Enoyl CoA isomerase

fatty acids at gamma-carbon (position 3) to trans double bonds at beta-carbon

unsaturated fatty acids in beta oxidation

fatty acids with double bonds at even-numbered carbon positions also produces 3-trans-enoyl-CoA in mammals and yeasts, enoyl-CoA isomerase is technically required for their metabolism as well.^[3] The reaction mechanism is detailed in figure 1,^[4] and the base that initiates the isomerization and NH groups that stabilize the intermediate are located on the active site of enoyl-coA isomerase

oxidation and carbon-to-carbon bond cleavage, thereby shortening the fatty acid

mitochondrial enoyl Co-A isomerase: short-chain and long-chain [4].^[6] In an immunoblot, antibodies were run against all enoyl CoA isomerase. However, two of these isomerases had antibody attachment: the short chain isomerase and the peroxisomal multifunctional enzyme.^[6] There was one enzyme which did not have binding specificity to this antibody: mitochondrial long-chain isomerase. Long-chain isomerase was found when it eluted at a lower potassium phosphate concentration in the gradient.^[6][7]

mitochondrial enzyme is essential for deriving maximum energy from lipids and fueling muscles.^[9]

hydratase activity.^[13] The Plant form did not form a 2-cis-isomer (from enoyl-CoA hydratase) or D- or L- 3 hydroxy derivative (L-(−)-3-hydroxyacyl-CoA dehydrogenase): products of multifunctional enzyme of rat liver.^[13] The turnover rates of these the two sub divisions of peroxisomes are very different. The Kcat/Km ratio in cotyledons is 10^6 M-1s-1 which outperforms the ratio .07 * 10^6 M-1s-1.^[13] Due to a high turnover rate, the plant peroxisomes contain a lesser amount of enoyl-CoA isomerase than their counterparts in the rat liver.^[13]

E. coli and rat liver.^[15][18]

alpha-helix.^[19]

carbonyl oxygen of the acyl-CoA intermediate. The formation of this oxyanion hole stabilizes the transition state of the enzyme-catalyzed reaction.^[4]

glutamate side chain to retain the proton and later deliver it back to the acyl-CoA, on a different carbon position.^[4]

peroxisomal enzymes in a yeast species, Saccharomyces cerevisiae. Their relative locations on the enzyme can be compared in figure 2.^[4]

enzymes in Saccharomyces cerevisiae is displayed in figure 3.^[20]

cDNA probes,^[3] but by copurification with a transferase, human glutathione S-transferases.^[22]

beta-oxidation to human diseases,^[22]

dicarboxylic acids, a condition called dicarboxylic aciduria.^[9]

latency of the virus and no existing cures to rid the virus specifically,^[25] HCV is a serious problem that is causing more deaths than HIV/AIDS in the United States,^[26] but its threat still do not receive adequate attention. The need for a HCV-specific treatment is essential, and according to John Ward, the director of the CDC Hepatitis Division, it can save up to 120,000 lives.^[26]

intracellular level.^[23]