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Results 1 - 10 of 26 > >>
EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD - 287670, 656321, 684447, 686044, 687754, 689918, 710711, 710910, 710964, 712958, 713589, 725869, 742238, 742709, 742798, 742934, 743585, 743637, 743737, 763714
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD 1 mol of FAD per mol of protein 287646
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD both as a covalently or noncovalently bound cofactor 697915
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD combined quantum mechanical and molecular mechanical simulations of one- and two-electron reduction potentials of flavin cofactor 688610
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD covalently bound in His-tagged recombinant enzyme 287668, 287674
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD covalently linked 697914
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD covalently linked to His69 in a second enzyme form 287676
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD dependent on 710959
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD dependent on, the enzyme contains a Rossmann fold (xh)2GxGxxGx(xxh)2(x) FAD binding site, where x is any amino acid and h an hydrophobic one, between V44 and E70 in the N-terminal region. CgChoA belongs to the non-covalent FAD-dependent enzymes belonging to the class I family. Residues N503 and Y464 are required for stabilization of the reduced form cofactor-enzyme binding 742195
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6FAD distortion of flavin geometry is linked to ligand binding in cholesterol oxidase 689910
Results 1 - 10 of 26 > >>