Comparative inhibition studies of enoyl-CoA hydratase 1 and enoyl-CoA hydratase 2 in long-chain fatty acid oxidation.
Enoyl-CoA hydratase 1 and enoyl-CoA hydratase 2 in long-chain fatty acid oxidation were comparatively investigated through mechanistic studies for inactivation of the enzymes with methylenecyclopropylformyl-CoA and 3-octynoyl-CoA. Methylenecyclopropylformyl-CoA can inactivate both enzymes, while 3-octynoyl-CoA inactivates enoyl-CoA hydratase 2 only. The study increased our understanding of these two enzymes in fatty acid oxidation.
Wu
Long
L
Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong SAR, P. R. China.
Lin
Shuping
S
Li
Ding
D
D000214:Acyl Coenzyme A / Q000737:chemistry* / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D004746:Enoyl-CoA Hydratase / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D005227:Fatty Acids / Q000737:chemistry / Q000378:metabolism*; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D020675:Peroxisomes / Q000737:chemistry / Q000378:metabolism; D051381:Rats; D053719:Tandem Mass Spectrometry
C439085:(methylenecyclopropyl)formyl coenzyme A; C454719:3-octynoyl-CoA; D000214:Acyl Coenzyme A; D004791:Enzyme Inhibitors; D005227:Fatty Acids; D007527:Isoenzymes; D004746:Enoyl-CoA Hydratase