{"created":"2025-02-26T01:35:37.134355+00:00","id":2000436,"links":{},"metadata":{"_buckets":{"deposit":"8b259da7-bdf1-4669-91aa-e2a39c0e23be"},"_deposit":{"created_by":17,"id":"2000436","owner":"17","owners":[17],"pid":{"revision_id":0,"type":"depid","value":"2000436"},"status":"published"},"_oai":{"id":"oai:kochi.repo.nii.ac.jp:02000436","sets":["103:105"]},"author_link":[],"control_number":"2000436","item_11_biblio_info_6":{"attribute_name":"bibliographic_information","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2025-02","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"1","bibliographicPageEnd":"162","bibliographicPageStart":"149","bibliographicVolumeNumber":"93","bibliographic_titles":[{"bibliographic_title":"Journal of Molecular Evolution","bibliographic_titleLang":"en"}]}]},"item_11_description_4":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Amino acid racemases catalyze the interconversion of l- and d-amino acids, maintaining intracellular levels of both d- and l-amino acids. While alanine and glutamate racemases are widespread in bacteria, serine racemase (SerR) is predominantly found in animals. Recently, homologs of animal SerR were reported in some bacterial genomes, but their evolutionary distribution\nand functional roles remain poorly understood. In this study, we cloned and expressed 20 SerR homologous genes from 13 bacterial species spanning five phyla and characterized their enzymatic activity. Six homologs exhibited serine dehydratase activity, while the remaining showed racemase activity with serine, aspartate, asparagine, or arginine. Notably,the SerR homologs from Parafannyhessea umbonata (Actinomycetota), Clostridium aceticum, Anaerovirgula multivorans,Alkaliphilus oremlandii (Bacillota), Acetomicrobium mobile, and Thermovirga lienii (Synergistota) demonstrated strong arginine racemase activity, with Km values ranging from 0.167 to 0.885 mM and kcat values ranging from 5.86 to 61.5 s−1 for l-arginine. Phylogenetic analysis revealed that bacterial and eukaryotic SerR homologs share a common ancestral gene, and substrate specificity has independently changed multiple times during evolution. Amino acid sequence alignment and analysis of site-directed mutants revealed that residues at positions 146 to 148 and surrounding regions, located near the substrate-binding site, play a crucial role in substrate specificity and/or catalytic activity. These results highlight the evolutionary processes that drive functional diversification in serine racemase homologs.","subitem_description_language":"en","subitem_description_type":"Abstract"}]},"item_11_publisher_31":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Springer","subitem_publisher_language":"en"}]},"item_11_relation_11":{"attribute_name":"item_11_relation_11","attribute_value_mlt":[{"subitem_relation_type":"isIdenticalTo","subitem_relation_type_id":{"subitem_relation_type_id_text":"https://doi.org/10.1007/s00239-024-10231-7","subitem_relation_type_select":"DOI"}}]},"item_11_rights_12":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.","subitem_rights_language":"en"}]},"item_11_source_id_7":{"attribute_name":"item_11_source_id_7","attribute_value_mlt":[{"subitem_source_identifier":"1432-1432","subitem_source_identifier_type":"EISSN"}]},"item_11_version_type_15":{"attribute_name":"出版タイプ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_access_right":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"open access","subitem_access_right_uri":"http://purl.org/coar/access_right/c_abf2"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Kouji, Uda","creatorNameLang":"en"}]},{"creatorNames":[{"creatorName":"Rie, Nishimura","creatorNameLang":"en"}]},{"creatorNames":[{"creatorName":"Yuexuan, Li","creatorNameLang":"en"}]},{"creatorNames":[{"creatorName":"Eisaku, Shimoda","creatorNameLang":"en"}]},{"creatorNames":[{"creatorName":"Tetsuya, Miyamoto","creatorNameLang":"en"}]},{"creatorNames":[{"creatorName":"Luke A. Moe","creatorNameLang":"en"}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2025-03-03"}],"filename":"Journal of Molecalar Evolution_93_1_149.pdf","filesize":[{"value":"1.3 MB"}],"format":"application/pdf","licensetype":"license_5","mimetype":"application/pdf","url":{"url":"https://kochi.repo.nii.ac.jp/record/2000436/files/Journal of Molecalar Evolution_93_1_149.pdf"},"version_id":"92dcfb81-c33d-4a57-8c84-f7da25772c76"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"D-amino acid","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Aspartate racemase","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Serine racemase","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Arginine racemase","subitem_subject_language":"en","subitem_subject_scheme":"Other"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"item_resource_type","attribute_value_mlt":[{"resourcetype":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"Evolution and Functional Diversification of Serine Racemase Homologs in Bacteria","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Evolution and Functional Diversification of Serine Racemase Homologs in Bacteria","subitem_title_language":"en"}]},"item_type_id":"11","owner":"17","path":["105"],"pubdate":{"attribute_name":"PubDate","attribute_value":"2025-03-03"},"publish_date":"2025-03-03","publish_status":"0","recid":"2000436","relation_version_is_last":true,"title":["Evolution and Functional Diversification of Serine Racemase Homologs in Bacteria"],"weko_creator_id":"17","weko_shared_id":-1},"updated":"2025-03-03T05:23:24.753654+00:00"}