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Crystal structure of the Schiff base intermediate of L-Lys epsilon-oxidase from Marinomonas mediterranea with L-Lys
Structural highlights
FunctionLODA_MARM1 Has antibacterial activity against a wide spectrum of Gram-positive and Gram-negative bacteria including nosocomial isolates of S.aureus and Pseudomonas sp. The antimicrobial activity is due to hydrogen peroxide generated by its lysine oxidase activity. Also has autotoxic activity. Involved in biofilm differentiation; responsible for cell death within microcolonies during biofilm development which is linked to the generation of a phenotypically diverse dispersal population and thus may play a role in colonization.[1] [2] [3] Publication Abstract from PubMedWe have determined the x-ray crystal structure of l-lysine epsilon-oxidase from Marinomonas mediterranea in its native and l-lysine-complex forms at 1.94- and 1.99-A 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 epsilon-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. X-Ray crystallographic evidence for the presence of the cysteine tryptophylquinone cofactor in L-lysine {varepsilon}-oxidase from Marinomonas mediterranea.,Okazaki S, Nakano S, Matsui D, Akaji S, Inagaki K, Asano Y J Biochem. 2013 Sep;154(3):233-6. doi: 10.1093/jb/mvt070. Epub 2013 Aug 1. PMID:23908359[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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