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Information on EC 1.3.3.6 - acyl-CoA oxidase and Organism(s) Homo sapiens

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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.
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
-
-
-
-
ACOX
-
-
ACOX1
ACOX1a
-
isoform
ACOX1b
-
isoform
ACOX2
isoform
ACOX3
isoform
acyl coenzyme A oxidase
-
-
-
-
Acyl-CoA oxidase
-
-
-
-
acyl-CoA oxidase 1
-
-
acyl-CoA oxidase 1a
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isoform
acyl-CoA oxidase 1b
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isoform
acyl-CoA-oxidase
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AOX
-
-
-
-
BRCACox
-
-
-
-
fatty acyl-CoA oxidase
-
-
-
-
fatty acyl-coenzyme A oxidase
-
-
-
-
oxidase, acyl-coenzyme A
-
-
-
-
palmitoyl-CoA oxidase
-
-
peroxisomal acyl-coenzyme A oxidase
-
-
Peroxisomal fatty acyl-CoA oxidase
-
-
-
-
Pristanoyl-CoA oxidase
-
-
-
-
SCOX
-
-
straight chain acyl-CoA oxidase
-
straight-chain acyl-coenzyme A 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
1,16-hexadecadioyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
16-hydroxy-palmitoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
4,8,12-trimethyl-tridecanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
4-methyl-nonanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
6-phenyl-6-phenyl-hexanoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
show the reaction diagram
decanoyl-CoA + O2
trans-2,3-dehydrodecanoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
eicosapentaenoyl-CoA + O2
?
show the reaction diagram
-
-
-
-
?
hexadecanoyl-CoA + O2
trans-2,3-dehydrohexadecanoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
pristanoyl-CoA + O2
trans-2,3-dehydropristanoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
trihydroxycholestanoyl-CoA + O2
trans-2,3-dehydrotrihydroxycholestanoyl-CoA + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
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
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Detergents
-
inactiviation via dissociation of subunits
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.09
palmitoyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000016
-
activity in one peroxisomal acyl-coenzyme A oxidase deficiency patient, pH not specified in the publication, temperature not specified in the publication
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
optimal palmitoyl-CoA oxidase activity for ACOX1b
8.5
-
optimal palmitoyl-CoA oxidase activity for ACOX1a
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37.5
-
the ACOX1b isoform has a maximum specific activity around 37.5°C
40
-
the maximum specific activity for ACOX1a is obtained at 40°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
isoform ACOX2 deficiency leads to a Zellweger spectrum disorder lacking functional peroxisomes
metabolism
physiological function
-
ACOX1b controls the spontaneous hepatic peroxisome proliferation
additional information
-
adult peroxisomal acyl-coenzyme A oxidase deficiency, formerly also called pseudoneonatal adrenoleucodystrophy, is a disorder of peroxisomal fatty acid oxidation with a severe presentation with cerebellar and brainstem atrophy, phenotype, overview. Accumulation of very-long-chain fatty acids is the only diagnostic marker for SCOX deficiency
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACOX3_HUMAN
700
0
77629
Swiss-Prot
other Location (Reliability: 2)
ACOX1_HUMAN
660
0
74424
Swiss-Prot
other Location (Reliability: 2)
ACOX2_HUMAN
681
0
76827
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
-
? * 51000 + ? * 21000, recombinant enzyme, SDS-PAGE
51000
-
? * 51000 + ? * 21000, recombinant enzyme, SDS-PAGE
72000
-
x * 72000, SDS-PAGE
81000
-
isoform ACOX1a and ACOX1b, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G231V
the mutation in combination with skipping of exon 13 leads to peroxisomal acyl-CoA oxidase deficiency
R210H
-
naturally occuring apparent homozygous missense mutation c.629G/A of SCOX in a peroxisomal acyl-coenzyme A oxidase deficiency patient
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37.5 - 70
-
the ACOX1b isoform retains 57% of its specific activity at 50°C and is more resistant to heat denaturation than ACOX1a since it conserves 30% of its specific activity after treatment at 50°C, the isoform shows 70% specific activity at 37.5°C
50
-
the specific activity of isoform ACOX1a drops to zero at 50°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
partially
-
recombinant His-tagged from Spodoptera frugiperda cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strains BL21 and C41, and in COS-7 cells (His-tagged enzyme)
-
expressed in Saccharomyces cerevisiae
expression as His-tagged protein in Spodoptera frugiperda cells via infection with Baculovirus
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expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the null phenotype, overview
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SCOX expression analysis in peroxisomal acyl-coenzyme A oxidase deficiency patients, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
ACOX1 is a rate-limiting enzyme in peroxisomal fatty acids beta-oxidation and its deficiency is associated with a lethal, autosomal recessive disease, called pseudoneonatal-adrenoleukodystrophy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bronfman, M.; Inestrosa, N.C.; Nervi, F.O.; Leighton, F.
Acyl-CoA synthetase and the peroxisomal enzymes of beta-oxidation in human liver. Quantitative analysis of their subcellular localization
Biochem. J.
224
709-720
1984
Homo sapiens
Manually annotated by BRENDA team
Chu, R.; Varanasi, U.; Chu, S.; Lin, Y.; Usuda, N.; Rao, M.S.; Reddy, J.K.
Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells
J. Biol. Chem.
270
4908-4915
1995
Homo sapiens
Manually annotated by BRENDA team
Carrozzo, R.; Bellini, C.; Lucioli, S.; Deodato, F.; Cassandrini, D.; Cassanello, M.; Caruso, U.; Rizzo, C.; Rizza, T.; Napolitano, M.L.; Wanders, R.J.; Jakobs, C.; Bruno, C.; Santorelli, F.M.; Dionisi-Vici, C.; Bonioli, E.
Peroxisomal acyl-CoA-oxidase deficiency: two new cases
Am. J. Med. Genet. A
146A
1676-1681
2008
Homo sapiens (Q15067), Homo sapiens
Manually annotated by BRENDA team
Oaxaca-Castillo, D.; Andreoletti, P.; Vluggens, A.; Yu, S.; van Veldhoven, P.P.; Reddy, J.K.; Cherkaoui-Malki, M.
Biochemical characterization of two functional human liver acyl-CoA oxidase isoforms 1a and 1b encoded by a single gene
Biochem. Biophys. Res. Commun.
360
314-319
2007
Homo sapiens
Manually annotated by BRENDA team
Ferdinandusse, S.; Barker, S.; Lachlan, K.; Duran, M.; Waterham, H.; Wanders, R.; Hammans, S.
Adult peroxisomal acyl-coenzyme A oxidase deficiency with cerebellar and brainstem atrophy
J. Neurol. Neurosurg. Psychiatry
81
310-312
2010
Homo sapiens
Manually annotated by BRENDA team
Vluggens, A.; Andreoletti, P.; Viswakarma, N.; Jia, Y.; Matsumoto, K.; Kulik, W.; Khan, M.; Huang, J.; Guo, D.; Yu, S.; Sarkar, J.; Singh, I.; Rao, M.S.; Wanders, R.J.; Reddy, J.K.; Cherkaoui-Malki, M.
Reversal of mouse acyl-CoA oxidase 1 (ACOX1) null phenotype by human ACOX1b isoform [corrected]
Lab. Invest.
90
696-708
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Ferdinandusse, S.; Denis, S.; van Roermund, C.W.T.; Preece, M.A.; Koster, J.; Ebberink, M.S.; Waterham, H.R.; Wanders, R.J.A.
A novel case of ACOX2 deficiency leads to recognition of a third human peroxisomal acyl-CoA oxidase
Biochim. Biophys. Acta Mol. Basis Dis.
1864
952-958
2018
Homo sapiens (O15254), Homo sapiens (Q15067), Homo sapiens (Q99424), Homo sapiens
Manually annotated by BRENDA team