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Gerlt, John A. Hubbard, Brian Kent 2015-09-25T22:14:38Z 2015-09-25T22:14:38Z 10000-01-01 2000 2000 In this thesis, the enolase superfamily is traced phylogentically and studied in detail to ascertain which active site residues are necessary to maintain function, kinetic competence, and/or substrate specificity. Methods for understanding the details of many enzymes in the enolase superfamily are developed as well as methods for predicting the function of previously uncharacterized members of the enolase superfamily. Made available in DSpace on 2015-09-25T22:14:38Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9955627.pdf: 5920785 bytes, checksum: bc8639410ffb802dc87ac49321387e87 (MD5) Previous issue date: 2000 Embargo set by: Seth Robbins for item 85746 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 165 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000. http://hdl.handle.net/2142/84465 (MiAaPQ)AAI9955627 eng Chemistry, Organic Functional and Mechanistic Investigations of Enzymes in the Enolase Superfamily text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.