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Information on EC 1.3.3.6 - acyl-CoA oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9ZQP2
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1.3.3.6 acyl-CoA oxidaseIUBMB Comments
A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18.
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Word Map
- 1.3.3.6
-
beta-oxidation
-
proliferator-activated
-
ppars
- carnitine
- catalase
- triglyceride
- hepatocytes
- cholesterol
- pparalpha
-
thiolase
- palmitoyltransferase
- steatosis
- adipose
- proliferators
-
high-fat
- sterol
- clofibrate
-
hypolipidemic
- enoyl-coa
- 3-ketoacyl-coa
- adrenoleukodystrophy
- ciprofibrate
- zellweger
- fenofibrate
- refsum
- bezafibrate
-
very-long-chain
-
perfluorooctanoic
- cyp4a1
- plasmalogens
-
pristanic
- srebp-1c
- 3-hydroxyacyl-coa
-
phytanic
-
fibrates
-
cyanide-insensitive
-
rxralpha
-
vlcfas
-
nafenopin
-
lignoceric
- medicine
- pmp70
-
rhizomelic
- 3-oxoacyl-coa
- nutrition
- degradation
- analysis
-
2,4-dienoyl-coa
-
omega-oxidation
- biotechnology
-
di2-ethylhexylphthalate
-
clofibrate-treated
-
peroxisome-proliferator
-
l-fabp
- peroxins
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACX1.2
also known as ACX5, its substrate preference overlaps considerably with ACX1 for long chain acyl-CoA substrates and influences jasmonic acid synthesis
3alpha,7alpha, 12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
-
-
-
-
ACX
ACX1
ACX2
ACX3
ACX4
acyl coenzyme A oxidase
-
-
-
-
Acyl-CoA oxidase
-
-
-
-
AOX
-
-
-
-
AtACX1
AtACX2
AtACX3
BRCACox
-
-
-
-
fatty acyl-CoA oxidase
-
-
-
-
fatty acyl-coenzyme A oxidase
-
-
-
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oxidase, acyl-coenzyme A
-
-
-
-
Peroxisomal fatty acyl-CoA oxidase
-
-
-
-
Pristanoyl-CoA oxidase
-
-
-
-
THCA-CoA oxidase
-
-
-
-
THCCox
-
-
-
-
Trihydroxycoprostanoyl-CoA oxidase
-
-
-
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ACX1
preference for medium to long chain acyl-CoAs and jasmonic acid-CoA
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
61116-22-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
AtSACX shows preference for
-
-
?
jasmonic acid-CoA + O2
?
preferred substrate of ACX1
-
-
?
octadecanoyl-CoA + O2
?
preferred substrate of ACX2
-
-
?
additional information
?
-
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
AtACX1 is medium-chain specific, AtACX2 is medium- to long-chain specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
AtACX3 is medium-chain-specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
AtACX3 is medium-chain-specific
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
AtACX1 is medium- to long-chain specific, AtSACXis strictly short-chain specific
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
AtACX3 and AtACX1 show preference for
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
preferred substrate of ACX3
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
propionate
-
increase in propionate concentration lead to increase of enzyme amount
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACO12_ARATH
664
0
74298
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
-
native AtACX1 and AtACX2, and recombinant AtACX1, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
acx1-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is unaltered in the acx1-1 mutant, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx1-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype, wound-induced increase in jasmonic acid is only compromised in the acx1-1 mutant
additional information
acx1-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is unaltered in the acx1-1 mutant, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx1-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype, wound-induced increase in jasmonic acid is only compromised in the acx1-1 mutant
additional information
acx1-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is unaltered in the acx1-1 mutant, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx1-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype, wound-induced increase in jasmonic acid is only compromised in the acx1-1 mutant
additional information
acx1-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is unaltered in the acx1-1 mutant, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx1-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype, wound-induced increase in jasmonic acid is only compromised in the acx1-1 mutant
additional information
acx2-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is slightly delayed in the acx2-1 mutant, with 3-day-old acx2-1 seedlings accumulating long-chain acyl-CoAs, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx2-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype
additional information
acx2-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is slightly delayed in the acx2-1 mutant, with 3-day-old acx2-1 seedlings accumulating long-chain acyl-CoAs, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx2-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype
additional information
acx2-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is slightly delayed in the acx2-1 mutant, with 3-day-old acx2-1 seedlings accumulating long-chain acyl-CoAs, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx2-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype
additional information
acx2-1 mutant, acx1-1 acx2-1 double mutant, lipid catabolism during germination and early post-germinative growth is slightly delayed in the acx2-1 mutant, with 3-day-old acx2-1 seedlings accumulating long-chain acyl-CoAs, seedlings of the double mutant acx1-1 acx2-1 are unable to catabolize seed storage lipid, accumulate long-chain acyl-CoAs, and are unable to establish photosynthetic competency in the absence of an exogenous carbon supply, germination frequency of the double mutant acx1-1 acx2-1 is significantly reduced compared with wild-type seeds, is improved by dormancy-breaking treatments, the acx2-1 and acx1-2 acx2-1 double mutants exhibit a sucrose-independent germination phenotype
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
additional information
-
the ibr3-1 acx3-4 double mutant shows greatly enhanced indole-3-butyric acid resistance
additional information
-
generation of higher-order acx mutants, 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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli of His-tagged proteins: AtSACX, AtACX1, and AtACX3, sequence analysis also with AtACX2
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
LITERATURE
additional information
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
additional information
solvent-accessible acyl binding pocket is not required for oxygen reactivity, the oligomeric state plays a role in substrate pocket architecture but is not linked to oxygen reactivity
additional information
-
solvent-accessible acyl binding pocket is not required for oxygen reactivity, the oligomeric state plays a role in substrate pocket architecture but is not linked to oxygen reactivity
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)
Hooks, M.A.; Kellas, F.; Graham, I.A.
Long-chain acyl-CoA oxidases of Arabidopsis
Plant J.
20
1-13
1999
Arabidopsis thaliana
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
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
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
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
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)
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
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)
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
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