{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,23]],"date-time":"2026-07-23T07:21:37Z","timestamp":1784791297382,"version":"3.55.0"},"reference-count":43,"publisher":"Microbiology Society","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,7,1]]},"abstract":"<jats:p><jats:italic>Fusobacterium nucleatum<\/jats:italic>produces a large amount of the toxic metabolite hydrogen sulfide in the oral cavity. Here, we report the molecular basis of<jats:italic>F. nucleatum<\/jats:italic>H<jats:sub>2<\/jats:sub>S production, which is associated with two different enzymes: the previously reported Cdl (Fn1220) and the newly identified Lcd (Fn0625). SDS-PAGE analysis with activity staining revealed that crude enzyme extracts from<jats:italic>F. nucleatum<\/jats:italic>ATCC 25586 contained three major H<jats:sub>2<\/jats:sub>S-producing proteins. Two of the proteins with low molecular masses migrated similarly to purified Fn0625 and Fn1220. Their kinetic values suggested that Fn0625 had a lower enzymic capacity to produce H<jats:sub>2<\/jats:sub>S from<jats:sc>l<\/jats:sc>-cysteine (\u223c30\u200a%) than Fn1220. The Fn0625 protein degraded a variety of substrates containing<jats:italic>\u03b2<\/jats:italic>C\u2013S linkages to produce ammonia, pyruvate and sulfur-containing products. Unlike Fn0625, Fn1220 produced neither pyruvate nor ammonia from<jats:sc>l<\/jats:sc>-cysteine. Reversed-phase HPLC separation and mass spectrometry showed that incubation of<jats:sc>l<\/jats:sc>-cysteine with Fn1220 produced H<jats:sub>2<\/jats:sub>S and an uncommon amino acid, lanthionine, which is a natural constituent of the peptidoglycans of<jats:italic>F. nucleatum<\/jats:italic>ATCC 25586. In contrast, most of the sulfur-containing substrates tested, except<jats:sc>l<\/jats:sc>-cysteine, were not used by Fn1220. Real-time PCR analysis demonstrated that the<jats:italic>fn1220<\/jats:italic>gene showed several-fold higher expression than<jats:italic>fn0625<\/jats:italic>and housekeeping genes in exponential-phase cultures of<jats:italic>F. nucleatum<\/jats:italic>. Thus, we conclude that Fn0625 and Fn1220 produce H<jats:sub>2<\/jats:sub>S in distinct manners: Fn0625 carries out<jats:italic>\u03b2<\/jats:italic>-elimination of<jats:sc>l<\/jats:sc>-cysteine to produce H<jats:sub>2<\/jats:sub>S, pyruvate and ammonia, whereas Fn1220 catalyses the<jats:italic>\u03b2<\/jats:italic>-replacement of<jats:sc>l<\/jats:sc>-cysteine to produce H<jats:sub>2<\/jats:sub>S and lanthionine, the latter of which may be used for peptidoglycan formation in<jats:italic>F. nucleatum<\/jats:italic>.<\/jats:p>","DOI":"10.1099\/mic.0.039180-0","type":"journal-article","created":{"date-parts":[[2010,4,23]],"date-time":"2010-04-23T00:46:40Z","timestamp":1271983600000},"page":"2260-2269","source":"Crossref","is-referenced-by-count":46,"title":["Production of hydrogen sulfide by two enzymes associated with biosynthesis of homocysteine and lanthionine in Fusobacterium nucleatum subsp. nucleatum ATCC 25586"],"prefix":"10.1099","volume":"156","author":[{"given":"Yasuo","family":"Yoshida","sequence":"first","affiliation":[{"name":"Department of Pathogenesis and Control of Oral Disease, Iwate Medical University School of Dentistry, Morioka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuntaro","family":"Ito","sequence":"additional","affiliation":[{"name":"Department of Conservative Dentistry and Oral Rehabilitation, Iwate Medical University School of Dentistry, Morioka, Japan"},{"name":"Department of Pathogenesis and Control of Oral Disease, Iwate Medical University School of Dentistry, Morioka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masaharu","family":"Kamo","sequence":"additional","affiliation":[{"name":"Department of Oral Biology, Iwate Medical University School of Dentistry, Morioka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuichiro","family":"Kezuka","sequence":"additional","affiliation":[{"name":"Department of Structural Biology, Iwate Medical University School of Pharmacy, Yahaba, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haruki","family":"Tamura","sequence":"additional","affiliation":[{"name":"Department of Pathogenesis and Control of Oral Disease, Iwate Medical University School of Dentistry, Morioka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazushi","family":"Kunimatsu","sequence":"additional","affiliation":[{"name":"Department of Conservative Dentistry and Oral Rehabilitation, Iwate Medical University School of Dentistry, Morioka, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hirohisa","family":"Kato","sequence":"additional","affiliation":[{"name":"Department of Pathogenesis and Control of Oral Disease, Iwate Medical University School of 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