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Title:Assignment of Enzyme Function Through Characterization of the RuBisCO and Enolase Superfamilies
Author(s):Imker, Heidi J.
Doctoral Committee Chair(s):Gerlt, John A.
Department / Program:Biochemistry
Discipline:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Chemistry, Biochemistry
Abstract:The second superfamily explored in this work is that of the enolase superfamily. Genomic context and primary amino acid sequence make it clear that although the enzymes in this superfamily are structurally and mechanistically related, the chemistry and substrates are varied. Two highly divergent enzymes from Thermotoga maritima and Enterococcus faecalis were targeted for characterization through a multi-disciplinary effort that included structural, computational, and bioinformatic analysis as well as classical enzymology. The T. maritima and E. faecalis enzymes were subsequently confirmed as dipeptide epimerases with unique specificity for hydrophobic dipeptides through screening of dipeptide libraries by mass spectrometry followed by full kinetic characterization of individual dipeptide substrates. These results have provided additional evidence for the utility of multi-disciplinary approaches to functional assignment through use of well-characterized enzyme superfamilies.
Issue Date:2008
Type:Text
Language:English
Description:219 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008.
URI:http://hdl.handle.net/2142/84860
Other Identifier(s):(MiAaPQ)AAI3347396
Date Available in IDEALS:2015-09-25
Date Deposited:2008


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