The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants.
Amine oxidases utilize a
flavin cofactor to catalyze the oxidation of primary amines to aldehydes. The active site base is thought to be the primary determinant of cofactor reactivity. To test this hypothesis, we have determined the crystal structures of two E. coli amine oxidase variants, E. coli amine oxidase (ECAO)