{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,11]],"date-time":"2026-08-11T10:34:32Z","timestamp":1786444472971,"version":"build-2736575974"},"reference-count":52,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2017,2,10]],"date-time":"2017-02-10T00:00:00Z","timestamp":1486684800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["15K07997"],"award-info":[{"award-number":["15K07997"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2017,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Cystathionine \u03b2\u2010synthase (CBS) catalyzes the formation of <jats:sc>l<\/jats:sc>\u2010cystathionine from <jats:sc>l<\/jats:sc>\u2010serine and <jats:sc>l<\/jats:sc>\u2010homocysteine. The resulting <jats:sc>l<\/jats:sc>\u2010cystathionine is decomposed into <jats:sc>l<\/jats:sc>\u2010cysteine, ammonia, and \u03b1\u2010ketobutylic acid by cystathionine \u03b3\u2010lyase (CGL). This reverse transsulfuration pathway, which is catalyzed by both enzymes, mainly occurs in eukaryotic cells. The eukaryotic CBS and CGL have recently been recognized as major physiological enzymes for the generation of hydrogen sulfide (H<jats:sub>2<\/jats:sub>S). In some bacteria, including the plant\u2010derived lactic acid bacterium <jats:italic>Lactobacillus plantarum<\/jats:italic>, the CBS\u2010 and CGL\u2010encoding genes form a cluster in their genomes. Inactivation of these enzymes has been reported to suppress H<jats:sub>2<\/jats:sub>S production in bacteria; interestingly, it has been shown that H<jats:sub>2<\/jats:sub>S suppression increases their susceptibility to various antibiotics. In the present study, we characterized the enzymatic properties of the <jats:italic>L. plantarum<\/jats:italic> CBS, whose amino acid sequence displays a similarity with those of <jats:italic>O<\/jats:italic>\u2010acetyl\u2010<jats:sc>l<\/jats:sc>\u2010serine sulfhydrylase (OASS) that catalyzes the generation of <jats:sc>l<\/jats:sc>\u2010cysteine from <jats:italic>O<\/jats:italic>\u2010acetyl\u2010<jats:sc>l<\/jats:sc>\u2010serine (<jats:sc>l<\/jats:sc>\u2010OAS) and H<jats:sub>2<\/jats:sub>S. The <jats:italic>L. plantarum<\/jats:italic> CBS shows <jats:sc>l<\/jats:sc>\u2010OAS\u2010 and <jats:sc>l<\/jats:sc>\u2010cysteine\u2010dependent CBS activities together with OASS activity. Especially, it catalyzes the formation of H<jats:sub>2<\/jats:sub>S in the presence of <jats:sc>l<\/jats:sc>\u2010cysteine and <jats:sc>l<\/jats:sc>\u2010homocysteine, together with the formation of <jats:sc>l<\/jats:sc>\u2010cystathionine. The high affinity toward <jats:sc>l<\/jats:sc>\u2010cysteine as a first substrate and tendency to use <jats:sc>l<\/jats:sc>\u2010homocysteine as a second substrate might be associated with its enzymatic ability to generate H<jats:sub>2<\/jats:sub>S. Crystallographic and mutational analyses of CBS indicate that the Ala70 and Glu223 residues at the substrate binding pocket are important for the H<jats:sub>2<\/jats:sub>S\u2010generating activity.<\/jats:p>","DOI":"10.1002\/pro.3123","type":"journal-article","created":{"date-parts":[[2017,1,27]],"date-time":"2017-01-27T08:52:28Z","timestamp":1485507148000},"page":"763-783","source":"Crossref","is-referenced-by-count":28,"title":["Crystallographic and mutational analyses of cystathionine \u03b2\u2010synthase in the H<sub>2<\/sub>S\u2010synthetic gene cluster in <i>Lactobacillus plantarum<\/i>"],"prefix":"10.1002","volume":"26","author":[{"given":"Yasuyuki","family":"Matoba","sequence":"first","affiliation":[{"name":"Graduate School of Biomedical and Health Sciences, Hiroshima University Kasumi 1\u20102\u20103 Minami\u2010ku Hiroshima 734\u20108551 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