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Literature summary for 1.3.3.6 extracted from

  • 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 (2007), Biochem. Biophys. Res. Commun., 360, 314-319.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
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 Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strains BL21 and C41, and in COS-7 cells (His-tagged enzyme) Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.073
-
palmitoyl-CoA isoform ACOX1a Homo sapiens
0.09
-
palmitoyl-CoA isoform ACOX1b Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
81000
-
isoform ACOX1a and ACOX1b, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
isoform ACOX1a exhibits only 50% specific activity toward palmitoyl-CoA as compared to ACOX1b Homo sapiens
additional information
-
specific activities in units/mg for isoform ACOX1a: 0.186 for eicosapentaenoyl-CoA, 0.237 for 4-methyl-nonanoyl-CoA, 0.15 for 16-hydroxy-palmitoyl-CoA, 0.336 for 4,8,12-trimethyl-tridecanoyl-CoA, 0.372 for 1,16-hexadecadioyl-CoA, 0.699 for 6-phenyl-6-phenyl-hexanoyl-CoA, 0.076 for palmitoyl-CoA, specific activities in units/mg for isoform ACOX1b: 0.226 for eicosapentaenoyl-CoA, 0.278 for 4-methyl-nonanoyl-CoA, 0.298 for 16-hydroxy-palmitoyl-CoA, 0.423 for 4,8,12-trimethyl-tridecanoyl-CoA, 0.504 for 1,16-hexadecadioyl-CoA, 0.573 for 6-phenyl-6-phenyl-hexanoyl-CoA, 0.166 for palmitoyl-CoA Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,16-hexadecadioyl-CoA + O2
-
Homo sapiens ?
-
?
16-hydroxy-palmitoyl-CoA + O2
-
Homo sapiens ?
-
?
4,8,12-trimethyl-tridecanoyl-CoA + O2
-
Homo sapiens ?
-
?
4-methyl-nonanoyl-CoA + O2
-
Homo sapiens ?
-
?
6-phenyl-6-phenyl-hexanoyl-CoA + O2
-
Homo sapiens ?
-
?
acyl-CoA + O2
-
Homo sapiens trans-2,3-dehydroacyl-CoA + H2O2
-
?
eicosapentaenoyl-CoA + O2
-
Homo sapiens ?
-
?
palmitoyl-CoA + O2
-
Homo sapiens 2-trans-hexadecenoyl-CoA + H2O2
-
?

Synonyms

Synonyms Comment Organism
ACOX1a isoform Homo sapiens
ACOX1b isoform Homo sapiens
acyl-CoA oxidase 1a isoform Homo sapiens
acyl-CoA oxidase 1b isoform Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37.5
-
the ACOX1b isoform has a maximum specific activity around 37.5°C Homo sapiens
40
-
the maximum specific activity for ACOX1a is obtained at 40°C Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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 Homo sapiens
50
-
the specific activity of isoform ACOX1a drops to zero at 50°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8.5 optimal palmitoyl-CoA oxidase activity for ACOX1b Homo sapiens
8.5
-
optimal palmitoyl-CoA oxidase activity for ACOX1a Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Homo sapiens