The microsomal dicarboxylyl-CoA synthetase

Vamecq, Jòseph; Hoffmann, Edmond de; Hoof, F. Van

doi:10.1042/bj2300683

Cited by 88 publications

(41 citation statements)

References 49 publications

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“…The use of a KO mouse model revealed a similar picture with defi cient C14-DCA oxidation in hepatocytes devoid of Pex5 ( 17 ). Before peroxisomal ␤ -oxidation, long-chain DCAs are activated to their CoA ester by a microsomal acyl-CoA synthetase ( 42,43 ), the molecular identity of which is unknown. Acsl1, which is present in the gene coexpression subnetwork, is a candidate gene for this function ( 44 ).…”

Section: Decreased Medium-chain Dicarboxylic Acid Levels In Ehhadh Komentioning

confidence: 89%

Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids

Houten

Denis

Argmann

et al. 2012

Journal of Lipid Research

145

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Section: Decreased Medium-chain Dicarboxylic Acid Levels In Ehhadh Komentioning

confidence: 89%

Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids

Houten

Denis

Argmann

et al. 2012

Journal of Lipid Research

145

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“…By analogy, one might mention, here, the formation of a glutaconoyl moiety in the unesterified form from glutaric acid, a pathway which proceeds according to a parallel sequence of reactions: i.e. successive involvements of microsomal dicarboxylyl-CoA synthetase [30] and peroxisomal glutaryl-CoA oxidase [20,21].…”

Section: Discussionmentioning

confidence: 99%

CoA esters of valproic acid and related metabolites are oxidized in peroxisomes through a pathway distinct from peroxisomal fatty and bile acyl‐CoA β‐oxidation

et al. 1993

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In rat liver homogenates fortified with the appropriate cofactors (ATP and CoA), valproic acid induced H,02 production rates by far lower than those recorded on the straight medium-chain fatty acid n-octanoic acid. Using directly the CoA esters of these carboxylic acids as substrates for the rat liver H,O,-generating enzyme activities, valproyl-CoA, and n-octanoyl-CoA were found to induce similar oxidation rates. In the rat liver homogenates, cyanide-insensitive valproyl-CoA and octanoyl-CoA oxidations occurred at rates similar to those of valproyl-CoA and octanoyl-CoA oxidase(s), respectively. Studies on fractions obtained from rat liver postnuclear supernatants by isopycnic centrifugation on a linear sucrose density gradient disclose that the density distribution of valproyl-CoA oxidase superimposes to those of catalase, fatty acyl-CoA oxidase and cyanideinsensitive fatty acyl-CoA oxidation, three peroxisomal marker activities. By contrast, the cyanide-insensitive valproyl-CoA oxidation does not adopt the typical peroxisomal distribution of these activities but rather exhibits a mitochondrial localization with, however, a minor peroxisomal component. Interestingly enough, the comparative study of rat tissue distribution, inducibility by clofibrate and sensitivity to deoxycholate indicated that valproyl-CoA oxidase is an enzyme distinct from fatty acyl-CoA oxidase and bile acyl-CoA oxidase. Taken as a whole, the results presented here support the occurrence of a peroxisomal oxidation of the CoA ester of valproic acid and its d4-enoic derivate which might be characterized by two major features: initiation by an acyl-CoA oxidase distinct from fatty and bile acyl-CoA oxidases, and inability to complete thej3-oxidation cycle which would not proceed, at significant rates, further than the /I-hydroxyacyl-CoA dehydrogenation step in peroxisomes.

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“…Fatty acids are first converted into -hydroxymonocarboxylic acids by a microsomal cytochrome P450 and then further oxidized to -ketomonocarboxylic acids and finally DCAs through the sequential action of cytosolic long-chain alcohol and aldehyde dehydrogenases. After activation by a dicarboxylyl-CoA synthetase present in microsomes, at least in rat liver (1), the dicarboxylyl-CoA esters are shortened via ␤ -oxidation ( Fig. 1 ).…”

mentioning

confidence: 99%

Identification of the peroxisomal β-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids

Ferdinandusse

Denis

Roermund

et al. 2004

Journal of Lipid Research

127

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Dicarboxylic acids (DCAs) are -oxidation products of monocarboxylic acids. After activation by a dicarboxylyl-CoA synthetase, the dicarboxylyl-CoA esters are shortened via ␤ -oxidation. Although it has been studied extensively where this ␤ -oxidation process takes place, the intracellular site of DCA oxidation has remained controversial. Making use of fibroblasts from patients with defined mitochondrial and peroxisomal fatty acid oxidation defects, we show in this paper that peroxisomes, and not mitochondria, are involved in the ␤ -oxidation of C16DCA. Additional studies in fibroblasts from patients with X-linked adrenoleukodystrophy, straight-chain acyl-CoA oxidase (SCOX) deficiency, d -bifunctional protein (DBP) deficiency, and rhizomelic chondrodysplasia punctata type 1, together with direct enzyme measurements with human recombinant l -bifunctional protein (LBP) and DBP expressed in a fox2 deletion mutant of Saccharomyces cerevisiae , show that the main enzymes involved in ␤ -oxidation of C16DCA are SCOX, both LBP and DBP, and sterol carrier protein X, possibly together with the classic 3-ketoacyl-CoA thiolase. This is the first indication of a specific function for LBP, which has remained elusive until now. -Ferdinandusse, S., S. Denis, C. W. T. van Roermund, R. J. A. Wanders, and G. Dacremont. Identification of the peroxisomal ␤ -oxidation enzymes involved in the degradation of long-chain dicarboxylic acids.

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The microsomal dicarboxylyl-CoA synthetase

Cited by 88 publications

References 49 publications

Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids

Peroxisomal L-bifunctional enzyme (Ehhadh) is essential for the production of medium-chain dicarboxylic acids

CoA esters of valproic acid and related metabolites are oxidized in peroxisomes through a pathway distinct from peroxisomal fatty and bile acyl‐CoA β‐oxidation

Identification of the peroxisomal β-oxidation enzymes involved in the degradation of long-chain dicarboxylic acids

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