X-ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in L-lysine ε-oxidase from Marinomonas mediterranea
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) previou...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2013-09, Vol.154 (3), p.233-236 |
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| container_issue | 3 |
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| container_title | Journal of biochemistry (Tokyo) |
| container_volume | 154 |
| creator | Okazaki, Seiji Nakano, Shogo Matsui, Daisuke Akaji, Shusaku Inagaki, Kenji Asano, Yasuhisa |
| description | 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. |
| doi_str_mv | 10.1093/jb/mvt070 |
| format | Article |
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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. 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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. 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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.</abstract><cop>England</cop><pmid>23908359</pmid><doi>10.1093/jb/mvt070</doi><tpages>4</tpages></addata></record> |
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| ispartof | Journal of biochemistry (Tokyo), 2013-09, Vol.154 (3), p.233-236 |
| issn | 0021-924X 1756-2651 |
| language | eng |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acid Oxidoreductases - chemistry Bacterial Proteins - chemistry Catalytic Domain Coenzymes - chemistry Crystallography, X-Ray Dipeptides - chemistry Electrons Indolequinones - chemistry Kinetics Marinomonas - chemistry Marinomonas - enzymology Models, Molecular Schiff Bases - chemistry |
| title | X-ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in L-lysine ε-oxidase from Marinomonas mediterranea |
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