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Literature summary for 1.3.3.6 extracted from

  • Tamaoki, H.; Setoyama, C.; Miura, R.; Hazekawa, I.; Nishina, Y.; Shiga, K.
    Spectroscopic studies of rat liver acyl-CoA oxidase with reference to recognition and activation of substrate (1997), J. Biochem., 121, 1139-1146.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
ACO-I and ACO-II Rattus norvegicus
expression in Escherichia coli Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
3-ketoacyl-CoA substrate analogues complex formation with anionic forms of 3-ketoacyl-CoA Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
Rattus norvegicus 5777
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
two isoforms: ACO-I, ACO-II
-

Purification (Commentary)

Purification (Comment) Organism
ACO-i and ACO-II, recombinant from Escherichia coli Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2 structural analysis of enzyme complexed with 3-ketoacyl-CoA substrate analogues Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + O2 isoform ACO-I prefers short-chain acyl-CoA substrates, isoform ACO-II prefers long-chain acyl-CoA substrates Rattus norvegicus trans-2,3-dehydroacyl-CoA + H2O2
-
?

Synonyms

Synonyms Comment Organism
ACO-I
-
Rattus norvegicus
ACO-II
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
FAD
-
Rattus norvegicus