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oai:www.ideals.illinois.edu:2142/85468 2023-07-11 col_2142_5131 col_2142_14828 com_2142_5130 com_2142_14827 com_2142_14793 com_2142_8903

Oldfield, Eric Yin, Fenglin 2015-09-25T22:46:11Z 2015-09-25T22:46:11Z 10000-01-01 2008 2008 Enzymes in isoprenoid biosynthesis pathway play important roles in all living organisms. Several of them have been identified as drug targets. Here we reported the inhibition study of isopentenyl diphosphate/dimethylallyl diphosphate isomerase (IPPI) and deoxyzylolus reductoisomerase (DXR), along with crystal structures of enzyme inhibitor complexes. A high throughput screening method was developed, by which novel potent inhibitors against farnesyl diphosphate synthase (FPPS) and Staph. Aureus dehydrosqulene synthase (CrtM) were identified. We also conducted thermodynamic study of FPPS inhibition, which revealed that both enthalpy and antropy driven binding inhibitors have similar activity. Made available in DSpace on 2015-09-25T22:46:11Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3314948.pdf: 1523630 bytes, checksum: c190a25d5559bf8bd7075e02d3067599 (MD5) Previous issue date: 2008 Embargo set by: Seth Robbins for item 86749 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 87 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008. http://hdl.handle.net/2142/85468 (MiAaPQ)AAI3314948 eng Chemistry, Biochemistry Enzymes as Drug Targets in the Isoprenoid Biosynthesis Pathway: Structure, Mechanism and Inhibition text Biophysics and Computational Biology Biophysics and Computational Biology University of Illinois at Urbana-Champaign Dissertation Ph.D.