112195-81-0Relevant articles and documents
Kinetic Characteristics of Rat Liver Peroxisomal Nafenopin-CoA Ligase
Roberts, Benjamin J.,Macleod, John K.,Singh, Inderjit,Knights, Kathleen M.
, p. 1335 - 1340 (2007/10/03)
In this study we have demostrated that rat hepatic peroxisomes catalyse the formation of nafenopin-CoA. The process is mediated by apparent high affinity (Km 6.7 μM), low capacity (Vmax 0.31 nmol/mg/min) and low affinity, high capacity isoforms. Palmitic acid (Ki 1.1 μM), R(-) ibuprofen (Ki 7.9 μM), ciprofibrate (Ki 60.2 μM) and clofibric acid (Ki 86,8 μM) competitively inhibited nafenopin-CoA formation catalysed by the apparent high affinity isoform. An antibody raised against the microsomal palmitoyl-CoA ligase inhibited the equivalent peroxisomal enzyme significantly (P 0.001) but did not inhibit peroxisomal nafenopin-CoA ligase activity. These data suggest that nafenopin-CoA formation is catalysed by a peroxisomal CoA ligase which differs from the peroxisomal long chain fatty acid-CoA ligase in relation to its xenobiotic/antibody inhibitor profile and kinetic characteristics.