Expression and mechanistic studies on orotidine-5'-monophosphate decarboxylase /

Kitzmiller, Kathryn J.; Youngstown State University. Dept. of Chemistry.

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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

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