{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,28]],"date-time":"2026-02-28T09:11:45Z","timestamp":1772269905131,"version":"3.50.1"},"reference-count":38,"publisher":"PeerJ","license":[{"start":{"date-parts":[[2019,2,6]],"date-time":"2019-02-06T00:00:00Z","timestamp":1549411200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004199","name":"Okinawa Institute of Science and Technology","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100004199","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>\n                    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\n                    <jats:italic>Aplysia kurodai<\/jats:italic>\n                    ADP-ribosyl cyclase and vertebrate CD38 genes, snake venom NADase genes comprise eight exons; however, in the\n                    <jats:italic>Protobothrops mucrosquamatus<\/jats:italic>\n                    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\u2013149) that bounds the active site and the catalytic residue, Glu228. In addition, they possess a disulfide bond (Cys121\u2013Cys202) 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\u2032-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.\n                  <\/jats:p>","DOI":"10.7717\/peerj.6154","type":"journal-article","created":{"date-parts":[[2019,2,6]],"date-time":"2019-02-06T04:09:38Z","timestamp":1549426178000},"page":"e6154","source":"Crossref","is-referenced-by-count":5,"title":["Snake venom NAD glycohydrolases: primary structures, genomic location, and gene structure"],"prefix":"10.7717","volume":"7","author":[{"given":"Ivan","family":"Koludarov","sequence":"first","affiliation":[{"name":"Ecology and Evolution Unit, Okinawa Institute of Science and Technology, Onna, Kunigami-gun, Okinawa, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Steven D.","family":"Aird","sequence":"additional","affiliation":[{"name":"Ecology and Evolution Unit and Division of Faculty Affairs, Okinawa Institute of Science and Technology, Onna, Kunigami-gun, Okinawa, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"4443","published-online":{"date-parts":[[2019,2,6]]},"reference":[{"key":"10.7717\/peerj.6154\/ref-1","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1016\/S0041-0101(01)00232-X","article-title":"Ophidian envenomation strategies and the role of purines","volume":"40","author":"Aird","year":"2002","journal-title":"Toxicon"},{"key":"10.7717\/peerj.6154\/ref-2","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1201\/9781420008661.ch20","article-title":"The role of purine and pyrimidine nucleosides in snake venoms","volume-title":"Handbook of venoms and toxins of 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