<unk>  is very similar in amino acid sequence to xanthine oxidase (XO). The active sites of<unk>  has been found to have a superimposed structure to that of XO, in studies involving mouse liver.<unk>  is a homodimer, and requires FAD, molybdenum (MoCo) and two 2Fe-2S clusters as cofactors. These two 2Fe-2S cofactors each bind to the two distinct 150-kDa monomers of<unk> . Three separate domains harbor these three requirements. There is a 20 kDa N-terminal which binds to the two 2Fe-2S cofactors, a 40 kDa domain which provides a means of binding to the FAD, and a C-terminal which houses the molybdenum.
Aldehyde oxidase
Xanthine oxidase
Aldehyde dehydrogenase
Transaminase
Biotinidase
Amidase
Flavin-containing monooxygenase 3
Glutamate dehydrogenase