Abstract
We have determined the x-ray crystal structure of l-lysine ε-oxidase from Marinomonas mediterranea in its native and l-lysine-complex forms at 1.94- and 1.99-Å resolution, respectively. In the native enzyme, electron densities clearly indicate the presence of cysteine tryptophylquinone (CTQ) previously identified in quinohemoprotein amine dehydrogenase. In the l-lysine-complex, an electron density corresponding to the bound l-lysine shows that its ε-amino group is attached to the C6 carbonyl group of CTQ, suggesting the formation of a Schiff-base intermediate. Collectively, the present crystal structure provides the first example of an enzyme employing a tryptophylquinone cofactor in an amine oxidase.
Original language | English |
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Pages (from-to) | 233-236 |
Number of pages | 4 |
Journal | Journal of biochemistry |
Volume | 154 |
Issue number | 3 |
DOIs | |
Publication status | Published - Sep 2013 |
Keywords
- CTQ
- crystal structure
- iodide SAD
- l-lysine
- oxidative deamination
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology