EC Number |
Cofactor |
Reference |
---|
1.5.3.1 | cytochrome |
- |
392390 |
1.5.3.1 | FAD |
- |
671702, 675389, 764037, 764208 |
1.5.3.1 | FAD |
1 mol of covalently bound and 1 mol of noncovalently bound FAD per mol of enzyme |
392391 |
1.5.3.1 | FAD |
binds both FAD and FMN. Residue Phe 339 is the cofactor binding site |
765378 |
1.5.3.1 | FAD |
contains 1 mol of noncovalently bound Flavin and 1 mol of covalently bound flavin per mole of enzyme |
764119 |
1.5.3.1 | FAD |
covalent and non-covalent |
687443 |
1.5.3.1 | FAD |
covalent flavin is 8alpha-(s-cysteinyl)FAD attached to Cys315 |
392395 |
1.5.3.1 | FAD |
covalently bound |
685194, 685219, 685282 |
1.5.3.1 | FAD |
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 |
1.5.3.1 | FAD |
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 |