Enzymes as drug targets in the isoprenoid biosynthesis pathway: Structure, mechanism and inhibition
by Yin, Fenglin, Ph.D., UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN, 2008, 87 pages; 3314948

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.

 
AdviserEric Oldfield
SchoolUNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN
SourceDAI/B 69-05, p. , Sep 2008
Source TypeDissertation
SubjectsPharmacology; Biochemistry; Biophysics
Publication Number3314948
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