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Automethylation : a response to enzyme aging

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dc.contributor.advisor McFadden, Philip N.
dc.creator Lindquist, Jonathan A.
dc.date.accessioned 2012-10-25T19:07:41Z
dc.date.available 2012-10-25T19:07:41Z
dc.date.copyright 1995-05-09
dc.date.issued 1995-05-09
dc.identifier.uri http://hdl.handle.net/1957/34697
dc.description Graduation date: 1996 en_US
dc.description.abstract This is the first study to explore the ability of an enzyme to recognize and repair spontaneous age-dependent damage to its own sequence. Protein (D-aspartyl/L-isoaspartyl) carboxyl methyltransferase (PCM) is known to repair damage that arises from a spontaneous isomerization of aspartyl and asparaginyl residues in other proteins during aging. As PCM contains several conserved aspartyl and asparaginyl residues, this dissertation tested whether PCM can serve as a methyl acceptor in its own methylation reaction. In investigating the ability of PCM to automethylate, it was discovered that PCM is damaged. The mechanism of this automethylation reaction was determined to be an intermolecular, high affinity, slow turnover reaction and was limited to a subpopulation of damaged PCM molecules, termed αPCM. en_US
dc.language.iso en_US en_US
dc.subject.lcsh Methyltransferases -- Methylation en_US
dc.subject.lcsh Methyltransferases -- Deterioration en_US
dc.title Automethylation : a response to enzyme aging en_US
dc.type Thesis/Dissertation en_US
dc.degree.name Doctor of Philosophy (Ph. D.) in Biochemistry and Biophysics en_US
dc.degree.level Doctoral en_US
dc.degree.discipline Science en_US
dc.degree.grantor Oregon State University en_US
dc.contributor.committeemember Barofsky, Douglas
dc.contributor.committeemember Ho, P. Shing
dc.contributor.committeemember Schimerlik, Michael
dc.contributor.committeemember Somoza, Carmen
dc.description.digitization File scanned at 300 ppi (Monochrome, 8-bit Grayscale) using ScandAll PRO 1.8.1 on a Fi-6670 in PDF format. CVista PdfCompressor 4.0 was used for pdf compression and textual OCR. en_US
dc.description.peerreview no en_us


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