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Information on EC 1.3.3.6 - acyl-CoA oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession O65202

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     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.
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Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: O65202
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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, peroxisomal fatty acyl-coa oxidase, acyl-coenzyme a oxidase, acyl-coenzyme a oxidase 1, pristanoyl-coa oxidase, trihydroxycoprostanoyl-coa oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3alpha,7alpha, 12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
-
-
-
0
ACX1.2
284157
also known as ACX5, its substrate preference overlaps considerably with ACX1 for long chain acyl-CoA substrates and influences jasmonic acid synthesis
acyl coenzyme A oxidase
-
-
-
0
Acyl-CoA oxidase
-
-
-
0
acyl-CoA oxidase 1
302
-
acyl-CoA oxidase 4
302
-
AOX
-
-
-
0
AtACX1
AtACX2
AtACX3
AtSACX
280534
-
BRCACox
-
-
-
0
fatty acyl-CoA oxidase
-
-
-
0
fatty acyl-coenzyme A oxidase
-
-
-
0
long-chain-specific acyl-CoA oxidase 1
280532
-
oxidase, acyl-coenzyme A
-
-
-
0
Peroxisomal fatty acyl-CoA oxidase
-
-
-
0
Pristanoyl-CoA oxidase
-
-
-
0
short chain-specific acyl-CoA oxidase
280524
-
short-chain acyl-CoA oxidase
302
-
THCA-CoA oxidase
-
-
-
0
THCCox
-
-
-
0
Trihydroxycoprostanoyl-CoA oxidase
-
-
-
0
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
0
reduction
-
-
-
0
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
jasmonic acid-CoA + O2
?
show the reaction diagram
preferred substrate of ACX1
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
preferred substrate of ACX1
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
show the reaction diagram
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
show the reaction diagram
AtSACX shows preference for
-
-
?
indole-3-butyric acid-CoA + O2
?
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
show the reaction diagram
-
AtACX1
-
-
?
octadecanoyl-CoA + O2
?
show the reaction diagram
preferred substrate of ACX2
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
show the reaction diagram
-
AtACX2
-
-
?
additional information
?
-
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
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-
?
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
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
additional information
?
-
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
indole-3-butyric acid
-
inhibits root elongation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
propionate
-
increase in propionate concentration lead to increase of enzyme amount
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0157 - 0.0189
dodecanoyl-CoA
0.02
hexanoyl-CoA
isozyme AtSACX
0.0053
myristoyl-CoA
-
isozyme AtACX1
0.0044
stearoyl-CoA
-
isozyme AtACX2
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACOX1_ARATH
664
0
74302
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
-
native AtACX1 and AtACX2, and recombinant AtACX1, gel filtration
660000
-
recombinant AtACX2, aggregation in E. coli, gel filtration
74300
-
2 * 74300, AtACX1 and AtACX2, sequence determination
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 74300, AtACX1 and AtACX2, sequence determination
homotetramer
4 * 47000, ACX4
tetramer
crystallographic studies
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, the crystals diffract to 2.0 A using synchrotron radiation, have unit-cell parameters a = 85.2, b = 118.0, c = 131.0 A, alpha = beta = gamma = 90 and show P2(1)2(1)2(1) symmetry
by the hanging drop vapor diffusion technique, ACX4-acetoacetyl-CoA crystals to 2.7 A resolution, of His-tagged ACX4 to 3.9 A resolution
hanging-drop vapor-diffusion method, crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions, a = 85.6 A, b = 117.0 A, c = 1313.3 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration and anion exchange chromatography
recombinant from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL 21
expression in Escherichia coli of His-tagged proteins: AtSACX, AtACX1, and AtACX3, sequence analysis also with AtACX2
expression of AtACX1 and AtACX2 in Escherichia coli
-
into the pET24 vector and transformed into Escherichia coli BL21(DE3)
plant anti-sense constructs, investigation of substrate specificities and regulation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
amperometric propionate sensor
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Froman, B.E.; Edwards, P.C.; Bursch, A.G.; Dehesh, K.
ACX3, a novel medium-chain acyl-coenzyme A oxidase from Arabidopsis
Plant Physiol.
123
733-741
2000
Brassica napus, Arabidopsis thaliana (P0CZ23)
Manually annotated by BRENDA team
Hooks, M.A.; Kellas, F.; Graham, I.A.
Long-chain acyl-CoA oxidases of Arabidopsis
Plant J.
20
1-13
1999
Arabidopsis thaliana
Manually annotated by BRENDA team
Pedersen, L.; Henriksen, A.
Expression, purification and crystallization of two peroxisomal acyl-CoA oxidases from Arabidopsis thaliana
Acta Crystallogr. Sect. D
60
1125-1128
2004
Arabidopsis thaliana (O65202), Arabidopsis thaliana
Manually annotated by BRENDA team
Pedersen, L.; Henriksen, A.
Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism
J. Mol. Biol.
345
487-500
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Mackenzie, J.; Pedersen, L.; Arent, S.; Henriksen, A.
Controlling electron transfer in acyl-CoA oxidases and dehydrogenases
J. Biol. Chem.
281
31012-31020
2006
Arabidopsis thaliana (Q96329), Arabidopsis thaliana
Manually annotated by BRENDA team
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
Plant J.
41
859-874
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Pinfield-Wells, H.; Rylott, E.L.; Gilday, A.D.; Graham, S.; Job, K.; Larson, T.R.; Graham, I.A.
Sucrose rescues seedling establishment but not germination of Arabidopsis mutants disrupted in peroxisomal fatty acid catabolism
Plant J.
43
861-872
2005
Arabidopsis thaliana (O65201), Arabidopsis thaliana (O65202), Arabidopsis thaliana (P0CZ23), Arabidopsis thaliana (Q96329)
Manually annotated by BRENDA team
Zolman, B.K.; Nyberg, M.; Bartel, B.
IBR3, a novel peroxisomal acyl-CoA dehydrogenase-like protein required for indole-3-butyric acid response
Plant Mol. Biol.
64
59-72
2007
Arabidopsis thaliana
Manually annotated by BRENDA team
Arent, S.; Pye, V.E.; Henriksen, A.
Structure and function of plant acyl-CoA oxidases
Plant Physiol. Biochem.
46
292-301
2008
Arabidopsis thaliana (O65201), Arabidopsis thaliana (O65202), Arabidopsis thaliana (P0CZ23), Arabidopsis thaliana (Q96329), Arabidopsis thaliana (Q9ZQP2)
Manually annotated by BRENDA team
Sode, K.; Tsugawa, W.; Aoyagi, M.; Rajashekhara, E.; Watanabe, K.
Propionate sensor using coenzyme-A transferase and acyl-CoA oxidase
Protein Pept. Lett.
15
779-781
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Khan, B.R.; Adham, A.R.; Zolman, B.K.
Peroxisomal Acyl-CoA oxidase 4 activity differs between Arabidopsis accessions
Plant Mol. Biol.
78
45-58
2012
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Manually annotated by BRENDA team
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