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EC Number Subunits Commentary Reference
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26monomer - 737771
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26monomer 1 * 13500, SDS-PAGE 641240
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26monomer 1 * 28000, SDS-PAGE 641241
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26monomer 1 * 30000, SDS-PAGE 641245
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26monomer 1 * 35500, SDS-PAGE 641249
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26monomer 1 * 36000, SDS-PAGE -, 641253
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26monomer 1 * 40000, SDS-PAGE 641248
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26monomer x * 16600, recombinant truncated C-terminal RF kinase domain, SDS-PAGE 739570
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26More prokaryotic FAD synthetases (FADSs) are bifunctional enzymes composed of two modules, the C-terminal module with RFK activity, and the N-terminus with FMNAT activity 737771
Show all pathways known for 2.7.1.26Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.26More structure-function analysis, apo-HsRFK structural model 759167
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