{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,4,5]],"date-time":"2023-04-05T10:15:31Z","timestamp":1680689731920},"reference-count":0,"publisher":"Walter de Gruyter GmbH","issue":"9-10","license":[{"start":{"date-parts":[[1985,8,1]],"date-time":"1985-08-01T00:00:00Z","timestamp":491702400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1985,8,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p> Under conditions where 2\u2032-deoxycoformycin is enzymatically phosphorylated by wheat shoot phosphotransferase to the 5\u2032-phosphate in 15 - 20% yield, coformycin is a relatively poor substrate, and is phosphorylated only to the extent of \u2264 5%. However, chemical phosphorylation of coformycin by modifications of the Yoshikawa procedure led to isolation of coformycin-5\u2032-phosphate in 20% overall yield.<\/jats:p>\n               <jats:p>Coformycin-5\u2032-phosphate was characterized by various criteria, including <jats:sup>1<\/jats:sup>H NMR spectroscopy. Comparison of the spectrum with that of the parent nucleoside indicated that the nucleotide is predominantly, although not exclusively, in the conformation anti about the glycosidic bond.<\/jats:p>\n               <jats:p>Like 2\u2032-deoxycoformycin-5\u2032-phosphate, coformycin-5\u2032-phosphate was a feeble substrate of snake venom 5\u2032-nucleotidase, and is hydrolyzed, quantitatively, at only 2% the rate for 5\u2032-AMP. With 5\u2032-AMP analogues as substrate, the 5\u2032-phosphates of both coformycin and deoxycoformycin were poor inhibitors of the enzyme, with K<jats:sub>i<\/jats:sub> values &gt; 0.3 m\u1d0d.<\/jats:p>\n               <jats:p>The 5\u2032-phosphates of both coformycin and deoxycoformycin do not significantly inhibit adenosine deaminase (K<jats:sub>i<\/jats:sub> &gt; 0.2 m\u1d0d), but are potent inhibitors of adenylate deaminase {K<jats:sub>i<\/jats:sub> \u2264 10<jats:sup>\u22129<\/jats:sup> \u1d0d). Neither coformycin nor deoxycoformycin are inhibitors of mammalian purine nucleoside phosphorylase.<\/jats:p>\n               <jats:p>The stabilities of coformycin, deoxycoformycin, and their 5\u2032-phosphates, have been examined as a function of pH, and nature of the buffer medium. In particular, all exhibit instability in acid and neutral media, but are relatively stable in the vicinity of pH 9. Some biological aspects of the overall results are presented. <\/jats:p>","DOI":"10.1515\/znc-1985-9-1022","type":"journal-article","created":{"date-parts":[[2018,8,2]],"date-time":"2018-08-02T17:47:31Z","timestamp":1533232051000},"page":"710-714","source":"Crossref","is-referenced-by-count":7,"title":["Phosphorylation of Coformycin and 2\u2032 -Deoxycoformycin, and Substrate and Inhibitor Properties of the Nucleosides and Nucleotides in Several Enzyme Systems"],"prefix":"10.1515","volume":"40","author":[{"given":"Agnieszka","family":"Bzowska","sequence":"first","affiliation":[{"name":"Department of Biophysics, Institute of Experimental Physics, University of Warsaw, 02-089 Warszawa, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Piotr","family":"Lassota","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Biophysics, Academy of Sciences, 02-532 Warszawa, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"Shugara","sequence":"additional","affiliation":[{"name":"Department of Biophysics, Institute of Experimental Physics, University of Warsaw, 02-089 Warszawa, Poland"},{"name":"Institute of Biochemistry and Biophysics, Academy of Sciences, 02-532 Warszawa, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"374","published-online":{"date-parts":[[2014,6,2]]},"container-title":["Zeitschrift f\u00fcr Naturforschung C"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.degruyter.com\/view\/j\/znc.1985.40.issue-9-10\/znc-1985-9-1022\/znc-1985-9-1022.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/znc-1985-9-1022\/xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/znc-1985-9-1022\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,6,22]],"date-time":"2021-06-22T21:35:43Z","timestamp":1624397743000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.degruyter.com\/document\/doi\/10.1515\/znc-1985-9-1022\/html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1985,8,1]]},"references-count":0,"journal-issue":{"issue":"9-10","published-online":{"date-parts":[[2014,6,2]]},"published-print":{"date-parts":[[1985,8,1]]}},"alternative-id":["10.1515\/znc-1985-9-1022"],"URL":"https:\/\/doi.org\/10.1515\/znc-1985-9-1022","relation":{},"ISSN":["1865-7125","0939-5075"],"issn-type":[{"value":"1865-7125","type":"electronic"},{"value":"0939-5075","type":"print"}],"subject":[],"published":{"date-parts":[[1985,8,1]]}}}