{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T02:07:07Z","timestamp":1770689227259,"version":"3.49.0"},"reference-count":44,"publisher":"Portland Press Ltd.","issue":"4","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2018,2,28]]},"abstract":"<jats:p>Hydrogen sulfide (H2S) plays important roles in the pathogenesis of periodontitis. Oral pathogens typically produce H2S from l-cysteine in addition to pyruvate and . However, fn1055 from Fusobacterium nucleatum subsp. nucleatum ATCC 25586 encodes a pyridoxal 5\u2032-phosphate (PLP)-dependent enzyme that catalyzes the production of H2S and l-serine from l-cysteine and H2O, an unusual cysteine (hydroxyl) lyase reaction (\u03b2-replacement reaction). To reveal the reaction mechanism, the crystal structure of substrate-free Fn1055 was determined. Based on this structure, a model of the l-cysteine-PLP Schiff base suggested that the thiol group forms hydrogen bonds with Asp232 and Ser74, and the substrate \u03b1-carboxylate interacts with Thr73 and Gln147. Asp232 is a unique residue to Fn1055 and its substitution to asparagine (D232N) resulted in almost complete loss of \u03b2-replacement activity. The D232N structure obtained in the presence of l-cysteine contained the \u03b1-aminoacrylate-PLP Schiff base in the active site, indicating that Asp232 is essential for the addition of water to the \u03b1-aminoacrylate to produce the l-serine-PLP Schiff base. Rapid-scan stopped-flow kinetic analyses showed an accumulation of the \u03b1-aminoacrylate intermediate during the reaction cycle, suggesting that water addition mediated by Asp232 is the rate-limiting step. In contrast, mutants containing substitutions of other active-site residues (Ser74, Thr73, and Gln147) exhibited reduced \u03b2-replacement activity by more than 100-fold. Finally, based on the structural and biochemical analyses, we propose a mechanism of the cysteine (hydroxyl) lyase reaction by Fn1055. The present study leads to elucidation of the H2S-producing mechanism in F. nucleatum.<\/jats:p>","DOI":"10.1042\/bcj20170838","type":"journal-article","created":{"date-parts":[[2018,1,18]],"date-time":"2018-01-18T01:30:25Z","timestamp":1516239025000},"page":"733-748","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Structural insights into the catalytic mechanism of cysteine (hydroxyl) lyase from the hydrogen sulfide-producing oral pathogen, <i>Fusobacterium nucleatum<\/i>"],"prefix":"10.1042","volume":"475","author":[{"given":"Yuichiro","family":"Kezuka","sequence":"first","affiliation":[{"name":"Department of Structural Biology, School of Pharmacy, Iwate Medical University, Yahaba, Iwate 028-3694, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tetsuo","family":"Ishida","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Biology and Marine Science, Faculty of Science, University of the Ryukyus, Nishihara, Okinawa 903-0213, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yasuo","family":"Yoshida","sequence":"additional","affiliation":[{"name":"Department of Microbiology, School of Dentistry, Aichi Gakuin University, Nagoya, Aichi 452-8650, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Takamasa","family":"Nonaka","sequence":"additional","affiliation":[{"name":"Department of Structural Biology, School of Pharmacy, Iwate Medical University, Yahaba, Iwate 028-3694, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2018,2,16]]},"reference":[{"key":"2021112216574298200_BCJ-2017-0838C1","doi-asserted-by":"publisher","first-page":"783","DOI":"10.1902\/jop.1992.63.9.783","article-title":"Biochemical and clinical factors influencing oral malodor in periodontal patients","volume":"63","author":"Yaegaki","year":"1992","journal-title":"J. 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