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The acidic amino acid-rich C-terminal domain of VanabinX enhances reductase activity, attaining 1.3- to 1.7-fold vanadium reduction
https://oist.repo.nii.ac.jp/records/2881
https://oist.repo.nii.ac.jp/records/2881840797b0-2681-4778-81ad-632cda50df5a
名前 / ファイル | ライセンス | アクション |
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1-s2.0-S2405580822001492-main (4.4 MB)
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Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (https://creativecommons.org/licenses/by-nc-nd/4.0/)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2023-01-18 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | The acidic amino acid-rich C-terminal domain of VanabinX enhances reductase activity, attaining 1.3- to 1.7-fold vanadium reduction | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Next-generation sequencing | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Metal accumulation | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Metal transporters | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Metal binding | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Enzyme kinetics | |||||
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 | |||||
著者(英) |
Adi, Tri Kustono
× Adi, Tri Kustono× Fujie, Manabu× Satoh, Nori× Ueki, Tatsuya |
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書誌情報 |
en : Biochemistry and Biophysics Reports 巻 32, p. 101349, 発行日 2022-09-16 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | Ascidians accumulate extremely high levels of vanadium (V) in their blood cells. Several V-related proteins, including V-binding proteins (vanabins), have been isolated from V-accumulating ascidians. In this study, to obtain a deeper understanding of vanabins, we performed de novo transcriptome analysis of blood cells from a V-rich ascidian, Ascidia sydneiensis samea, and constructed a database containing 8532 predicted proteins. We found a novel vanabin with a unique acidic amino acid–rich C-terminal domain, designated VanabinX, in the database and studied it in detail. Reverse-transcription polymerase chain reaction analysis revealed that VanabinX was detected in all adult tissues examined, and was most prominent in blood cells and muscle tissue. We prepared recombinant proteins and performed immobilized metal ion affinity chromatography and a NADPH-coupled V(V)-reductase assay. VanabinX bound to metal ions, with increasing affinity for Cu(II) > Zn(II) > Co(II), but not to V(IV). VanabinX reduced V(V) to V(IV) at a rate of 0.170 μM per micoromolar protein within 30 min. The C-terminal acidic domain enhanced the reduction of V(V) by Vanabin2 to 1.3-fold and of VanabinX itself to 1.7-fold in trans mode. In summary, we constructed a protein database containing 8532 predicted proteins expressed in blood cells; among them, we discovered a novel vanabin, VanabinX, which enhances V reduction by vanabins. | |||||
出版者 | ||||||
出版者 | Elsevier B.V. | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 2405-5808 | |||||
PubMed番号 | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/36147050 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.1016/j.bbrep.2022.101349 | |||||
権利 | ||||||
権利情報 | © 2022 The Authors. | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://www.sciencedirect.com/science/article/pii/S2405580822001492?via%3Dihub | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 |