dc.contributor.author |
Kitzmiller, Kathryn J. |
en_US |
dc.contributor.author |
Youngstown State University. Dept. of Chemistry. |
en_US |
dc.date.accessioned |
2011-01-31T14:20:09Z |
|
dc.date.accessioned |
2019-09-08T02:34:54Z |
|
dc.date.available |
2011-01-31T14:20:09Z |
|
dc.date.available |
2019-09-08T02:34:54Z |
|
dc.date.created |
2004 |
en_US |
dc.date.issued |
2004 |
en_US |
dc.identifier.other |
b19606230 |
en_US |
dc.identifier.uri |
http://jupiter.ysu.edu/record=b1960623 |
en_US |
dc.identifier.uri |
http://hdl.handle.net/1989/6313 |
|
dc.description |
xi, 86 leaves : ill. ; 28 cm. |
en_US |
dc.description |
Thesis (M.S.)--Youngstown State University, 2004. |
en_US |
dc.description |
Includes bibliographical references (leaves 85-86). |
en_US |
dc.description.abstract |
Orotidine-5'-monophosphate decarboxylase, ODCase, catalyzes the conversion of
OMP to UMP in the pyrimidine biosynthetic pathway. This enzyme is remarkable in
both its rate enhancement and lack of a cofactor. For this reason, the mechanism has
been under investigation. Currently, a new hypothesis raises the question as to whether
the substrate binds with its C6 group or 02 group facing the lysine residue at position 93.
To determine this, an isoteric inhibitor along with chemically modified and mutated
ODCase clones would provide evidence through 15N labeled NMR samples. This thesis
produced the resources necessary to chemically modify the protein by providing an
adequate expression system and growth conditions for ODCase WT, CysFree, C930nly,
and K93C. |
en_US |
dc.description.statementofresponsibility |
by Kathryn J. Kitzmiller. |
en_US |
dc.language.iso |
en_US |
en_US |
dc.relation.ispartofseries |
Master's Theses no. 0814 |
en_US |
dc.subject.classification |
Master's Theses no. 0814 |
en_US |
dc.subject.lcsh |
Decarboxylases. |
en_US |
dc.title |
Expression and mechanistic studies on orotidine-5'-monophosphate decarboxylase / |
en_US |
dc.type |
Thesis |
en_US |