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dc.contributor.authorTalanian, Robert Vincent
dc.contributor.authorBrown, Neal C.
dc.contributor.authorMcKenna, Charles E.
dc.contributor.authorYe, Ting Gao
dc.contributor.authorLevy, Jeffrey N.
dc.contributor.authorWright, George E.
dc.date2022-08-11T08:08:49.000
dc.date.accessioned2022-08-23T16:09:19Z
dc.date.available2022-08-23T16:09:19Z
dc.date.issued1989-10-17
dc.date.submitted2009-01-13
dc.identifier.citation<p>Biochemistry. 1989 Oct 17;28(21):8270-4.</p>
dc.identifier.issn0006-2960 (Print)
dc.identifier.doi10.1021/bi00447a002
dc.identifier.pmid2557899
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32663
dc.description.abstractTwenty-three pyrophosphate analogues were screened as inhibitors of proliferating cell nuclear antigen independent DNA polymerase delta (pol delta) derived from calf thymus. Carbonyldiphosphonate (COMDP), also known as alpha-oxomethylenediphosphonate, inhibited pol delta with a potency (Ki = 1.8 microM) 20 times greater than that displayed for DNA polymerase alpha (pol alpha) derived from the same tissue. Characterization of the mechanism of inhibition of pol delta indicated that COMDP competed with the dNTP specified by the template and was not competitive with the template-primer. In the case of pol alpha, COMDP did not compete with either the dNTP or the polynucleotide substrate. COMDP inhibited the 3'----5' exonuclease activity of pol delta weakly, displaying an IC50 greater than 1 mM.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=2557899&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1021/bi00447a002
dc.subjectAnimals; Cattle; DNA; DNA Polymerase II; DNA Polymerase III; DNA-Directed DNA Polymerase; Diphosphonates; Exonucleases; Molecular Structure; Phosphonoacetic Acid; Poly dA-dT; Templates, Genetic
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleCarbonyldiphosphonate, a selective inhibitor of mammalian DNA polymerase delta
dc.typeJournal Article
dc.source.journaltitleBiochemistry
dc.source.volume28
dc.source.issue21
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1223
dc.identifier.contextkey693133
html.description.abstract<p>Twenty-three pyrophosphate analogues were screened as inhibitors of proliferating cell nuclear antigen independent DNA polymerase delta (pol delta) derived from calf thymus. Carbonyldiphosphonate (COMDP), also known as alpha-oxomethylenediphosphonate, inhibited pol delta with a potency (Ki = 1.8 microM) 20 times greater than that displayed for DNA polymerase alpha (pol alpha) derived from the same tissue. Characterization of the mechanism of inhibition of pol delta indicated that COMDP competed with the dNTP specified by the template and was not competitive with the template-primer. In the case of pol alpha, COMDP did not compete with either the dNTP or the polynucleotide substrate. COMDP inhibited the 3'----5' exonuclease activity of pol delta weakly, displaying an IC50 greater than 1 mM.</p>
dc.identifier.submissionpathgsbs_sp/1223
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentDepartment of Pharmacology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages8270-4


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