{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T20:03:29Z","timestamp":1792008209186,"version":"4.4.0"},"reference-count":27,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T00:00:00Z","timestamp":1788998400000},"content-version":"am","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>We identified and characterized a homocysteine S-methyltransferase (HMT) from the lactic acid bacterium Leuconostoc suionicum LT-38, representing the first characterization of an HMT from lactic acid bacteria. The enzyme exhibited a kcat\/Km value of 15.7\u00a0mM\u22121\u00a0s\u22121 toward l-homocysteine. It showed optimal activity at 30\u00b0C and pH\u00a07.5 and remained stable over a broad range of temperatures (30\u201360\u00b0C) and pH values (5\u20139). The enzyme accepted both l- and d-homocysteine as methyl acceptors but displayed markedly higher catalytic efficiency toward the l-form (~30-fold). In contrast, l-cysteine and d-cysteine were not utilized. Both S-methyl-l-methionine and S-methyl-d-methionine were consumed in reactions containing racemic S-methyl-dl-methionine, and S-adenosyl-l-methionine was also accepted, whereas betaine and related compounds were not utilized. Gel filtration analysis indicated a monomeric structure (~32\u00a0kDa). Phylogenetic analysis showed that Ls-HMT clustered with bacterial HMT homologs and was distinct from mammalian BHMT\/BHMT2 proteins. Inductively coupled plasma\u2013mass spectrometry revealed approximately one Zn atom per enzyme molecule, and the Zn-depleted apo enzyme showed no detectable activity. These findings support that Ls-HMT is a Zn-dependent HMT with relatively high activity and expand the functional diversity of microbial HMTs.<\/jats:p>","DOI":"10.1093\/jb\/mvag064","type":"journal-article","created":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T11:52:40Z","timestamp":1788954760000},"source":"Crossref","is-referenced-by-count":1,"title":["Biochemical characterization of a homocysteine\n                    <i>S<\/i>\n                    -methyltransferase from\n                    <i>Leuconostoc suionicum<\/i>"],"prefix":"10.1093","author":[{"given":"Tadao","family":"Oikawa","sequence":"first","affiliation":[{"name":"Department of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University , 3-3-35 Yamate-Cho, Suita, Osaka-Fu 564-8680 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nanami","family":"Harada","sequence":"additional","affiliation":[{"name":"Department of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University , 3-3-35 Yamate-Cho, Suita, Osaka-Fu 564-8680 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sumire","family":"Hanafusa","sequence":"additional","affiliation":[{"name":"Department of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University , 3-3-35 Yamate-Cho, Suita, Osaka-Fu 564-8680 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuya","family":"Yamanaka","sequence":"additional","affiliation":[{"name":"Department of Life Science and Biotechnology, Faculty of Chemistry, Materials and Bioengineering, Kansai University , 3-3-35 Yamate-Cho, Suita, Osaka-Fu 564-8680 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shiro","family":"Kato","sequence":"additional","affiliation":[{"name":"Faculty of Agriculture, Kagawa University , 2393 Ikenobe, Miki, Kagawa 761-0795 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,9,10]]},"reference":[{"key":"2026092504470806300_ref1","doi-asserted-by":"crossref","first-page":"8939","DOI":"10.1074\/jbc.M710449200","article-title":"Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase","volume":"283","author":"Szegedi","year":"2008","journal-title":"J. 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