Inhibition of mevalonate 5-diphosphate decarboxylase by fluorinated substrate analogs

• Published in: Biochimica et biophysica acta Vol. 1760; no. 7; pp. 1080 - 1087
• Main Authors: Qiu, Yongge, Li, Ding
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.07.2006
• Subjects: Animals; Cancer; Carboxy-Lyases - antagonists & inhibitors; Carboxy-Lyases - chemistry; Cardiovascular disease; Cardiovascular System - pathology; Cholesterol; Cholesterol - chemistry; Cloning, Molecular; Dose-Response Relationship, Drug; Fluorinated inhibitor; Fluorine - chemistry; Inhibitory Concentration 50; Kinetics; Mevalonate 5-diphosphate decarboxylase; Mevalonate kinase; Mevalonic Acid - chemistry; Models, Chemical; Phosphotransferases (Alcohol Group Acceptor) - chemistry; Rats; Substrate Specificity; PP; GGPP; MVK; GHMP; GPP; FPP; IPP; Fluorinated inhibitor; Cardiovascular disease; MDD; Cholesterol; PMK; TsCl; Mevalonate 5-diphosphate decarboxylase; Mevalonate kinase; HMG-CoA reductase; MVAPP; Cancer

Mevalonate 5-diphosphate decarboxylase (MDD) is a peroxisomal enzyme in the cholesterol biosynthetic pathway, which plays an important role in regulating cholesterol biosynthesis. In the present study, rat MDD was cloned and purified to apparent homogeneity. Two fluorinated MDD substrate analogs, P′...