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Results 1 - 6 of 6
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EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.187FAD either FAD or FMN can be used 726951
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.187FAD required 725191
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.187FAD residues L160 ans F374 are involved in binding 728170
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.187FMN either FAD or FMN can be used 726951
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.187FMN the predicted flavin-binding site is formed by residues emanating from all three DnmZ domains and the loop connecting alpha8 and alpha9 from a neighboring chain. Numerous nonpolar amino-acid side chains form a hydrophobic pocket that can accommodate the dimethylbenzene portion of the flavin cofactor. A hydrogen-bonding network including Ser174, Ser223, Ser225 and Trp215 holds the protein surface in the correct conformation to allow hydrogenbonding interactions with the flavin isoalloxazine, including a hydrogen bond between the flavin N5 atom and Ser174. This interaction is conserved in the flavin monooxygenases and is thought to play a role in stabilizing the hydroperoxyflavin intermediate 743958
Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.187NADPH - 725191, 743958
Results 1 - 6 of 6
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