{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,31]],"date-time":"2026-07-31T15:10:18Z","timestamp":1785510618669,"version":"3.56.0"},"reference-count":23,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"name":"KOSE Cosmetology Research Foundation","award":["818"],"award-info":[{"award-number":["818"]}]},{"DOI":"10.13039\/100007802","name":"Institute for Fermentation, Osaka","doi-asserted-by":"publisher","award":["G-2024-3-010"],"award-info":[{"award-number":["G-2024-3-010"]}],"id":[{"id":"10.13039\/100007802","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,1,7]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The demand for\u00a0d-amino acids is increasing as their unique physiological role continues to be elucidated. meso-Diaminopimelate dehydrogenase catalyzes the reversible NADP+-dependent oxidative deamination of meso-diaminopimelate to produce l-2-amino-6-oxopimelate. Moreover, a few enzymes show a broad range of reductive amination activity toward 2-oxo acids, synthesizing d-amino acids. Here, we report the identification and characterization of a novel NADP+-dependent meso-diaminopimelate dehydrogenase from Candidatus Syntrophocurvum alkaliphilum (CSaDAPDH). The purified enzyme exhibited oxidative deamination activity toward meso-diaminopimelate, as well as reductive amination activity toward several 2-oxo acids to produce the corresponding d-amino acids. The optimum pH and temperature for oxidative deamination of meso-diaminopimelate were 9.0 and 45\u00b0C, respectively. The optimum pH for reductive amination of pyruvate was 6.5, which was the lowest optimum pH among known enzymes, and thus, may lead to the development of new enzymatic methods for d-amino acid production. CSaDAPDH retained more than 60% of its activity after incubation for 30 min at 50 \u00b0C (pH 7.0) or at pHs ranging from 5.5 to 7.0 (50\u00b0C). Moreover, using known enzymes as comparisons, the coenzyme and substrate recognition mechanisms of CSaDAPDH were elucidated based on a multiple sequence alignment and the homology model.<\/jats:p>","DOI":"10.1093\/femsle\/fnag083","type":"journal-article","created":{"date-parts":[[2026,7,18]],"date-time":"2026-07-18T11:39:39Z","timestamp":1784374779000},"source":"Crossref","is-referenced-by-count":0,"title":["A novel NADP+-dependent\n                    <i>meso<\/i>\n                    -diaminopimelate dehydrogenase from Candidatus\n                    <i>Syntrophocurvum alkaliphilum<\/i>\n                    : a promising biocatalyst for\n                    <scp>d<\/scp>\n                    -amino acid production"],"prefix":"10.1093","volume":"373","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1395-8643","authenticated-orcid":false,"given":"Hironaga","family":"Akita","sequence":"first","affiliation":[{"name":"College of Industrial Technology, Nihon University, Narashino 275\u20138575 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryo","family":"Hasegawa","sequence":"additional","affiliation":[{"name":"College of Industrial Technology, Nihon University, Narashino 275\u20138575 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomoe","family":"Komoriya","sequence":"additional","affiliation":[{"name":"College of Industrial Technology, Nihon University, Narashino 275\u20138575 ,","place":["Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,7,20]]},"reference":[{"key":"2026073110365664900_bib1","doi-asserted-by":"publisher","first-page":"1760","DOI":"10.3389\/fmicb.2018.01760","article-title":"Artificial thermostable d -amino acid dehydrogenase: creation and application","volume":"9","author":"Akita","year":"2018","journal-title":"Front 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