Kinetic characteristics of rat liver peroxisomal nafenopin-CoA ligase

Benjamin J. Roberts; John K. Macleod; Inderjit Singh; Kathleen M. Knights

doi:10.1016/0006-2952(94)00516-O

Kinetic characteristics of rat liver peroxisomal nafenopin-CoA ligase

Benjamin J. Roberts, John K. Macleod, Inderjit Singh, Kathleen M. Knights

Research output: Contribution to journal › Article › peer-review

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Abstract

In this study we have demonstrated that rat hepatic peroxisomes catalyse the formation of nafenopin-CoA. The process is mediated by apparent high affinity (K_m 6.7 μM), low capacity (V_max 0.31 nmol/mg/min) and low affinity, high capacity isoforms. Palmitic acid (K_i 1.1 μM), r(-) ibuprofen (K_i 7.9 μM), ciprofibrate (K_i 60.2 μM) and clofibric acid (K_i 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.

Original language	English
Pages (from-to)	1335-1339
Number of pages	5
Journal	Biochemical Pharmacology
Volume	49
Issue number	9
DOIs	https://doi.org/10.1016/0006-2952(94)00516-O
Publication status	Published - 11 May 1995

Keywords

hepatic peroxisomes
nafenopin
nafenopin-CoA ligase
palmitic acid, long chain fatty acid-CoA ligase
xenobiotic carboxylic acids

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title = "Kinetic characteristics of rat liver peroxisomal nafenopin-CoA ligase",

abstract = "In this study we have demonstrated 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.",

keywords = "hepatic peroxisomes, nafenopin, nafenopin-CoA ligase, palmitic acid, long chain fatty acid-CoA ligase, xenobiotic carboxylic acids",

author = "Roberts, {Benjamin J.} and Macleod, {John K.} and Inderjit Singh and Knights, {Kathleen M.}",

year = "1995",

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AU - Roberts, Benjamin J.

AU - Macleod, John K.

AU - Singh, Inderjit

AU - Knights, Kathleen M.

PY - 1995/5/11

Y1 - 1995/5/11

N2 - In this study we have demonstrated 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.

AB - In this study we have demonstrated 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.

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KW - palmitic acid, long chain fatty acid-CoA ligase

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