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dc.contributor.authorObianyo, Obiamaka
dc.contributor.authorThompson, Paul R
dc.date2022-08-11T08:11:00.000
dc.date.accessioned2022-08-23T17:28:12Z
dc.date.available2022-08-23T17:28:12Z
dc.date.issued2012-02-17
dc.date.submitted2015-05-22
dc.identifier.citationJ Biol Chem. 2012 Feb 17;287(8):6062-71. doi: 10.1074/jbc.M111.333609. Epub 2012 Jan 3. <a href="http://dx.doi.org/10.1074/jbc.M111.333609">Link to article on publisher's site</a>
dc.identifier.issn0021-9258 (Linking)
dc.identifier.doi10.1074/jbc.M111.333609
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50029
dc.description<p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</p>
dc.description.abstractThe protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the mono- and dimethylation of arginine residues in a variety of proteins. Although these enzymes play important roles in a variety of cellular processes, aberrant PRMT activity is associated with several disease states, including heart disease and cancer. In an effort to guide the development of inhibitors targeting individual PRMTs, we initiated studies to characterize the molecular mechanisms of PRMT catalysis. Herein, we report studies on the kinetic mechanism of PRMT6. Initial velocity, product inhibition, and dead-end analog inhibition studies with the AcH4-21 and R1 peptides, as well as their monomethylated versions, indicate, in contrast to a previous report, that PRMT6 utilizes a rapid equilibrium random mechanism with dead-end EAP and EBQ complexes.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=22219200&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3325592/
dc.subjectAmino Acid Sequence
dc.subjectBiocatalysis
dc.subjectDrug Discovery
dc.subjectEnzyme Inhibitors
dc.subjectHumans
dc.subjectKinetics
dc.subjectNuclear Proteins
dc.subjectPeptides
dc.subjectProtein-Arginine N-Methyltransferases
dc.subjectBiochemistry
dc.subjectEnzymes and Coenzymes
dc.subjectMedicinal-Pharmaceutical Chemistry
dc.subjectTherapeutics
dc.titleKinetic mechanism of protein arginine methyltransferase 6 (PRMT6).
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume287
dc.source.issue8
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/thompson/39
dc.identifier.contextkey7135705
html.description.abstract<p>The protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the mono- and dimethylation of arginine residues in a variety of proteins. Although these enzymes play important roles in a variety of cellular processes, aberrant PRMT activity is associated with several disease states, including heart disease and cancer. In an effort to guide the development of inhibitors targeting individual PRMTs, we initiated studies to characterize the molecular mechanisms of PRMT catalysis. Herein, we report studies on the kinetic mechanism of PRMT6. Initial velocity, product inhibition, and dead-end analog inhibition studies with the AcH4-21 and R1 peptides, as well as their monomethylated versions, indicate, in contrast to a previous report, that PRMT6 utilizes a rapid equilibrium random mechanism with dead-end EAP and EBQ complexes.</p>
dc.identifier.submissionpaththompson/39
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages6062-71


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