X-Ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in l-lysine ε-oxidase from Marinomonas mediterranea

摘要: We have determined the x-ray crystal structure of L-lysine e-oxidase from Marinomonas mediterranea in its native and L-lysine-complex forms at 1.94- 1.99-A resolution, respectively. In enzyme, electron densities clearly indicate presence cysteine tryptophylquinone (CTQ) previously identified quinohemoprotein amine dehydrogenase. L-lysine-complex, an density corresponding to bound shows that e-amino group is attached C6 carbonyl CTQ, suggesting formation a Schiff-base intermediate. Collectively, present provides first example enzyme employing cofactor oxidase.