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Acyl-CoA Oxidase

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Rja Wanders – One of the best experts on this subject based on the ideXlab platform.

  • Straight-chain Acyl-CoA Oxidase deficiency presenting with dysmorphia, neurodevelopmental autistic-type regression and a selective pattern of leukodystrophy
    Journal of inherited metabolic disease, 2004
    Co-Authors: M. A. Kurian, Rja Wanders, Stephanie Ryan, G. T. N. Besley, Mary D. King

    Abstract:

    Summary: We report a rare case of straight-chain Acyl-CoA Oxidase deficiency (McKusick 264470) presenting with dysmorphism, neurodevelopmental regression and leukodystrophy.

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  • Novel deletion in a patient with an isolated peroxisoml Acyl-CoA Oxidase deficiency
    American Journal of Human Genetics, 1994
    Co-Authors: B. T. Poll-the, B. Fournier, H. Clevers, Rja Wanders

    Abstract:

    Disorders with defective peroxisome assembly are associated with multiple peroxisomal enzymatic abnormalities. Besides these diseases patients have been described suspected of having a single enzyme defect in the peroxisomal {beta}-oxidation pathway. Laboratory findings for these patients include elevated plasma very long chain fatty acids (VLCFA) and impaired VLCFA oxidation in fibroblasts. Complementation analysis between these patients and those with a proven single enzyme deficiency, using peroxisomal {beta}-oxidation of VLCFA as the criterion for complementation, has been used to show whether the patients are deficient in Acyl-CoA Oxidase, peroxisomal trifunctional protein or thiolase activity. Fibroblasts from a patient showing the clinical and biochemical abnormalities of isolated Acyl-CoA Oxidase deficiency (using cell complementation) were analyzed at the molecular level. Isolation of RNA from patient`s fibroblasts was followed by random reverse transcription of RNA and PCR amplification. PCR products were blotted and hybridized with the human Acyl-CoA Oxidase cDNA. A fragment 150 bp shorter than normal was found. Upon sequencing, exon 7 was found to be deleted leading to a frameshift in the Acyl-CoA Oxidase mRNA. Southern blot analysis of the patient`s DNA did not reveal any deletion in contrast to two siblings previously reported as having a deletion of at least 17more » kb in the Acyl-CoA Oxidase gene.« less

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  • The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain Acyl-CoA Oxidase in human liver and kidney.
    The Journal of biological chemistry, 1993
    Co-Authors: G Vanhove, Rja Wanders, P. P. Van Veldhoven, H J Eyssen, Marc Fransen, Simone Denis, G P Mannaerts

    Abstract:

    Rat liver peroxisomes contain three Acyl-CoA Oxidases: palmitoyl-CoA Oxidase, which oxidizes the CoA esters of straight chain fatty acids and prostaglandins; pristanoyl-CoA Oxidase, which oxidizes the CoA esters of 2-methyl-branched fatty acids (e.g. pristanic acid); and trihydroxycoprostanoyl-CoA Oxidase, which oxidizes the CoA esters of the bile acid intermediates di- and trihydroxycoprostanic acids (Van Veldhoven, P. P., Vanhove, G., Asselberghs, S., Eyssen, H. J., and Mannaerts, G. P. (1992) J. Biol. Chem. 267, 20065-20074). In the present report we demonstrate that human liver peroxisomes contain only two Acyl-CoA Oxidases: palmitoyl-CoA Oxidase, which oxidizes the CoA esters of straight chain fatty acids and prostaglandins, and a novel branched chain Acyl-CoA Oxidase, which oxidizes the CoA esters of 2-methyl-branched fatty acids as well as those of the bile acid intermediates (which also possess a 2-methyl substitution in their side chains). The branched chain Acyl-CoA Oxidase was purified to near homogeneity by means of column chromatography. It appeared to be a 70-kDa monomeric protein that did not cross-react with antisera raised against rat palmitoyl-CoA Oxidase and pristanoyl-CoA Oxidase. No indication was found for the presence of a separate trihydroxycoprostanoyl-CoA Oxidase in human liver. The branched chain Acyl-CoA Oxidase was present also in human kidney, suggesting that it is expressed in other extrahepatic tissues as well. Our results explain a number of clinical-chemical observations made in certain cases of peroxisomal beta-oxidation disorders.

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Mikio Nishimura – One of the best experts on this subject based on the ideXlab platform.

  • A Novel Acyl-CoA Oxidase That Can Oxidize Short-chain Acyl-CoA in Plant Peroxisomes
    The Journal of biological chemistry, 1999
    Co-Authors: H. Hayashi, L. De Bellis, A. Ciurli, Maki Kondo, M. Hayashi, Mikio Nishimura

    Abstract:

    Abstract Short-chain Acyl-CoA Oxidases are β-oxidation enzymes that are active on short-chain Acyl-CoAs and that appear to be present in higher plant peroxisomes and absent in mammalian peroxisomes. Therefore, plant peroxisomes are capable of performing complete β-oxidation of Acyl-CoA chains, whereas mammalian peroxisomes can perform β-oxidation of only those Acyl-CoA chains that are larger than octanoyl-CoA (C8). In this report, we have shown that a novel Acyl-CoA Oxidase can oxidize short-chain Acyl-CoA in plant peroxisomes. A peroxisomal short-chain Acyl-CoA Oxidase from Arabidopsis was purified following the expression of the Arabidopsis cDNA in a baculovirus expression system. The purified enzyme was active on butyryl-CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8). Cell fractionation and immunocytochemical analysis revealed that the short-chain Acyl-CoA Oxidase is localized in peroxisomes. The expression pattern of the short-chain Acyl-CoA Oxidase was similar to that of peroxisomal 3-ketoAcyl-CoA thiolase, a marker enzyme of fatty acid β-oxidation, during post-germinative growth. Although the molecular structure and amino acid sequence of the enzyme are similar to those of mammalian mitochondrial Acyl-CoA dehydrogenase, the purified enzyme has no activity as Acyl-CoA dehydrogenase. These results indicate that the short-chain Acyl-CoA Oxidases function in fatty acid β-oxidation in plant peroxisomes, and that by the cooperative action of long- and short-chain Acyl-CoA Oxidases, plant peroxisomes are capable of performing the complete β-oxidation of Acyl-CoA.

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  • Purification and characterization of pumpkin long‐chain acyl‐CoA Oxidase
    Physiologia Plantarum, 1999
    Co-Authors: Luigi De Bellis, Pietro Giuntini, Hiroshi Hayashi, Makoto Hayashi, Mikio Nishimura

    Abstract:

    Pumpkin (Cucurbita sp.) long-chain Acyl-CoA Oxidase (ACOX) (EC 1.3.3.6) was purified to homogeneity by hydrophobic interaction, hydroxyapatite, affinity, and anion exchange chromatographies. The purified isoenzyme is a dimeric protein, consisting of two apparently identical 72-kDa subunits. The protein is exclusively localized in glyoxysomes. The enzyme catalyzes selectively the oxidation of CoA esters of fatty acids with 12-18 C atoms and exhibits highest activity with C-14 fatty acids, but no activity with isobutyryl-CoA and isovaleryl-CoA (branched chain) or glutaryl-CoA (dicarboxylic). The enzyme is strongly inhibited by high concentrations of palmitoyl-CoA and weakly inhibited by high concentration of myristoyl-CoA. It is also inhibited by Triton X-100 at concentrations above 0.018% (w/v) the critical micellar concentration. The consequences of the substrate inhibition for the evaluation of long-chain ACOX activity in plant tissues are discussed.

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  • Molecular characterization of a glyoxysomal long chain Acyl-CoA Oxidase that is synthesized as a precursor of higher molecular mass in pumpkin.
    The Journal of biological chemistry, 1998
    Co-Authors: Hidenori Hayashi, L. De Bellis, M. Hayashi, Katsushi Yamaguchi, Akira Kato, Mikio Nishimura

    Abstract:

    Abstract A cDNA clone for pumpkin Acyl-CoA Oxidase (EC1.3.3.6; ACOX) was isolated from a λgt11 cDNA library constructed from poly(A)+ RNA extracted from etiolated cotyledons. The inserted cDNA clone contains 2313 nucleotides and encodes a polypeptide of 690 amino acids. Analysis of the amino-terminal sequence of the protein indicates that the pumpkin Acyl-CoA Oxidase protein is synthesized as a larger precursor containing a cleavable amino-terminal presequence of 45 amino acids. This presequence shows high similarity to the typical peroxisomal targeting signal (PTS2). Western blot analysis following cell fractionation in a sucrose gradient revealed that ACOX is localized in glyoxysomes. A partial purification of ACOX from etiolated pumpkin cotyledons indicated that the ACOX cDNA codes for a long chain Acyl-CoA Oxidase. The amount of ACOX increased and reached to the maximum activity by day 5 of germination but decreased about 4-fold on the following days during the subsequent microbody transition from glyoxysomes to leaf peroxisomes. By contrast, the amount of mRNA was already high at day 1 of germination, increased by about 30% at day 3, and faded completely by day 7. These data indicated that the expression pattern of ACOX was very similar to that of the glyoxysomal enzyme 3-ketoAcyl-CoA thiolase, another marker enzyme of the β-oxidation spiral, during germination and suggested that the expression of each enzyme of β-oxidation is coordinately regulated.

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Bjørn O. Christophersen – One of the best experts on this subject based on the ideXlab platform.

  • Peroxisomal beta-oxidation of polyunsaturated long chain fatty acids in human fibroblasts. The polyunsaturated and the saturated long chain fatty acids are retroconverted by the same Acyl-CoA Oxidase.
    Scandinavian Journal of Clinical & Laboratory Investigation, 1993
    Co-Authors: Erik Christensen, B. T. Poll-the, Rja Wanders, Berit Woldseth, Tor-arne Hagve, H. Sprecher, Oddvar Stokke, Bjørn O. Christophersen

    Abstract:

    The metabolism of the C22 unsaturated fatty acids erucic acid (22:1(n-9)), adrenic acid (22:4(n-6)), docosapentaenoic acid (22:5(n-3)) and docosahexaenoic acid (22:6(n-3)) was studied in cultured fibroblasts from patients with Acyl-CoA Oxidase deficiency, the Zellweger syndrome, X-linked adrenoleukodystrophy (X-ALD) and normal controls.[3-14C] 22:4 (n-6) and [3-14C] 22:5 (n-3) were shortened (retroconverted) to [1-I4C] 20:4 (n-6) and [1-14C] 20:5 (n-3), respectively, in normal and X-ALD fibroblasts. In Zellweger and Acyl-CoA Oxidase deficient fibroblasts these reactions were deficient.Since the retroconversion is normal in X-ALD fibroblasts peroxisomal very long chain (lignoceryl) CoA ligase is probably not required for the activation of C22 unsaturated fatty acids.The present work with fibroblasts from patients with a specific Acyl-CoA Oxidase deficiency, previously shown to have a deficient peroxisomal clofibrate-inducible Acyl-CoA Oxidase, and which accumulate 24:0 and 26:0 fatty acids, supports the vi…

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  • Peroxisomal β-oxidation of Polyunsaturated Long Chain Fatty Acids in Human Fibroblasts. The Polyunsaturated and the Saturated Long Chain Fatty Acids are Retroconverted by the Same Acyl-CoA Oxidase
    Scandinavian Journal of Clinical and Laboratory Investigation, 1993
    Co-Authors: Erik Christensen, B. T. Poll-the, Rja Wanders, Berit Woldseth, Tor-arne Hagve, H. Sprecher, Oddvar Stokke, Bjørn O. Christophersen

    Abstract:

    The metabolism of the C22 unsaturated fatty acids erucic acid (22:1(n-9)), adrenic acid (22:4(n-6)), docosapentaenoic acid (22:5(n-3)) and docosahexaenoic acid (22:6(n-3)) was studied in cultured fibroblasts from patients with Acyl-CoA Oxidase deficiency, the Zellweger syndrome, X-linked adrenoleukodystrophy (X-ALD) and normal controls. [3-14C] 22:4 (n-6) and [3-14C] 22:5 (n-3) were shortened (retroconverted) to [1-14C] 20:4 (n-6) and [1-14C] 20:5 (n-3), respectively, in normal and X-ALD fibroblasts. In Zellweger and Acyl-CoA Oxidase deficient fibroblasts these reactions were deficient. Since the retroconversion is normal in X-ALD fibroblasts peroxisomal very long chain (lignoceryl) CoA ligase is probably not required for the activation of C22 unsaturated fatty acids. The present work with fibroblasts from patients with a specific Acyl-CoA Oxidase deficiency, previously shown to have a deficient peroxisomal clofibrate-inducible Acyl-CoA Oxidase, and which accumulate 24:0 and 26:0 fatty acids, supports the view that this enzyme is responsible for the chain-shortening of docosahexaenoic acid (22:6(n-3)), erucic acid (22:1(n-9)), docosapentaenoic acid (22:5(n-3)), and adrenic acid (22:4(n-6)) as wel

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  • Peroxisomal beta-oxidation of polyunsaturated long chain fatty acids in human fibroblasts. The polyunsaturated and the saturated long chain fatty acids are retroconverted by the same Acyl-CoA Oxidase.
    Scandinavian journal of clinical and laboratory investigation. Supplementum, 1993
    Co-Authors: Erik Christensen, B. T. Poll-the, Berit Woldseth, Tor-arne Hagve, H. Sprecher, Oddvar Stokke, R J Wanders, Bjørn O. Christophersen

    Abstract:

    The metabolism of the C22 unsaturated fatty acids erucic acid (22:1(n-9)), adrenic acid (22:4(n-6)), docosapentaenoic acid (22:5(n-3)) and docosahexaenoic acid (22:6(n-3)) was studied in cultured fibroblasts from patients with Acyl-CoA Oxidase deficiency, the Zellweger syndrome, X-linked adrenoleukodystrophy (X-ALD) and normal controls. [3-14C] 22:4 (n-6) and [3-14C] 22:5 (n-3) were shortened (retroconverted) to [1-14C] 20:4 (n-6) and [1-14C] 20:5 (n-3), respectively, in normal and X-ALD fibroblasts. In Zellweger and Acyl-CoA Oxidase deficient fibroblasts these reactions were deficient. Since the retroconversion is normal in X-ALD fibroblasts peroxisomal very long chain (lignoceryl) CoA ligase is probably not required for the activation of C22 unsaturated fatty acids. The present work with fibroblasts from patients with a specific Acyl-CoA Oxidase deficiency, previously shown to have a deficient peroxisomal clofibrate-inducible Acyl-CoA Oxidase, and which accumulate 24:0 and 26:0 fatty acids, supports the view that this enzyme is responsible for the chain-shortening of docosahexaenoic acid (22:6(n-3)), erucic acid (22:1(n-9)), docosapentaenoic acid (22:5(n-3)), and adrenic acid (22:4(n-6)) as well.

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