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Gerlt, John A. Rakus, John Frank 2015-09-25T22:28:15Z 2015-09-25T22:28:15Z 10000-01-01 2009 2009 Studying the functional and catalytic diversity in the enolase superfamily is a valuable enterprise in accelerating the field of genomic enzymology. This is of paramount importance as the accumulation of genomic data is threatening to outstrip the ability for biochemists to study proteins at a pace that is commensurate with sequencing. Therefore, these contributions to defining the functional diversity within the confines of a mechanistically diverse superfamily are undeniably important in providing the basic understanding to allow for the most rapid possible assignment of protein functions. Made available in DSpace on 2015-09-25T22:28:15Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3392442.pdf: 2411492 bytes, checksum: 771db08cc1d1511437123d5150b43572 (MD5) Previous issue date: 2009 Embargo set by: Seth Robbins for item 86147 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 176 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2009. http://hdl.handle.net/2142/84866 (MiAaPQ)AAI3392442 eng Chemistry, Biochemistry The Identification of Novel Enzymatic Functions in the Enolase Superfamily text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.