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evolution
the enzyme is a member of the acyl-CoA oxidase/dehydrogenase superfamily
additional information
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adult peroxisomal acyl-coenzyme A oxidase deficiency, formerly also called pseudoneonatal adrenoleucodystrophy, is a disorder of peroxisomal fatty acid oxidation with a severe presentation with cerebellar and brainstem atrophy, phenotype, overview. Accumulation of very-long-chain fatty acids is the only diagnostic marker for SCOX deficiency
malfunction
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deletion of gene aoxA leads to reduced growth on long chain fatty acids, but growth is not abolished by this mutation
malfunction
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the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type. Reducing ACX4 expression in several Arabidopsis backgrounds shows a split response, suggesting that the ACX4 gene and/or protein functions differently in Arabidopsis accessions, phenotypes, detailed overview. ACX2 levels are increased in acx1acx3acx4Col compared to Col-0 wild-type samples
malfunction
isolation of a mutant strain strongly impaired in oil remobilization and defective in gene CrACX2, under nitrogen depletion the mutant accumulated 20% more oil than the wild-type. The cracx2 mutant is impaired in fatty acid turnover during day/night cycles. The mutant strain is defective in beta-oxidation of fatty acids and cannot grow on oleic acid. The cracx2 mutant does not over-accumulate acyl-CoAs. Phenotype, overview
malfunction
mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production
malfunction
mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production. The acox-1 mutant produces an increased amount of asc-C9 and a reduced amount of asc-DELTAC9. Worms with mutations in acox-1 have a less severe phenotype, overview. They produce very little asc-omegaC3, asc-C5, asc-DELTAC7, and asc-DELTAC9 and, instead, accumulate asc-omegaC5 and asc-C9, implicating ACOX-1 in the beta-oxidation of both omega- and (omega-1)-ascarosides
malfunction
specific inhibition of ACOX1 by 10,12-tricosadiynoic acid increases hepatic mitochondrial fatty acid oxidation via activation of the adenosine 5'-monophosphate-activated protein kinase (SIRT1-AMPK) pathway and proliferator activator receptor alpha and reduces hydrogen peroxide accumulation in high fat diet-fed rats, which significantly decreases hepatic lipid and ROS contents, reduces body weight gain, and decreases serum triglyceride and insulin levels. The phosphorylation level of p70S6K (Thr389) in the livers of TDYA-treated rats decreases by 49% compared with the high-fat diet group
malfunction
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enzyme knockdown results in a lethal phenotype of the infective stage and likely developmental parasitic larval stage within host animals
malfunction
isoform ACOX2 deficiency leads to a Zellweger spectrum disorder lacking functional peroxisomes
malfunction
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the acx3acx4Col and acx1acx3acx4Col mutants are viable, enzyme activity in these mutants is significantly reduced on a range of substrates compared to the wild-type. Reducing ACX4 expression in several Arabidopsis backgrounds shows a split response, suggesting that the ACX4 gene and/or protein functions differently in Arabidopsis accessions, phenotypes, detailed overview. ACX2 levels are increased in acx1acx3acx4Col compared to Col-0 wild-type samples
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malfunction
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enzyme knockdown results in a lethal phenotype of the infective stage and likely developmental parasitic larval stage within host animals
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malfunction
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mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production
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metabolism
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ACOX1 is the first and rate-limiting enzyme of the peroxisomal beta-oxidation pathway
metabolism
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SCOX is the first enzyme of the peroxisomal beta-oxidation system and is involved in the oxidation of various fatty acids including very-long-chain fatty acids, long-chain dicarboxylic acids and polyunsaturated fatty acids, but not branched-chain fatty acids such as pristanic acid and the C27-bile acid intermediates
metabolism
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the enzyme is involved in the peroxisomal beta-oxidation pathway
metabolism
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the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview
metabolism
ascaroside pheromones and beta-oxidation enzymes implicated in their biosynthesis, model for the role of specific acyl-CoA oxidase homo- and heterodimers in the biosynthetic pathway of (omega-1)-ascarosides and omega-ascarosides, overview
metabolism
the enzyme participates in the biosynthesis of jasmonic acid in tea
metabolism
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the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview
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metabolism
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ascaroside pheromones and beta-oxidation enzymes implicated in their biosynthesis, model for the role of specific acyl-CoA oxidase homo- and heterodimers in the biosynthetic pathway of (omega-1)-ascarosides and omega-ascarosides, overview
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physiological function
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involved in fatty acid oxidation, essential energy generation
physiological function
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ACOX1b controls the spontaneous hepatic peroxisome proliferation
physiological function
acyl-CoA oxidase 1 is involved in gamma-decalactone release from Prunus persica fruits. gamma-Decalactone accumulation in peach mesocarp is highly correlated with ACX enzyme activity and natural PpACX1 content. Adding the purified recombinant PpACX1 induces gamma-decalactone biosynthesis in cultured mesocarp discs in vitro
physiological function
acyl-CoA oxidase-1 (ACOX1) is a flavoenzyme that catalyzes the initial and rate-determining reaction of the classical peroxisomal fatty acid oxidation using straight-chain fatty acyl-CoAs as the substrates, which donates electrons to molecular oxygen generating hydrogen peroxide
physiological function
Caenorhabditis elegans uses ascaroside pheromones to induce development of the stress-resistant dauer larval stage and to coordinate various behaviors. Peroxisomal beta-oxidation cycles are required for the biosynthesis of the fatty acid-derived side chains of the ascarosides. The three acyl-CoA oxidases, which catalyze the first step in these beta-oxidation cycles, form different protein homo- and heterodimers with distinct substrate preferences. When the acyl-CoA oxidases are expressed alone or in pairs and purified, the resulting acyl-CoA oxidase homo- and heterodimers display different side-chain length preferences in an in vitro activity assay. The ACOX isozymes 1, 2, and 3 are involved in the important mechanism by which Caenorhabditis elegans increases the production of the most potent dauer pheromones, those with the shortest side chains, under specific environmental conditions. An ACOX-1 homodimer controls the production of ascarosideswith side chains with nine or fewer carbons, an ACOX-1/ACOX-3 heterodimer controls the production of those with side chains with seven or fewer carbons, and an ACOX-2 homodimer controls the production of those with omega-side chains with less than five carbons. ACOX-1 is required in the first step of the beta-oxidation cycle that processes a 9-carbon (omega-1)-side chain to a 7-carbon (omega-1)-side chain. Roles of the ACOX-1/ACOX-3 heterodimer and ACOX-1/ACOX-2 heterodimer in ascaroside biosynthesis, overview
physiological function
Caenorhabditis elegans uses ascaroside pheromones to induce development of the stress-resistant dauer larval stage and to coordinate various behaviors. Peroxisomal beta-oxidation cycles are required for the biosynthesis of the fatty acid-derived side chains of the ascarosides. The three acyl-CoA oxidases, which catalyze the first step in these beta-oxidation cycles, form different protein homo- and heterodimers with distinct substrate preferences. When the acyl-CoA oxidases are expressed alone or in pairs and purified, the resulting acyl-CoA oxidase homo- and heterodimers display different side-chain length preferences in an in vitro activity assay. The ACOX isozymes 1, 2, and 3 are involved in the important mechanism by which Caenorhabditis elegans increases the production of the most potent dauer pheromones, those with the shortest side chains, under specific environmental conditions. An ACOX-1 homodimer controls the production of ascarosideswith side chains with nine or fewer carbons, an ACOX-1/ACOX-3 heterodimer controls the production of those with side chains with seven or fewer carbons, and an ACOX-2 homodimer controls the production of those with omega-side chains with less than five carbons. Role of the ACOX-1/ACOX-2 heterodimer in ascaroside biosynthesis, overview
physiological function
Caenorhabditis elegans uses ascaroside pheromones to induce development of the stress-resistant dauer larval stage and to coordinate various behaviors. Peroxisomal beta-oxidation cycles are required for the biosynthesis of the fatty acid-derived side chains of the ascarosides. The three acyl-CoA oxidases, which catalyze the first step in these beta-oxidation cycles, form different protein homo- and heterodimers with distinct substrate preferences. When the acyl-CoA oxidases are expressed alone or in pairs and purified, the resulting acyl-CoA oxidase homo- and heterodimers display different side-chain length preferences in an in vitro activity assay. The ACOX isozymes 1, 2, and 3 are involved in the important mechanism by which Caenorhabditis elegans increases the production of the most potent dauer pheromones, those with the shortest side chains, under specific environmental conditions. An ACOX-1 homodimer controls the production of ascarosideswith side chains with nine or fewer carbons, an ACOX-1/ACOX-3 heterodimer controls the production of those with side chains with seven or fewer carbons, and an ACOX-2 homodimer controls the production of those with omega-side chains with less than five carbons. . Role of the ACOX-1/ACOX-3 heterodimer in ascaroside biosynthesis, overview
physiological function
CrACX2 is a genuine acyl-CoA oxidase, which is responsible for the first step of the peroxisomal fatty acid beta-oxidation spiral. The enzyme is required for breakdown of fatty acids during lipid remobilization
physiological function
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increased expression of isoform ACOX2 in the kidney along with increases in plasma phytanic acid and the altered gut microbiota may be involved in the oxidation in the kidney and the pathogenesis of hypertension
physiological function
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the enzyme plays an essential role in the post-embryonic larval development
physiological function
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the enzyme plays an essential role in the post-embryonic larval development
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physiological function
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Caenorhabditis elegans uses ascaroside pheromones to induce development of the stress-resistant dauer larval stage and to coordinate various behaviors. Peroxisomal beta-oxidation cycles are required for the biosynthesis of the fatty acid-derived side chains of the ascarosides. The three acyl-CoA oxidases, which catalyze the first step in these beta-oxidation cycles, form different protein homo- and heterodimers with distinct substrate preferences. When the acyl-CoA oxidases are expressed alone or in pairs and purified, the resulting acyl-CoA oxidase homo- and heterodimers display different side-chain length preferences in an in vitro activity assay. The ACOX isozymes 1, 2, and 3 are involved in the important mechanism by which Caenorhabditis elegans increases the production of the most potent dauer pheromones, those with the shortest side chains, under specific environmental conditions. An ACOX-1 homodimer controls the production of ascarosideswith side chains with nine or fewer carbons, an ACOX-1/ACOX-3 heterodimer controls the production of those with side chains with seven or fewer carbons, and an ACOX-2 homodimer controls the production of those with omega-side chains with less than five carbons. . Role of the ACOX-1/ACOX-3 heterodimer in ascaroside biosynthesis, overview
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