Enzymes as Drug Targets in the Isoprenoid Biosynthesis Pathway: Structure, Mechanism and Inhibition
Yin, Fenglin
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https://hdl.handle.net/2142/85468
Description
Title
Enzymes as Drug Targets in the Isoprenoid Biosynthesis Pathway: Structure, Mechanism and Inhibition
Author(s)
Yin, Fenglin
Issue Date
2008
Doctoral Committee Chair(s)
Oldfield, Eric
Department of Study
Biophysics and Computational Biology
Discipline
Biophysics and Computational Biology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
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.
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