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EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.14FAD - 694583, 706354, 743455
Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.14FAD dependent on 725625
Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.14FAD dependent on. Residue K300 is hydrogen-bound to the N5 atom of FAD via a H2O molecule (HOH309), the only solvent molecule present inside the catalytic site in the enzyme inhibitor complexes. In turn, K300 is the only active-site residue whose conformation changes upon FAD reduction, possibly allowing for a reorientation of the HOH309 molecule. The water molecule might thus function as a hydrogen-bond acceptor with the protonated N5 atom of reduced FAD 724968
Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.14FAD oxidized FAD is the prominent form during steady-state turnover, consistent with the reductive half-reaction being rate-limiting 672006
Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.14FAD the FAD prosthetic group is non-covalently bound to the protein and is deeply embedded within the structure. All FAD atoms are solvent-inaccessible, with the exception of the flavin C5a, N5 and C4a atoms that line the active centre 695161
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