Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Zhang, X.; Feng, L.; Chinta, S.; Singh, P.; Wang, Y.; Nunnery, J.K.; Butcher, R.A.
    Acyl-CoA oxidase complexes control the chemical message produced by Caenorhabditis elegans (2015), Proc. Natl. Acad. Sci. USA, 112, 3955-3960 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.3.6 ACOX-1, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview Caenorhabditis elegans
1.3.3.6 ACOX-2, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview Caenorhabditis elegans
1.3.3.6 ACOX-3, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.6 acyl-CoA + O2 Caenorhabditis elegans
-
 trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2 Caenorhabditis elegans ACOX-2 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of short-chain omega-ascarosides trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2 Caenorhabditis elegans ACOX-3 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of (omega-1)-ascarosides trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2 Caenorhabditis elegans N2 ACOX-3 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of (omega-1)-ascarosides trans-2,3-dehydroacyl-CoA + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.6 Caenorhabditis elegans O62137
-
-
1.3.3.6 Caenorhabditis elegans O62138
-
-
1.3.3.6 Caenorhabditis elegans O62140
-
-
1.3.3.6 Caenorhabditis elegans N2 O62138
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.6 acyl-CoA + O2
-
 Caenorhabditis elegans trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2 ACOX-2 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of short-chain omega-ascarosides Caenorhabditis elegans trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2 ACOX-3 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of (omega-1)-ascarosides Caenorhabditis elegans trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2
-
 Caenorhabditis elegans N2 trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2 ACOX-3 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of (omega-1)-ascarosides Caenorhabditis elegans N2 trans-2,3-dehydroacyl-CoA + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.3.6 ACOX-1
-
 Caenorhabditis elegans
1.3.3.6 ACOX-2
-
 Caenorhabditis elegans
1.3.3.6 ACOX-3
-
 Caenorhabditis elegans

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.3.6 FAD
-
 Caenorhabditis elegans

Expression

EC Number Organism Comment Expression
1.3.3.6 Caenorhabditis elegans high temperature and low food availability conditions induce the expression of acox-2 and/or acox-3 and lead to corresponding changes in ascaroside production up

General Information

EC Number General Information Comment Organism
1.3.3.6 malfunction mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production Caenorhabditis elegans
1.3.3.6 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 Caenorhabditis elegans
1.3.3.6 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 Caenorhabditis elegans
1.3.3.6 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 Caenorhabditis elegans
1.3.3.6 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 Caenorhabditis elegans
1.3.3.6 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 Caenorhabditis elegans