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1,16-hexadecadioyl-CoA + O2
?
-
-
-
-
?
16-hydroxy-palmitoyl-CoA + O2
?
-
-
-
-
?
2-oxoheptadecyldethio-CoA + O2
?
-
-
-
-
?
4,8,12-trimethyl-tridecanoyl-CoA + O2
?
-
-
-
-
?
4-methyl-nonanoyl-CoA + O2
?
-
-
-
-
?
6-phenyl-6-phenyl-hexanoyl-CoA + O2
?
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
acyl-CoA + O2
trans-2-enoyl-CoA + H2O2
-
assay at 25°C
-
-
ir
arachidoyl-CoA + O2
2-trans-eicosenoyl-CoA + H2O2
-
-
-
-
?
behenoyl-CoA + O2
2-trans-docosenoyl-CoA + H2O2
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
cis-3-decenoyl-CoA + O2
?
-
-
-
-
?
cis-3-hexenoyl-CoA + O2
?
-
best substrate for the isomerase activity of the enzyme
-
-
?
cis-3-octenoyl-CoA + O2
?
-
-
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
dec-4-trans-enoyl-CoA + O2
2-trans-4-trans-decadienoyl-CoA + H2O2
-
-
-
?
decanoyl-CoA + O2
trans-2,3-dehydrodecanoyl-CoA + H2O2
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
dicarboxylic acid-CoAs with 6-16 carbon atoms + O2
?
-
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
dodecanoyl-CoA + O2
trans-dodec-2-enoyl-CoA + H2O2
-
-
-
-
r
eicosapentaenoyl-CoA + O2
?
-
-
-
-
?
furylpropionyl-CoA + O2
furylacryloyl-CoA + H2O2
-
also oxidizes aromatic/heterocyclic ring-substituted chromogenic substrates
-
?
hexadecanedioyl-CoA + O2
?
hexadecanoyl-CoA + O2
trans-2,3-dehydrohexadecanoyl-CoA + H2O2
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
indole-3-butyric acid-CoA + O2
?
-
-
-
-
?
jasmonic acid-CoA + O2
?
preferred substrate of ACX1
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
leukodiacetyl-2,7-dichlorofluorescein + O2
?
-
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
nonanoyl-CoA + O2
trans-2-nonenoyl-CoA + H2O2
-
-
-
-
?
octadecanoyl-CoA + O2
?
preferred substrate of ACX2
-
-
?
octanoyl-CoA + O2
trans-2,3-dehydrooctanoyl-CoA + H2O2
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA + H2O2
pristanoyl-CoA + O2
trans-2,3-dehydropristanoyl-CoA + H2O2
-
-
-
?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
trans-3-decenoyl-CoA + O2
?
-
-
-
-
?
trans-3-hexenoyl-CoA + O2
?
-
-
-
-
?
trans-3-octenoyl-CoA + O2
?
-
-
-
-
?
trihydroxycholestanoyl-CoA + O2
trans-2,3-dehydrotrihydroxycholestanoyl-CoA + H2O2
-
-
-
?
trihydroxycoprostanoyl-CoA + O2
?
-
-
-
-
?
additional information
?
-
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
-
-
-
?
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
-
-
?
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
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
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
ACOX-3 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of (omega-1)-ascarosides
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
ACOX-3 serves as specialized acyl-CoA oxidase that promotes the biosynthesis of (omega-1)-ascarosides
-
-
?
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
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
specificity: C4-C20 acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
significance in metabolism of alkanes of Candida tropicalis
-
-
?
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
the purified recombinant CrACX2 expressed in Escherichia coli catalyzes the oxidation of fatty acyl-CoAs into trans-2-enoyl-CoA and produces H2O2
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
enzyme acts selectively on fatty acyl-CoA with 16 or 18 carbon atoms, cis-9-unsaturated esters with a C16 or C18 acyl moiety being converted with higher rate than saturated or polyunsaturated fatty acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
Cucurbita sp.
-
preference for long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
Cucurbita sp.
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
highly specific for short-chain fatty acids
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
both isoforms ACX1.1 and 1.2 show similar broad substrate specificities
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
preference for C12-C18 acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
key enzyme of beta-oxidation. A basal level of long chain ACX is always present along the barley life cycle, while a higher level of expression is typical of actively growing tissues such as germinating embryos, ovary before anthesis, developing embryos, shoots and root apexes. The enzyme plays a role not only during oil reserve mobilization, but also in plant growth and metabolism
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
preference for long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
involved in lignin degradative system
-
-
?
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
-
-
-
?
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
-
3'-phosphate on the ribose ring and the structure of the adenine moiety are essential for substrate recognition, specificity is relatively low with respect to the structure of the pantric acid moiety
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
isoform ACO-I prefers short-chain acyl-CoA substrates, isoform ACO-II prefers long-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
chain-length specificity changes with acyl-CoA concentration used
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
most active towards C12-C18 acyl-CoA, C20 and C22 acyl-CoA also oxidized, C4 and C6 acyl-CoA hardly oxidized
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
C4-C18 monocarboxylic acid-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
C6-C16 dicarboxylic-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
beta-oxidation of dicarboxylic acid-CoAs in rat liver is carried out exclusively in peroxisomes
-
-
?
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
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
C8-C18 acyl CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
long- and short-chain acyl-CoA substrates
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
long- and short-chain acyl-CoA substrates
-
-
?
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
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
medium-chain-length specific
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
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
-
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
isoform SCOX prefers C4-C8 substrates, isoform MCOX prefers C10-C14 substrates
-
?
behenoyl-CoA + O2
2-trans-docosenoyl-CoA + H2O2
-
-
-
-
?
behenoyl-CoA + O2
2-trans-docosenoyl-CoA + H2O2
-
-
-
-
?
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
-
-
-
-
?
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
-
-
-
-
?
butyryl-CoA + O2
trans-2-butenoyl-CoA + H2O2
-
-
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
-
-
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
-
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
-
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
-
-
-
-
?
decanoyl-CoA + O2
trans-2-decenoyl-CoA + H2O2
-
-
-
?
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
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
-
-
-
-
?
dodecanoyl-CoA + O2
(2E)-dodec-2-enoyl-CoA + H2O2
-
-
-
?
hexadecanedioyl-CoA + O2
?
-
-
-
-
?
hexadecanedioyl-CoA + O2
?
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
AtSACX shows preference for
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
-
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
-
-
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
-
recombinant enzyme
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
-
low activity
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
binding mode of C12-fatty acid suggests that the active site does not close upon substrate binding, but remains spacious during the entire catalytic process, the oxygen accessibility in the oxidative half-reaction thereby being maintained
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
-
-
-
-
?
lauroyl-CoA + O2
trans-2-dodecenoyl-CoA + H2O2
-
-
-
-
?
lignoceroyl-CoA + O2
?
-
-
-
-
?
lignoceroyl-CoA + O2
?
-
-
-
-
?
lignoceroyl-CoA + O2
?
-
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
-
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
-
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
-
AtACX1
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
preferred substrate of ACX1
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
highest activity
-
-
ir
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
maximum activity
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
highest activity
-
-
ir
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
-
-
-
-
?
myristoyl-CoA + O2
trans-2-tetradecenoyl-CoA + H2O2
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
-
-
-
-
?
octanoyl-CoA + O2
trans-2-octenoyl-CoA + H2O2
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
-
-
-
-
?
oleoyl-CoA + O2
2-trans-9-trans-octadecendienoyl-CoA + H2O2
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
?, ir
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
-
ir
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
?, ir
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
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?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
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-
-
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?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
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-
-
-
?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
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-
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r
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
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-
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?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
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isozyme ACOX1b shows higher activity than isozyme ACOX1a
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?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
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-
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?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA + H2O2
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-
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?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA + H2O2
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-
-
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?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA + H2O2
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-
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?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
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AtACX2
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?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
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?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
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-
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?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
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-
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?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
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-
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?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
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-
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?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
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-
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?
stearoyl-CoA + O2
trans-2-octadecenoyl-CoA + H2O2
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-
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?
additional information
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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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additional information
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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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additional information
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isoform ACX1 shows preference for C12-C16-CoA substrates and then C18 substrates, exhibiting a peak of activity with C16 acyl-CoA, but shows a little activity with short-chain (C6) acyl-CoA and very long-chain acyl-CoA (C20)
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additional information
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isoform ACX1 shows preference for C12-C16-CoA substrates and then C18 substrates, exhibiting a peak of activity with C16 acyl-CoA, but shows a little activity with short-chain (C6) acyl-CoA and very long-chain acyl-CoA (C20)
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additional information
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POX4-encoded acyl-CoA oxidase shows activities to broad substrates from short-chain or long-chain fatty acids, but POX5-encoded acyl-CoA oxidase shows activities to narrow substrate spectrum such (C10 and C12)
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additional information
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POX4-encoded acyl-CoA oxidase shows activities to broad substrates from short-chain or long-chain fatty acids, but POX5-encoded acyl-CoA oxidase shows activities to narrow substrate spectrum such (C10 and C12)
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additional information
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POX4-encoded acyl-CoA oxidase shows activities to broad substrates from short-chain or long-chain fatty acids, but POX5-encoded acyl-CoA oxidase shows activities to narrow substrate spectrum such (C10 and C12)
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additional information
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CrACX2 is more active toward long chain acyl-CoAs (C18:1-, C18:0-, C20:0-, C16:0-CoAs) than to medium chain acyl-CoA (C12:0-CoA)
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?
additional information
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CrACX2 is more active toward long chain acyl-CoAs (C18:1-, C18:0-, C20:0-, C16:0-CoAs) than to medium chain acyl-CoA (C12:0-CoA)
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?
additional information
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ACOX-1 interacts with PEX-5 in peroxisomes
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additional information
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ACOX-1 interacts with PEX-5 in peroxisomes
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additional information
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isoform ACOX1 is responsible for the oxidation of straight-chain fatty acids with different chain lengths
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additional information
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isoform ACOX1 is responsible for the oxidation of straight-chain fatty acids with different chain lengths
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additional information
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isoform ACOX1 is responsible for the oxidation of straight-chain fatty acids with different chain lengths
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additional information
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isoform ACOX1 is responsible for the oxidation of straight-chain fatty acids with different chain lengths
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additional information
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isoform ACOX2 is the only human acyl-CoA oxidase involved in bile acid biosynthesis, and is involved in the degradation of the branched-chain fatty acids
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additional information
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isoform ACOX2 is the only human acyl-CoA oxidase involved in bile acid biosynthesis, and is involved in the degradation of the branched-chain fatty acids
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additional information
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isoform ACOX2 is the only human acyl-CoA oxidase involved in bile acid biosynthesis, and is involved in the degradation of the branched-chain fatty acids
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additional information
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isoform ACOX2 is the only human acyl-CoA oxidase involved in bile acid biosynthesis, and is involved in the degradation of the branched-chain fatty acids
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additional information
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isoform ACOX3 is involved in the degradation of the branched-chain fatty acids
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additional information
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isoform ACOX3 is involved in the degradation of the branched-chain fatty acids
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additional information
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isoform ACOX3 is involved in the degradation of the branched-chain fatty acids
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additional information
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isoform ACOX3 is involved in the degradation of the branched-chain fatty acids
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additional information
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high activity toward acyl-CoAs with a chain length of C12-C18, inactive with short chain acyl-CoAs with a chain length of C4 and C6
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-
?
additional information
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high activity toward acyl-CoAs with a chain length of C12-C18, inactive with short chain acyl-CoAs with a chain length of C4 and C6
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-
?
additional information
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exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
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?
additional information
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exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
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?
additional information
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high activity toward acyl-CoAs with a chain length of C12-C18, inactive with short chain acyl-CoAs with a chain length of C4 and C6
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?
additional information
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exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
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?
additional information
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rate-limiting enzyme of the peroxisomal beta-oxidation spiral
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?
additional information
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rate-limiting enzyme of the peroxisomal beta-oxidation spiral
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?
additional information
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PpACX1 exhibits activity with medium- to long-chain fatty acyl-CoAs, equally for C10-CoA to C16-CoA. Isozyme PpACX1 activity using C6-CoA and C10-CoA as substrates is relatively lower and both maintains constant during the reaction time, while a linear activity with C16-CoA substrate is observed
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?
additional information
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PpACX1 exhibits activity with medium- to long-chain fatty acyl-CoAs, equally for C10-CoA to C16-CoA. Isozyme PpACX1 activity using C6-CoA and C10-CoA as substrates is relatively lower and both maintains constant during the reaction time, while a linear activity with C16-CoA substrate is observed
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?
additional information
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key enzyme for the beta-oxidation of fatty acids
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?
additional information
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Eucalyptus terpenes elevate hepatic AOX expression in possum
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?
additional information
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Aox2p expression regulates the size of cellular triacylglycerol pools and the size and number of intracellular lipid bodies in which these gatty acids accumulate
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?
additional information
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no activity with hexadecanoyl-CoA and 3-methylheptadecanoyl-CoA
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?
additional information
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no activity with hexadecanoyl-CoA and 3-methylheptadecanoyl-CoA
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?
additional information
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isoform ACOX3 exhibits activity for short-chain acyl-CoAs (C4-C10)
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additional information
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the enzyme prefers short-chain dicarboxylyl-CoAs as a substrate
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additional information
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the enzyme prefers short-chain dicarboxylyl-CoAs as a substrate
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additional information
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the enzyme prefers short-chain dicarboxylyl-CoAs as a substrate
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additional information
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isoform ACOX3 exhibits activity for short-chain acyl-CoAs (C4-C10)
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additional information
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structural and functional comparison of isoforms with each other and enzymes from other species, regulatory aspects
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?
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evolution
the enzyme is a member of the acyl-CoA oxidase/dehydrogenase superfamily
additional information
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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
malfunction
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deletion of gene aoxA leads to reduced growth on long chain fatty acids, but growth is not abolished by this mutation
malfunction
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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
malfunction
isolation of a mutant strain strongly impaired in oil remobilization and defective in gene CrACX2, under nitrogen depletion the mutant accumulated 20% more oil than the wild-type. The cracx2 mutant is impaired in fatty acid turnover during day/night cycles. The mutant strain is defective in beta-oxidation of fatty acids and cannot grow on oleic acid. The cracx2 mutant does not over-accumulate acyl-CoAs. Phenotype, overview
malfunction
mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production
malfunction
mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production. The acox-1 mutant produces an increased amount of asc-C9 and a reduced amount of asc-DELTAC9. Worms with mutations in acox-1 have a less severe phenotype, overview. They produce very little asc-omegaC3, asc-C5, asc-DELTAC7, and asc-DELTAC9 and, instead, accumulate asc-omegaC5 and asc-C9, implicating ACOX-1 in the beta-oxidation of both omega- and (omega-1)-ascarosides
malfunction
specific inhibition of ACOX1 by 10,12-tricosadiynoic acid increases hepatic mitochondrial fatty acid oxidation via activation of the adenosine 5'-monophosphate-activated protein kinase (SIRT1-AMPK) pathway and proliferator activator receptor alpha and reduces hydrogen peroxide accumulation in high fat diet-fed rats, which significantly decreases hepatic lipid and ROS contents, reduces body weight gain, and decreases serum triglyceride and insulin levels. The phosphorylation level of p70S6K (Thr389) in the livers of TDYA-treated rats decreases by 49% compared with the high-fat diet group
malfunction
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enzyme knockdown results in a lethal phenotype of the infective stage and likely developmental parasitic larval stage within host animals
malfunction
isoform ACOX2 deficiency leads to a Zellweger spectrum disorder lacking functional peroxisomes
malfunction
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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
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malfunction
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enzyme knockdown results in a lethal phenotype of the infective stage and likely developmental parasitic larval stage within host animals
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malfunction
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mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production
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metabolism
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ACOX1 is the first and rate-limiting enzyme of the peroxisomal beta-oxidation pathway
metabolism
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SCOX is the first enzyme of the peroxisomal beta-oxidation system and is involved in the oxidation of various fatty acids including very-long-chain fatty acids, long-chain dicarboxylic acids and polyunsaturated fatty acids, but not branched-chain fatty acids such as pristanic acid and the C27-bile acid intermediates
metabolism
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the enzyme is involved in the peroxisomal beta-oxidation pathway
metabolism
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the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview
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
metabolism
the enzyme participates in the biosynthesis of jasmonic acid in tea
metabolism
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the isozymes are involved in the beta-oxidation in peroxisomes. Aox3p function is responsible for 90% and 75% of the total polyhydroxyalkanoate produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of polyhydroxyalkanoate from C9:0 fatty acid. Other Aox isozymes, such as Aox1p, Aox2p, Aox4p and Aox6p, play no significant role in PHA biosynthesis, independent of the chain length of the fatty acid used, leaky-hose pipe beta-oxidation cycle model in Yarrowia lipolytica, overview
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metabolism
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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
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physiological function
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involved in fatty acid oxidation, essential energy generation
physiological function
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ACOX1b controls the spontaneous hepatic peroxisome proliferation
physiological function
acyl-CoA oxidase 1 is involved in gamma-decalactone release from Prunus persica fruits. gamma-Decalactone accumulation in peach mesocarp is highly correlated with ACX enzyme activity and natural PpACX1 content. Adding the purified recombinant PpACX1 induces gamma-decalactone biosynthesis in cultured mesocarp discs in vitro
physiological function
acyl-CoA oxidase-1 (ACOX1) is a flavoenzyme that catalyzes the initial and rate-determining reaction of the classical peroxisomal fatty acid oxidation using straight-chain fatty acyl-CoAs as the substrates, which donates electrons to molecular oxygen generating hydrogen peroxide
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. ACOX-1 is required in the first step of the beta-oxidation cycle that processes a 9-carbon (omega-1)-side chain to a 7-carbon (omega-1)-side chain. Roles of the ACOX-1/ACOX-3 heterodimer and ACOX-1/ACOX-2 heterodimer in ascaroside biosynthesis, 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
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-3 heterodimer in ascaroside biosynthesis, overview
physiological function
CrACX2 is a genuine acyl-CoA oxidase, which is responsible for the first step of the peroxisomal fatty acid beta-oxidation spiral. The enzyme is required for breakdown of fatty acids during lipid remobilization
physiological function
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increased expression of isoform ACOX2 in the kidney along with increases in plasma phytanic acid and the altered gut microbiota may be involved in the oxidation in the kidney and the pathogenesis of hypertension
physiological function
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the enzyme plays an essential role in the post-embryonic larval development
physiological function
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the enzyme plays an essential role in the post-embryonic larval development
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physiological function
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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-3 heterodimer in ascaroside biosynthesis, overview
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G432R
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conversion of Aox from component A to components B and C is completely prevented at both 30°C and 37°C
G231V
the mutation in combination with skipping of exon 13 leads to peroxisomal acyl-CoA oxidase deficiency
R210H
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naturally occuring apparent homozygous missense mutation c.629G/A of SCOX in a peroxisomal acyl-coenzyme A oxidase deficiency patient
C159T/C420S
activity less than one tenth of that of the wild type
C159T/C420S/C424V
shows no activity at all
C159T/C424V
activity less than one tenth of that of the wild type
C420S/424V
activity less than one tenth of that of the wild type
C424V
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looses more than half of the activity after incubation with N-Ethylmaleimide
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E421G
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inactive mutant enzyme
Y232F
the mutant shows reduced activity compared to the wild type enzyme
Y232G
the mutant shows reduced activity compared to the wild type enzyme
Y232S
the mutant shows reduced activity compared to the wild type enzyme
Y401F
the mutant shows reduced activity compared to the wild type enzyme
Y401G
the inactive mutant shows no FAD binding
Y401S
the inactive mutant shows no FAD binding
T138I
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compromised in wound-response signaling owing to a deficiency in jasmonic acid synthesis, FAD is not bound in the mutant protein
C159T
exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
C159T
60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
C420S
exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
C420S
41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
C424V
looses more than half of the activity after incubation with N-Ethylmaleimide
C424V
98% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
C159T
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exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
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C159T
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60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
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C420S
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exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
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C420S
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41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide
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E421A
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inactive mutant enzyme
E421A
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does not show any isomerase activity
E421D
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Km-value for octanoyl-CoA is 1.23fold higher than the wild-type value. The turnover number for octanoyl-CoA is 1.6fold lower than activity of the wild-type enzyme
E421D
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isomerase activity is decreased for all tested cis- and trans-substrates compared with that of wild-type enzyme
E421Q
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inactive mutant enzyme
E421Q
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does not show any isomerase activity
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
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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
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the ibr3-1 acx3-4 double mutant shows greatly enhanced indole-3-butyric acid resistance
additional information
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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
additional information
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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
-
additional information
screening of a Chlamydomonas reinhardtii insertional mutant library identifies a strain strongly impaired in oil remobilization and defective in Cre05.g232002 (CrACX2), Nb7D4 is disrupted in gene Cre05.g232002. The mutant strain is defective in beta-oxidation of fatty acids and cannot grow on oleic acid. Turnover of fatty acids during diurnal growth is compromised in cracx2 mutant cells. Cellular oil content is increased by 20% in cracx2 mutants during N starvation. Phenotype, overview
additional information
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screening of a Chlamydomonas reinhardtii insertional mutant library identifies a strain strongly impaired in oil remobilization and defective in Cre05.g232002 (CrACX2), Nb7D4 is disrupted in gene Cre05.g232002. The mutant strain is defective in beta-oxidation of fatty acids and cannot grow on oleic acid. Turnover of fatty acids during diurnal growth is compromised in cracx2 mutant cells. Cellular oil content is increased by 20% in cracx2 mutants during N starvation. Phenotype, overview
additional information
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ACOX1-/- mice show twofold increased expression of isozyme ACOX1a compared to wild-type mice, ACOX1b-/- and ACOX1a-/- phenotypes, overview. Expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the hepatic null phenotype, but with only weak reversal of the hepatic steatosis phenotype in the mice, overview. Expression of human isozyme ACOX1a has only poor effects
additional information
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OAF1-gene disrupted construct with reduced number of peroxisomes, no longer inducible by oleate
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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.
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Arabidopsis thaliana
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Arent, S.; Pye, V.E.; Henriksen, A.
Structure and function of plant acyl-CoA oxidases
Plant Physiol. Biochem.
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2008
Arabidopsis thaliana (O65201), Arabidopsis thaliana (O65202), Arabidopsis thaliana (P0CZ23), Arabidopsis thaliana (Q96329), Arabidopsis thaliana (Q9ZQP2)
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Sode, K.; Tsugawa, W.; Aoyagi, M.; Rajashekhara, E.; Watanabe, K.
Propionate sensor using coenzyme-A transferase and acyl-CoA oxidase
Protein Pept. Lett.
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2008
Arabidopsis thaliana
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Zeng, J.; Wu, L.; Zhang, X.; Liu, Y.; Deng, G.; Li, D.
Oct-2-en-4-ynoyl-CoA as a specific inhibitor of acyl-CoA oxidase
Org. Lett.
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Rattus norvegicus
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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
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2010
Homo sapiens
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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.
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Homo sapiens, Mus musculus
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Reiser, K.; Davis, M.A.; Hynes, M.J.
AoxA is a major peroxisomal long chain fatty acyl-CoA oxidase required for beta-oxidation in A. nidulans
Curr. Genet.
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Aspergillus nidulans
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Haddouche, R.; Delessert, S.; Sabirova, J.; Neuveglise, C.; Poirier, Y.; Nicaud, J.M.
Roles of multiple acyl-CoA oxidases in the routing of carbon flow towards beta-oxidation and polyhydroxyalkanoate biosynthesis in Yarrowia lipolytica
FEMS Yeast Res.
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Yarrowia lipolytica, Yarrowia lipolytica W29 / ATCC 20460
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Khan, B.R.; Adham, A.R.; Zolman, B.K.
Peroxisomal Acyl-CoA oxidase 4 activity differs between Arabidopsis accessions
Plant Mol. Biol.
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Arabidopsis thaliana, Arabidopsis thaliana Col-0
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Zeng, J.; Deng, S.; Wang, Y.; Li, P.; Tang, L.; Pang, Y.
Specific inhibition of acyl-CoA oxidase-1 by an acetylenic acid improves hepatic lipid and reactive oxygen species (ROS) metabolism in rats fed a high fat diet
J. Biol. Chem.
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2017
Rattus norvegicus (P07872)
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Zhang, L.; Li, H.; Gao, L.; Qi, Y.; Fu, W.; Li, X.; Zhou, X.; Gao, Q.; Gao, Z.; Jia, H.
Acyl-CoA oxidase 1 is involved in gamma-decalactone release from peach (Prunus persica) fruit
Plant Cell Rep.
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2017
Prunus persica (J7K6M3), Prunus persica
brenda
Kong, F.; Liang, Y.; Legeret, B.; Beyly-Adriano, A.; Blangy, S.; Haslam, R.P.; Napier, J.A.; Beisson, F.; Peltier, G.; Li-Beisson, Y.
Chlamydomonas carries out fatty acid beta-oxidation in ancestral peroxisomes using a bona fide acyl-CoA oxidase
Plant J.
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Chlamydomonas reinhardtii (A8J3M3), Chlamydomonas reinhardtii
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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
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3955-3960
2015
Caenorhabditis elegans (O62137), Caenorhabditis elegans (O62138), Caenorhabditis elegans (O62140), Caenorhabditis elegans, Caenorhabditis elegans N2 (O62138)
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Deng, S.; Li, P.; Wang, Y.; Zeng, J.
tyrosine residues 232 and 401 play a critical role in the binding of the cofactor FAD of acyl-CoA oxidase
Appl. Biochem. Biotechnol.
185
875-883
2018
Rattus norvegicus (P07872)
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Kim, S.; Kim, K.J.
Structural insight into the substrate specificity of acyl-CoA oxidase1 from Yarrowia lipolytica for short-chain dicarboxylyl-CoAs
Biochem. Biophys. Res. Commun.
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2018
Yarrowia lipolytica (O74934), Yarrowia lipolytica, Yarrowia lipolytica CLIB 122 (O74934)
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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.
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2018
Homo sapiens (O15254), Homo sapiens (Q15067), Homo sapiens (Q99424), Homo sapiens
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Ju, J.H.; Oh, B.R.; Heo, S.Y.; Lee, Y.U.; Shon, J.H.; Kim, C.H.; Kim, Y.M.; Seo, J.W.; Hong, W.K.
Production of adipic acid by short- and long-chain fatty acid acyl-CoA oxidase engineered in yeast Candida tropicalis
Bioprocess Biosyst. Eng.
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2020
Candida tropicalis (P06598), Candida tropicalis, Candida tropicalis KCTC 7212 (P06598)
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Kempinski, B.; Chelstowska, A.; Poznanski, J.; Krol, K.; Rymer, L.; Frydzinska, Z.; Girzalsky, W.; Skoneczna, A.; Erdmann, R.; Skoneczny, M.
The peroxisomal targeting signal 3 (PTS3) of the budding yeast acyl-CoA oxidase is a signal patch
Front. Cell Dev. Biol.
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198
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Saccharomyces cerevisiae
brenda
Okamura, M.; Ueno, T.; Tanaka, S.; Murata, Y.; Kobayashi, H.; Miyamoto, A.; Abe, M.; Fukuda, N.
Increased expression of acyl-CoA oxidase 2 in the kidney with plasma phytanic acid and altered gut microbiota in spontaneously hypertensive rats
Hypertens. Res.
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651-661
2021
Rattus norvegicus
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Kim, S.; Kim, K.J.
Crystal structure of acyl-CoA oxidase 3 from Yarrowia lipolytica with specificity for short-chain acyl-CoA
J. Microbiol. Biotechnol.
28
597-605
2018
Yarrowia lipolytica (O74936), Yarrowia lipolytica CLIB 122 (O74936)
brenda
Xin, Z.; Chen, S.; Ge, L.; Li, X.; Sun, X.
The involvement of a herbivore-induced acyl-CoA oxidase gene, CsACX1, in the synthesis of jasmonic acid and its expression in flower opening in tea plant (Camellia sinensis)
Plant Physiol. Biochem.
135
132-140
2019
Camellia sinensis (A0A222YU64), Camellia sinensis
brenda
Shi, H.; Huang, X.; Chen, X.; Yang, Y.; Wang, Z.; Yang, Y.; Wu, F.; Zhou, J.; Yao, C.; Ma, G.; Du, A.
Acyl-CoA oxidase ACOX-1 interacts with a peroxin PEX-5 to play roles in larval development of Haemonchus contortus
PLoS Pathog.
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e1009767
2021
Haemonchus contortus, Haemonchus contortus ZJ
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