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

Seiji Okazaki, Shogo Nakano, Daisuke Matsui, Shusaku Akaji, Kenji Inagaki, Yasuhisa Asano

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

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 languageEnglish
Pages (from-to)233-236
Number of pages4
JournalJournal of biochemistry
Volume154
Issue number3
DOIs
Publication statusPublished - Sep 1 2013

Keywords

  • CTQ
  • crystal structure
  • iodide SAD
  • l-lysine
  • oxidative deamination

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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