3WEV

Crystal structure of the Schiff base intermediate of L-Lys epsilon-oxidase from Marinomonas mediterranea with L-Lys

Summary for 3WEV

• Entry DOI: 10.2210/pdb3wev/pdb
• Related: 3WEU
• Descriptor: L-lysine 6-oxidase, LYSINE, SULFATE ION, ... (6 entities in total)
• Functional Keywords: amino acid oxidase, arm, beta barrel, three be-ta sheets, amine oxidase, l-lys binding, oxidoreductase
• Biological source: Marinomonas mediterranea
• Cellular location: Secreted: F2JXJ3
• Total number of polymer chains: 2
• Total formula weight: 163564.08

Authors

Okazaki, S.,Nakano, S.,Matsui, D.,Akaji, S.,Inagaki, K.,Asano, Y. (deposition date: 2013-07-12, release date: 2013-09-04, Last modification date: 2023-11-08)

Primary citation

Okazaki, S.,Nakano, S.,Matsui, D.,Akaji, S.,Inagaki, K.,Asano, Y.
X-Ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in L-lysine {varepsilon}-oxidase from Marinomonas mediterranea
J.Biochem., 154:233-236, 2013

PubMed 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.

PubMed: 23908359
DOI: 10.1093/jb/mvt070

Experimental method

X-RAY DIFFRACTION (1.98 Å)