredoxin makes a single distinct interaction with its binding site on the enzyme and triggers the conformational change through very subtle structural interactions 744368
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1fusion of putidaredoxin reductase PdR to the carboxy-terminus of camphor monooxygenase CYP101A1 (P450cam) via a linker peptide and reconstitution of camphor hydroxylase activity with free putidaredoxin gives a functional system with comparable in vivo camphor oxidation activity as the native system. In vitro, the fused system’s steady state NADH oxidation rate is 2fold faster than that of the native system. In contrast to the native system, NADH oxidation rates for the fusion enzyme show nonhyperbolic dependence on putidaredoxin concentration 744637
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1mutant F87W/Y96F/V247L in complex with 1,3,5-trichlorobenzene or (+)-alpha-pinene 657898
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1mutant Y96F/F87W/V247L, binding of substrate (+)-alpha-pinene in two orientations related by rotation of the molecule 658971
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1Pseudomonas putida PpG786, cytochrome m 347692
Show all pathways known for 1.14.15.1Display the word mapDisplay the reaction diagram Show all sequences 1.14.15.1Pseudomonas sp., ternary complex 347696
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