Mutation and inhibition studies of mevalonate 5-diphosphate decarboxylase.
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.
Qiu
Yongge
Y
Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, PR China.
Gao
Jinbo
J
Guo
Fei
F
Qiao
Yuqin
Y
Li
Ding
D
D000818:Animals; D002262:Carboxy-Lyases / Q000037:antagonists & inhibitors* / Q000737:chemistry* / Q000235:genetics; D002784:Cholesterol / Q000378:metabolism; D004353:Drug Evaluation, Preclinical; D020128:Inhibitory Concentration 50; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D051381:Rats; D015398:Signal Transduction / Q000187:drug effects; D013329:Structure-Activity Relationship; D013379:Substrate Specificity / Q000235:genetics; D015003:Yeasts / Q000201:enzymology
D002784:Cholesterol; D002262:Carboxy-Lyases; C022503:pyrophosphomevalonate decarboxylase