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Literature summary for 1.3.3.6 extracted from

  • Adham, A.R.; Zolman, B.K.; Millius, A.; Bartel, B.
    Mutations in Arabidopsis acyl-CoA oxidase genes reveal distinct and overlapping roles in beta-oxidation (2005), Plant J., 41, 859-874.
    View publication on PubMed

Application

Application Comment Organism
additional information inability of ACX1, ACX3, and ACX4 to fully compensate for one another in indole-3-butyric acid-mediated root elongation inhibition and ability of ACX2 and ACX5 to contribute to indole-3-butyric acid response suggests that indole-3-butyric acid-response defects in acx mutants may reflect indirect blocks in peroxisomal metabolism and indole-3-butyric acid beta-oxidation, rather than direct enzymatic activity of ACX isozymes on indole-3-butyric acid-CoA Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information mutants defective in ACX1, ACX3, or ACX4 have reduced fatty acyl-CoA oxidase activity, acx1 acx2 double mutants display enhanced indole-3-butyric acid resistance and are sucrose dependent during seedling development, acx1 acx3 and acx1 acx5 double mutants display enhanced indole-3-butyric acid resistance but remain sucrose independent Arabidopsis thaliana

Inhibitors

Inhibitors Comment Organism Structure
indole-3-butyric acid inhibits root elongation Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
Col-0 accession
-

Source Tissue

Source Tissue Comment Organism Textmining
root
-
Arabidopsis thaliana
-
seedling
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + O2
-
Arabidopsis thaliana trans-2,3-dehydroacyl-CoA + H2O2
-
?

Synonyms

Synonyms Comment Organism
ACX1
-
Arabidopsis thaliana
ACX2
-
Arabidopsis thaliana
ACX3
-
Arabidopsis thaliana
ACX4
-
Arabidopsis thaliana
ACX5
-
Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
FAD
-
Arabidopsis thaliana