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Gerlt, John A. Imker, Heidi J. 2015-09-25T22:28:13Z 2015-09-25T22:28:13Z 10000-01-01 2008 2008 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. Made available in DSpace on 2015-09-25T22:28:13Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3347396.pdf: 15165404 bytes, checksum: 0321feeb50c6cc4aa2d63a9e320ec2c6 (MD5) Previous issue date: 2008 Embargo set by: Seth Robbins for item 86141 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 219 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008. http://hdl.handle.net/2142/84860 (MiAaPQ)AAI3347396 eng Chemistry, Biochemistry Assignment of Enzyme Function Through Characterization of the RuBisCO and Enolase Superfamilies text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.