Inactivation of thiolase by 2-alkynoyl-CoA via its intrinsic isomerase activity.
Selective inactivation of cytosolic thiolase by 2-alkynoyl-CoA via its intrinsic isomerase activity was studied, which provides an example for rationally developing mechanism-based inhibitors based on a side activity of the enzyme, and may become a supplemental method for better treatment of cardiovascular disease and cancer.
Wu
Long
L
Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, PRC.
Zeng
Jia
J
Deng
Guisheng
G
Guo
Fei
F
Li
Nan
N
Liu
Xiaojun
X
Chu
Xiusheng
X
Li
Ding
D
D000105:Acetyl Coenzyme A / Q000737:chemistry* / Q000378:metabolism*; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D002384:Catalysis; D002460:Cell Line; D004789:Enzyme Activation; D007536:Isomerism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D051381:Rats; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000378:metabolism*; D053719:Tandem Mass Spectrometry
D000596:Amino Acids; D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; D000105:Acetyl Coenzyme A