EC Number   |
General Information |
Reference |
|---|
    1.3.3.6 | evolution |
the enzyme is a member of the acyl-CoA oxidase/dehydrogenase superfamily |
746084 |
| 1.3.3.6 | malfunction |
deletion of gene aoxA leads to reduced growth on long chain fatty acids, but growth is not abolished by this mutation |
724805 |
| 1.3.3.6 | malfunction |
enzyme knockdown results in a lethal phenotype of the infective stage and likely developmental parasitic larval stage within host animals |
-, 765668 |
| 1.3.3.6 | malfunction |
isoform ACOX2 deficiency leads to a Zellweger spectrum disorder lacking functional peroxisomes |
764225 |
| 1.3.3.6 | 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 |
746084 |
| 1.3.3.6 | malfunction |
mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production |
-, 746305 |
| 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 |
746305 |
| 1.3.3.6 | 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 |
745377 |
| 1.3.3.6 | malfunction |
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 |
-, 726186 |
| 1.3.3.6 | metabolism |
ACOX1 is the first and rate-limiting enzyme of the peroxisomal beta-oxidation pathway |
712913 |
