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Results 1 - 10 of 16 > >>
EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10- 759064
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10crystallization of human enzyme from a solution of racemic [6,7-dihydro-5H-cyclopenta[c]pyridin-7-yl(hydroxy)methylene]bis(phosphonic acid) results in a complex containing the R enantiomer in the enzyme active site. Contrary to known complexes of enzyme with risedronate, zoledronate, and minodronate, the complex with [6,7-dihydro-5H-cyclopenta[c]pyridin-7-yl(hydroxy)methylene]bis(phosphonic acid) displays only one Mg2+ ion 685599
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10crystals of mutant enzymes E97Y, T164Y, and T164W, are produced using the hanging drop vapor diffusion technique at 18°C. Proteins are co-crystallized with inhibitor 476A and substrate IPP in the presence of MgCl 758831
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10hanging drop vapor diffusion method, using 1.2 M phosphate buffer (pH 5.0), 25% (v/v) glycerol 739542
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10hanging drop vapor diffusion technique at 18°C. Crystal structures of mutant enzymes E97Y, T164W, and T164Y bound with 3-butyl-1-(2,2-diphosphonoethyl)pyridinium, isopentenyl diphosphate, and modeled farnesyl diphosphate provide strong evidence that these mutations produce the observed effects by altering the size of the binding pocket for the growing isoprenoid chain in the active site of the enzyme 758831
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10in complex with chiral risedronate analog, [6,7-dihydro-5H-cyclopenta[c]pyridin-7-yl(hydroxy)methylene]bis(phosphonic acid), i.e. NE-10501. The complex contains the R enantiomer in the enzymic active site, which is confirmed by docking studies. Presence of one Mg2+ 685599
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10in complex with isopentenyl diphosphate and inhibitors, hanging drop vapor diffusion method, using 15-25% (w/v) PEG 3350, 0.1-0.2 M calcium acetate, 0.1 M MES sodium salt pH 6.5 737349
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10in complex with Mg2+ and inhibitors, vapor diffusion method, using 100 mM sodium acetate, pH 4.6-5.2, 200 mM ammonium sulfate, and 2-10% (w/v) PEG 4K 722923
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10in complex with natural substrates and inhibitors, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M NaF, 0.1 M bis-Tris propane pH 6.5 737359
Show all pathways known for 2.5.1.10Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.10in complex with substrate isopentenyl diphosphate and five nitrogen-containing bisphosphonate inhibitors. The C1-hydroxyl and the nitrogen-containing groups of the inhibitors alter the binding of isopentenyl diphosphate and the conformation of residues Y94 and Q167. binding of the inhibitors changes the binding properties of the second site of the dimer 706667
Results 1 - 10 of 16 > >>