Literature summary for 1.3.3.6 extracted from

Nakajima, Y.; Miyahara, I.; Hirotsu, K.; Nishina, Y.; Shiga, K.; Setoyama, C.; Tamaoki, H.; Miura, R.
Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase (2002), J. Biochem., 131, 365-374.

Search for more literature for 1.3.3.6

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment)	Organism
native ACO-II, hanging-drop vapor-diffusion method with 3% (w/v) polyethylene glycol 20000 as precipitant in 20 mM potassium phosphate, pH 7.4	Rattus norvegicus
X-ray structure analysis	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
native and recombinant ACO-II from Escherichia coli	Rattus norvegicus

Reaction

Reaction	Comment	Organism	Reaction ID
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2	mechanism, substrate binding site, and active site structure	Rattus norvegicus	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Rattus norvegicus	-

Subunits

Subunits	Comment	Organism
dimer	-	Rattus norvegicus

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
FAD	both subunits are involved in FAD-binding	Rattus norvegicus

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Release 2023.1 (January 2023)