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Mutation and inhibition studies of mevalonate 5-diphosphate decarboxylase.

Abstract
Mevalonate 5-diphosphate decarboxylase plays an important role in regulating cholesterol biosynthesis, which was studied through incubation with various synthetic substrate analogs and characterization of mutated enzymes. The results are potentially useful for further developing inhibitors that block the mevalonate pathway which is a drug target for treating cardiovascular disease and cancer.
AuthorsYongge Qiu, Jinbo Gao, Fei Guo, Yuqin Qiao, Ding Li
JournalBioorganic & medicinal chemistry letters (Bioorg Med Chem Lett) Vol. 17 Issue 22 Pg. 6164-8 (Nov 15 2007) ISSN: 0960-894X [Print] England
PMID17888661 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Cholesterol
  • Carboxy-Lyases
  • pyrophosphomevalonate decarboxylase
Topics
  • Animals
  • Carboxy-Lyases (antagonists & inhibitors, chemistry, genetics)
  • Cholesterol (metabolism)
  • Drug Evaluation, Preclinical
  • Inhibitory Concentration 50
  • Kinetics
  • Liver (enzymology)
  • Molecular Structure
  • Mutagenesis, Site-Directed
  • Rats
  • Signal Transduction (drug effects)
  • Structure-Activity Relationship
  • Substrate Specificity (genetics)
  • Yeasts (enzymology)

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