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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.3.3.6 - acyl-CoA oxidase and Organism(s) Caenorhabditis elegans and UniProt Accession O62137

for references in articles please use BRENDA:EC1.3.3.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.6 acyl-CoA oxidase
IUBMB Comments
A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Caenorhabditis elegans
UNIPROT: O62137
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acyl-coa oxidase, acox1, fatty acyl-coa oxidase, palmitoyl-coa oxidase, acyl-coa oxidase 1, acox2, peroxisomal fatty acyl-coa oxidase, acyl-coenzyme a oxidase, acyl-coenzyme a oxidase 1, pristanoyl-coa oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3alpha,7alpha, 12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
-
-
-
-
acyl coenzyme A oxidase
-
-
-
-
Acyl-CoA oxidase
-
-
-
-
AOX
-
-
-
-
BRCACox
-
-
-
-
fatty acyl-CoA oxidase
-
-
-
-
fatty acyl-coenzyme A oxidase
-
-
-
-
oxidase, acyl-coenzyme A
-
-
-
-
Peroxisomal fatty acyl-CoA oxidase
-
-
-
-
Pristanoyl-CoA oxidase
-
-
-
-
THCA-CoA oxidase
-
-
-
-
THCCox
-
-
-
-
Trihydroxycoprostanoyl-CoA oxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:oxygen 2-oxidoreductase
A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18.
CAS REGISTRY NUMBER
COMMENTARY hide
61116-22-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
ACOX-2 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of short-chain omega-ascarosides
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production
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
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
malfunction
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
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACX12_CAEEL
661
0
75091
Swiss-Prot
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ACOX-2, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview
ACOX-1, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview
ACOX-3, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Proc. Natl. Acad. Sci. USA
112
3955-3960
2015
Caenorhabditis elegans (O62137), Caenorhabditis elegans (O62138), Caenorhabditis elegans (O62140), Caenorhabditis elegans, Caenorhabditis elegans N2 (O62138)
Manually annotated by BRENDA team