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  1. 理工学
  2. 学術論文

Evolution and Functional Diversification of Serine Racemase Homologs in Bacteria

http://hdl.handle.net/10126/0002000436
http://hdl.handle.net/10126/0002000436
e8acf3f6-5248-4802-b396-f3ab190490ed
名前 / ファイル ライセンス アクション
Journal Journal of Molecalar Evolution_93_1_149.pdf (1.3 MB)
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Item type 学術雑誌論文 / Journal Article(1)
公開日 2025-03-03
タイトル
タイトル Evolution and Functional Diversification of Serine Racemase Homologs in Bacteria
言語 en
言語
言語 eng
キーワード
言語 en
主題Scheme Other
主題 D-amino acid
キーワード
言語 en
主題Scheme Other
主題 Aspartate racemase
キーワード
言語 en
主題Scheme Other
主題 Serine racemase
キーワード
言語 en
主題Scheme Other
主題 Arginine racemase
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
著者 Kouji, Uda

× Kouji, Uda

en Kouji, Uda

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Rie, Nishimura

× Rie, Nishimura

en Rie, Nishimura

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Yuexuan, Li

× Yuexuan, Li

en Yuexuan, Li

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Eisaku, Shimoda

× Eisaku, Shimoda

en Eisaku, Shimoda

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Tetsuya, Miyamoto

× Tetsuya, Miyamoto

en Tetsuya, Miyamoto

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Luke A. Moe

× Luke A. Moe

en Luke A. Moe

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抄録
内容記述タイプ Abstract
内容記述 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
and 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.
言語 en
bibliographic_information en : Journal of Molecular Evolution

巻 93, 号 1, p. 149-162, 発行日 2025-02
item_11_source_id_7
収録物識別子タイプ EISSN
収録物識別子 1432-1432
item_11_relation_11
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 https://doi.org/10.1007/s00239-024-10231-7
権利
言語 en
権利情報 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/.
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
出版者
出版者 Springer
言語 en
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