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  1. 1100 学部・機構・専門職大学院
  2. 理工系学部
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A novel type IIb L-asparaginase from Latilactobacillus sakei LK-145 : characterization and application

http://hdl.handle.net/10112/0002003518
http://hdl.handle.net/10112/0002003518
59fa26e5-6b50-40e5-9bef-c4b325285e54
名前 / ファイル ライセンス アクション
KU-1100-20240518-01.pdf KU-1100-20240518-01.pdf (5.1 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2025-11-17
タイトル
タイトル A novel type IIb L-asparaginase from Latilactobacillus sakei LK-145 : characterization and application
言語 en
言語
言語 eng
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 加藤, 志郎

× 加藤, 志郎

WEKO 44805
e-Rad_Researcher 50547023

en Kato, Shiro

ja 加藤, 志郎

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田村, 和也

× 田村, 和也

en Tamura, Kazuya

ja 田村, 和也

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増田, 有紀

× 増田, 有紀

en Masuda, Yuki

ja 増田, 有紀

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小西, 守周

× 小西, 守周

en Konishi, Morichika

ja 小西, 守周

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山中, 一也

× 山中, 一也

WEKO 54136
e-Rad_Researcher 30756870
ORCID iD 0000-0002-6141-697X

en Yamanaka, Kazuya

ja 山中, 一也

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老川, 典夫

× 老川, 典夫

WEKO 6699
e-Rad_Researcher 80233005

en Oikawa, Tadao

ja 老川, 典夫

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概要
内容記述タイプ Abstract
内容記述 We succeeded in homogeneously expressing and purifying L-asparaginase from Latilactobacillus sakei LK-145 (Ls-Asn1) and its mutated enzymes C196S, C264S, C290S, C196S/C264S, C196S/C290S, C264S/C290S, and C196S/C264S/C290S Ls-Asn1. Enzymological studies using purified enzymes revealed that all cysteine residues of Ls-Asn1 were found to affect the catalytic activity of Ls-Asn1 to varying degrees. The mutation of Cys196 did not affect the specific activity, but the mutation of Cys264, even a single mutation, significantly decreased the specific activity. Furthermore, C264S/C290S- and C196S/C264S/C290S-Ls-Asn1 almost completely lost their activity, suggesting that C290 cooperates with C264 to influence the catalytic activity of Ls-Asn1. The detailed enzymatic properties of three single-mutated enzymes (C196S, C264S, and C290S-Ls-Asn1) were investigated for comparison with Ls-Asn1. We found that only C196S-Ls-Asn1 has almost the same enzymatic properties as that of Ls-Asn1 except for its increased stability for thermal, pH, and the metals NaCl, KCl, CaCl₂, and FeCl₂. We measured the growth inhibitory effect of Ls-Asn1 and C196S-Ls-Asn1 on Jurkat cells, a human T-cell acute lymphoblastic leukemia cell line, using L-asparaginase from Escherichia coli K-12 as a reference. Only C196S-Ls-Asn1 effectively and selectively inhibited the growth of Jurkat T-cell leukemia, which suggested that it exhibited antileukemic activity. Furthermore, based on alignment, phylogenetic tree analysis, and structural modeling, we also proposed that Ls-Asn1 is a so-called "Type IIb" novel type of asparaginase that is distinct from previously reported type I or type II asparaginases. Based on the above results, Ls-Asn1 is expected to be useful as a new leukemia therapeutic agent.
言語 en
書誌情報 en : Archives of Microbiology

巻 206, 号 6, p. 1-14, 発行日 2024-05-18
ISSN
収録物識別子タイプ EISSN
収録物識別子 0302-8933
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA00548209
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1007/s00203-024-03979-5
権利
言語 en
権利情報 This version of the article has been accepted for publication, after peer review (when applicable) and is subject to Springer Nature’s AM terms of use, but is not the Version of Record and does not reflect post-acceptance improvements, or any corrections. The Version of Record is available online at: https://doi.org/10.1007/s00203-024-03979-5.
著者版フラグ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
出版者
出版者 Springer Nature
言語 en
キーワード
言語 en
主題Scheme Other
主題 Lactic acid bacteria
キーワード
言語 en
主題Scheme Other
主題 Latilactobacillus sakei
キーワード
言語 en
主題Scheme Other
主題 L-Asparaginase
キーワード
言語 en
主題Scheme Other
主題 Leukemia drugs
キーワード
言語 ja
主題Scheme Other
主題 関西大学
キーワード
言語 en
主題Scheme Other
主題 Kansai University
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