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The inhibition of phosphoribosyl-pyrophosphate amidotransferase activity by cordycepin monophosphate
dc.contributor.authorRottman, Fritzen_US
dc.contributor.authorGuarino, Armand J.en_US
dc.date.accessioned2006-04-13T14:46:04Z
dc.date.available2006-04-13T14:46:04Z
dc.date.issued1964-09-18en_US
dc.identifier.citationRottman, Fritz, Guarino, Armand J. (1964/09/18)."The inhibition of phosphoribosyl-pyrophosphate amidotransferase activity by cordycepin monophosphate." Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects 89(3): 465-472. <http://hdl.handle.net/2027.42/32099>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B73GF-47PGWYM-1D/2/4950a09e18da16570cb1cc2f03345598en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32099
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=14209329&dopt=citationen_US
dc.description.abstract1. 1. Cordycepin monophosphate has been shown to inhibit the activity of phosphoribosyl-pyrophosphate amidotransferase (ribosylamine-5-phosphate:phyrophosphate phosphoribosyltransferase (glutamate-amidating), EC 2.4.2.14) obtained from both pigeon liver and Bacillus subtilis.2. 2. Evidence is presented for the existence of a phosphorylated derivative of cordycepin in Bacillus subtilis cells which were grown in the presence of cordycepin.3. 3. These results, accompanied by previous evidence, suggest that the inhibition of this enzymatic reaction may be the mechanism by which cordycepin inhibits the growth of Bacillus subtilis.en_US
dc.format.extent496944 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleThe inhibition of phosphoribosyl-pyrophosphate amidotransferase activity by cordycepin monophosphateen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Mich., U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Mich., U.S.A.en_US
dc.identifier.pmid14209329en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32099/1/0000149.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0926-6569(64)90072-0en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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