2026-09-22T12:12:10Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/84872 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Gerlt, John A. Wood, Bryant McKay 2015-09-25T22:28:16Z 2015-09-25T22:28:16Z 10000-01-01 2010 2010 By applying the tools of enzymology learned in the Gerlt Laboratory and working successfully with numerous collaborators, I have furthered our understanding of the mechanism of one of Nature's best catalysts, OMPDC. Increasingly in enzymology, the role of conformational change in enzyme catalysis has been recognized as an important one. This research has shed light on the conformational changes that take place when substrate binds OMPDC and how the two events are coordinated. Made available in DSpace on 2015-09-25T22:28:16Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3455890.pdf: 12370602 bytes, checksum: 165dd53e2f443ecf0e27ec0983029aad (MD5) Previous issue date: 2010 Embargo set by: Seth Robbins for item 86153 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 294 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2010. http://hdl.handle.net/2142/84872 (MiAaPQ)AAI3455890 eng Chemistry, Physical In Search of Catalytic Proficiency: The Importance of Enzyme Conformational Change to Orotidine 5'-Monophosphate Decarboxylase Catalysis text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.