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 ��PCM. / Graduation date: 1996
| Identifer | oai:union.ndltd.org:ORGSU/oai:ir.library.oregonstate.edu:1957/34697 |
| Date | 09 May 1995 |
| Creators | Lindquist, Jonathan A. |
| Contributors | McFadden, Philip N. |
| Source Sets | Oregon State University |
| Language | en_US |
| Detected Language | English |
| Type | Thesis/Dissertation |
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