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Snake venom NAD glycohydrolases: primary structures, genomic location, and gene structure
https://oist.repo.nii.ac.jp/records/987
https://oist.repo.nii.ac.jp/records/987e2001cc1-7272-43e3-b956-b2909b70d106
名前 / ファイル | ライセンス | アクション |
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Creative Commons
Attribution 4.0 International (https://creativecommons.org/licenses/by/4.0/) |
Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2019-07-04 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Snake venom NAD glycohydrolases: primary structures, genomic location, and gene structure | |||||
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 | |||||
著者(英) |
Koludarov, Ivan
× Koludarov, Ivan× Aird, Steven D. |
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書誌情報 |
en : PeerJ 巻 7, p. e6154, 発行日 2019-02-06 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | NAD glycohydrolase (EC 3.2.2.5) (NADase) sequences have been identified in 10 elapid and crotalid venom gland transcriptomes, eight of which are complete. These sequences show very high homology, but elapid and crotalid sequences also display consistent differences. As in Aplysia kurodai ADP-ribosyl cyclase and vertebrate CD38 genes, snake venom NADase genes comprise eight exons; however, in the Protobothrops mucrosquamatus genome, the sixth exon is sometimes not transcribed, yielding a shortened NADase mRNA that encodes all six disulfide bonds, but an active site that lacks the catalytic glutamate residue. The function of this shortened protein, if expressed, is unknown. While many vertebrate CD38s are multifunctional, liberating both ADP-ribose and small quantities of cyclic ADP-ribose (cADPR), snake venom CD38 homologs are dedicated NADases. They possess the invariant TLEDTL sequence (residues 144-149) that bounds the active site and the catalytic residue, Glu228. In addition, they possess a disulfide bond (Cys121-Cys202) that specifically prevents ADP-ribosyl cyclase activity in combination with Ile224, in lieu of phenylalanine, which is requisite for ADPR cyclases. In concert with venom phosphodiesterase and 5'-nucleotidase and their ecto-enzyme homologs in prey tissues, snake venom NADases comprise part of an envenomation strategy to liberate purine nucleosides, and particularly adenosine, in the prey, promoting prey immobilization via hypotension and paralysis. | |||||
出版者 | ||||||
出版者 | PeerJ | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 2167-8359 | |||||
PubMed番号 | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/30755823 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.7717/peerj.6154 | |||||
権利 | ||||||
権利情報 | © 2019 Koludarov and Aird. | |||||
情報源 | ||||||
関連名称 | https://creativecommons.org/licenses/by/4.0/ | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://peerj.com/articles/6154/ | |||||
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 |