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Results 1 - 10 of 35 > >>
EC Number Cofactor Commentary Reference
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1cytochrome - 392390
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD - 671702, 675389, 764037, 764208
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD 1 mol of covalently bound and 1 mol of noncovalently bound FAD per mol of enzyme 392391
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD binds both FAD and FMN. Residue Phe 339 is the cofactor binding site 765378
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD contains 1 mol of noncovalently bound Flavin and 1 mol of covalently bound flavin per mole of enzyme 764119
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD covalent and non-covalent 687443
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD covalent flavin is 8alpha-(s-cysteinyl)FAD attached to Cys315 392395
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD covalently bound 685194, 685219, 685282
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD covalently bound to wild-type. Production of soluble apoenzyme lacking FAD by controlled expression in Escherichia coli. Reconstitution of enzyme by incubation with FAD. Autoflavinylation occurs in a reaction that proceeds via reduced flavin intermediate and requires only apoenzyme and FAD 672027
Show all pathways known for 1.5.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.5.3.1FAD flavoenzyme. The simulation method of Markovian milestoning molecular dynamics simulations is used to compute the entry and exit kinetics of O2 in the enzyme. The rate of flavin oxidation by O2 is likely not strongly limited by diffusion from the solvent to the active site. The predicted faster entry and slower exit of O2 for the bound state indicate a longer residence time within the enzyme, increasing the likelihood of collisions with the flavin isoalloxazine ring, a step required for reduction of molecular O2 and subsequent reoxidation of the flavin 742971
Results 1 - 10 of 35 > >>