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Information on EC 1.3.3.6 - acyl-CoA oxidase
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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
-
pparalpha
-
thiolase
-
palmitoyltransferase
-
proliferators
- adipose
- clofibrate
-
high-fat
- sterol
- steatosis
-
enoyl-coa
- 3-ketoacyl-coa
-
hypolipidemic
- zellweger
- ciprofibrate
- fenofibrate
-
medium-chain
- adrenoleukodystrophy
-
receptor-alpha
-
rxralpha
- stearoyl-coa
-
plasmalogens
-
cyanide-insensitive
- bezafibrate
-
fibrates
- refsum
-
vlcfas
- 3-hydroxyacyl-coa
- cyp4a1
-
very-long-chain
-
srebp-1c
-
pristanic
-
phytanic
-
peroxisome-proliferator
-
nongenotoxic
- 3-oxoacyl-coa
-
perfluorooctanoic
-
2,4-dienoyl-coa
-
omega-oxidation
- medicine
-
lignoceric
- analysis
-
di2-ethylhexylphthalate
-
l-fabp
-
rhizomelic
- biotechnology
- degradation
- nutrition
-
clofibrate-treated
-
nafenopin
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acox1, fatty acyl-coa oxidase, palmitoyl-coa oxidase, peroxisomal fatty acyl-coa oxidase, acyl-coenzyme a oxidase, acyl-coa oxidase 1, pristanoyl-coa oxidase, trihydroxycoprostanoyl-coa oxidase, acyl-coenzyme a oxidase 1, acyl coenzyme a oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3alpha,7alpha, 12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
-
-
-
-
ACO
ACO-A1
ACOX
ACOX-3
ACOX1
ACX
ACX1
ACX1.2
also known as ACX5, its substrate preference overlaps considerably with ACX1 for long chain acyl-CoA substrates and influences jasmonic acid synthesis
ACX2
ACX3
ACX4
acyl coenzyme A oxidase
-
-
-
-
Acyl-CoA oxidase
acyl-CoA oxidase 1
acyl-CoA oxidase 4
acyl-coenzyme A oxidase
acyl-coenzyme A oxidase 1
acyl-coenzyme A: oxygen oxidoreductase
AOX
Aox3p
Aoxp
BRCACox
-
-
-
-
fatty acyl-CoA oxidase
-
-
-
-
fatty acyl-coenzyme A oxidase
-
-
-
-
MCAD Y375K
-
Y375K mutant of medium-chain acyl-CoA dehydrogenase that exhibits acyl-CoA oxidase activity
oxidase, acyl-coenzyme A
-
-
-
-
Peroxisomal fatty acyl-CoA oxidase
-
-
-
-
Pristanoyl-CoA oxidase
-
-
-
-
SCOX
THCA-CoA oxidase
-
-
-
-
THCCox
-
-
-
-
Trihydroxycoprostanoyl-CoA oxidase
-
-
-
-
ACX1
preference for medium to long chain acyl-CoAs and jasmonic acid-CoA
Acyl-CoA oxidase
-
-
-
-
AOX
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
acts on CoA derivatives of fatty acids with chain length from 8 to 18
-
-
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA; stereochemistry of the reaction
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
anti-elimination of pro-2R and pro-3R hydrogens of acyl-CoA; stereochemistry of the reaction
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
inducible by growth on di-(2-ethylhexyl)phthalate
-
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
genetic regulation
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
mechanism, substrate binding site, and active site structure
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
structural analysis of enzyme complexed with 3-ketoacyl-CoA substrate analogues
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
in the reductive half-reaction, the substrate acyl-CoA isalpha,beta-dehydrogenated into the corresponding 2-trans-enoyl-CoA, with electrons transferred to FAD, which becomes reduced, whereas in the oxidative half-reaction reduced FAD is reoxidized by molecular oxygen, generating hydrogen peroxide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate biosynthesis (6-desaturase), (5Z)-dodecenoate biosynthesis II, 10-cis-heptadecenoyl-CoA degradation (yeast), 10-trans-heptadecenoyl-CoA degradation (reductase-dependent, yeast), 6-gingerol analog biosynthesis (engineered), 9-cis, 11-trans-octadecadienoyl-CoA degradation (isomerase-dependent, yeast), crotonyl-CoA/ethylmalonyl-CoA/hydroxybutyryl-CoA cycle (engineered), docosahexaenoate biosynthesis III (6-desaturase, mammals), fatty acid beta-oxidation (peroxisome, yeast), fatty acid beta-oxidation II (peroxisome), fatty acid beta-oxidation V (unsaturated, odd number, di-isomerase-dependent), fatty acid beta-oxidation VI (peroxisome), jasmonic acid biosynthesis, methyl ketone biosynthesis (engineered), oleate beta-oxidation (isomerase-dependent, yeast), propanoyl-CoA degradation II
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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.
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CAS REGISTRY NUMBER
COMMENTARY
61116-22-1
-
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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
cis-3-hexenoyl-CoA + O2
?
-
best substrate for the isomerase activity of the enzyme
-
-
?
dec-4-trans-enoyl-CoA + O2
2-trans-4-trans-decadienoyl-CoA + H2O2
-
-
-
?
furylpropionyl-CoA + O2
furylacryloyl-CoA + H2O2
-
also oxidizes aromatic/heterocyclic ring-substituted chromogenic substrates
-
?
jasmonic acid-CoA + O2
?
preferred substrate of ACX1
-
-
?
octadecanoyl-CoA + O2
?
preferred substrate of ACX2
-
-
?
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
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
-
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
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
-
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
-
both isoforms ACX1.1 and 1.2 show similar broad substrate specificities
-
-
?
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
-
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
-
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
-
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
-
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
-
isoform SCOX prefers C4-C8 substrates, isoform MCOX prefers C10-C14 substrates
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-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
-
-
?
hexanoyl-CoA + O2
(2E)-hex-2-enoyl-CoA + H2O2
AtSACX shows preference for
-
-
?
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
-
-
?
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
preferred substrate of ACX1
-
-
?
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
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
-
-
-
-
?
palmitoyl-CoA + O2
trans-2,3-dehydropalmitoyl-CoA
-
isozyme ACOX1b shows higher activity than isozyme ACOX1a
-
-
?
additional information
?
-
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
-
additional information
?
-
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
-
additional information
?
-
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)
-
-
-
additional information
?
-
-
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)
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
-
-
-
additional information
?
-
exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
exhibits high activity towards acyl-CoAs with chain lenghths of C12-C18
-
-
-
additional information
?
-
-
rate-limiting enzyme of the peroxisomal beta-oxidation spiral
-
-
-
additional information
?
-
rate-limiting enzyme of the peroxisomal beta-oxidation spiral
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
-
additional information
?
-
-
Eucalyptus terpenes elevate hepatic AOX expression in possum
-
-
-
additional information
?
-
-
Aox2p expression regulates the size of cellular triacylglycerol pools and the size and number of intracellular lipid bodies in which these gatty acids accumulate
-
-
-
additional information
?
-
no activity with hexadecanoyl-CoA and 3-methylheptadecanoyl-CoA
-
-
-
additional information
?
-
-
no activity with hexadecanoyl-CoA and 3-methylheptadecanoyl-CoA
-
-
-
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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
P0CZ23
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
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
O62137, O62138, O62140
-
-
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
O62137, O62138, O62140
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
O62137, O62138, O62140
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
O62138
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
-
significance in metabolism of alkanes of Candida tropicalis
-
-
?
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
-
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
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
?
acyl-CoA + O2
trans-2,3-dehydroacyl-CoA + H2O2
-
involved in lignin degradative system
-
-
?
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
-
involved in beta-oxidation of fatty acids in peroxisomes and glyoxysomes, respectively
-
-
?
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
-
-
-
additional information
?
-
-
each ACX enzyme acts on specific chain-length targets, but in a partially overlapping manner, indicating a degree of functional redundancy
-
-
-
additional information
?
-
-
rate-limiting enzyme of the peroxisomal beta-oxidation spiral
-
-
-
additional information
?
-
Q8HYL8
rate-limiting enzyme of the peroxisomal beta-oxidation spiral
-
-
-
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
-
additional information
?
-
-
Eucalyptus terpenes elevate hepatic AOX expression in possum
-
-
-
additional information
?
-
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
8 mol FAD per mol of enzyme, 1 mol FAD per mol of subunit; flavoprotein
FAD
flavoenzyme with 1 mol FAD per subunit; one molecule of non-covalently bound FAD per subunit as a prosthetic group
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10,12-tricosadiynoic acid-CoA
-
TDYA-CoA, development of the specific inhibitor of acyl-CoA oxidase-1, the acetylenic acid is a suicide substrate of ACOX1 with high affinity to the target and high selectivity in vivo. TDYA-CoA rapidly inhibits ACOX1 activity in vitro by 92% and in vivo, but only if free TDYA is activated as the CoA thioester, the substrate form. Inhibition of ACOX1 by TDYA-CoA is irreversible, inhibition kinetics parameters KI and kinact are calculated to be 680 nM and 3.18/min, respectively. It is possible that TDYA-CoA forms a covalent bond with a key residue in the catalytic center of ACOX1 and irreversibly inhibits the enzyme. Isozyme ACOX2 activity is not affected by the compound
-
3-ketoacyl-CoA substrate analogues
-
complex formation with anionic forms of 3-ketoacyl-CoA
5,5'-dithiobis(2-nitro-benzoic acid)
-
inactivates by modification of sulfhydryl groups and loss of FAD
Mg2+
no effect on enzyme activity up to 20 mM, inhibitory above, 40% inhibition at 30 mM
oct-2-en-4-ynoyl-CoA
-
irreversible inactivation, pH dependent, higher under basic condition
phenol
-
high concentration, magnitude of inhibition depends on the nature of the acyl-CoA substrate
additional information
-
glutathione protects against inhibition with sulfhydryl reagents
-
N-ethylmaleimide
shows less than 10% activity in the presence of 10 mM at 37°C for 4 h
N-ethylmaleimide
-
shows less than 10% activity in the presence of 10 mM at 37 °C for 4 h
N-ethylmaleimide
ACO retains more than 60% of the initial activity in the presence of 10 mM N-ethylmaleimide, at 37°C for 4 h; purified enzyme retains more than 60% activity in the presence of 10 mM at 37°C for 4 h, while other commercially available ACOs show only less than 10% activities after the same treatment
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
enhances acyl-CoA oxidation, avoids H2O2 consumption by endogenous catalase
bovine serum albumin
-
slightly increases ACO activity, maximum value of ACO acitvity at 0.036 mM
-
CoA
co-treatment with ACX1 and CoA significantly promoted the biosynthesis of gamma-decalactone compared to the control
growth hormone
-
increases the mRNA of acyl CoA oxidase, directly induces the expression of AOX in adipocytes through STAT5A binding to the -1841 to -1825 site within the AOX promoter
-
jasmonate
upregulates expression of ACX1, starts 4 h after treatment and remains elevated until 24 h
n-Alkane
-
increases ACO activity progressively with palmitoyl-CoA by 23%, with stearoyl-CoA by 42%, with behenoyl-CoA by 47% and with lignoceroyl-CoA by 75%
-
perilla oil
-
elevates AOX activity in a 4-day fedding, the effect is gradually decreased in a 4-week feeding
-
phenol
-
low concentration, magnitude of activation depends on the nature of the acyl-CoA substrate
propionate
-
increase in propionate concentration lead to increase of enzyme amount
tetracosane
-
stimulates, highest activity with lignoceroyl-CoA as substrate
additional information
-
no upregulation by jasmonate; no upregulation by jasmonate
-
additional information
no upregulation by jasmonate; no upregulation by jasmonate
-
additional information
no upregulation by jasmonate; no upregulation by jasmonate
-
additional information
exogenous application of recombinant PpACX1 and C16-CoA substrate markedly promots gamma-decalactone biosynthesis, while C16-CoA substrate application alone does not promote its biosynthesis in mesocarp discs cultured in vitro
-
additional information
-
exogenous application of recombinant PpACX1 and C16-CoA substrate markedly promots gamma-decalactone biosynthesis, while C16-CoA substrate application alone does not promote its biosynthesis in mesocarp discs cultured in vitro
-
additional information
-
AOX stimulation is highly associated with the content of long chain n-3 polyunsaturated fatty acids
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
overview: Km of several monocarboxylic and dicarboxylic acyl-CoA as substrates
-
additional information
additional information
Michaelis-Menten hyperbolic kinetic model
-
additional information
additional information
-
Michaelis-Menten hyperbolic kinetic model
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH-dependency of turnover number
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
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
60.9
purified enzyme; purified recombinant enzyme, at 37°C
additional information
additional information
-
isoform ACOX1a exhibits only 50% specific activity toward palmitoyl-CoA as compared to ACOX1b; 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
additional information
-
no activity in a second peroxisomal acyl-coenzyme A oxidase deficiency patient
additional information
-
overview: specific activity of enzyme from several sources with several substrates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
pH 7: about 30% of activity maximum, pH 10: about 5% of activity maximum, inactive below pH 6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
pK 233, inducible by growth on alkanes
-
-
brenda
five cvs., two soft melting peaches Hu Jing Mi Lu and Feng Hua Yu Lu with strong aroma, one hard melting peach Tai Gu Rou Tao with intermediate aroma, and two hard melting peaches Zhong Hua Shou Tao and Zhong Nectarine 16 with slight aroma
UniProt
brenda
Yarrowia lipolytica W29 / ATCC 20460
medium-chain specific isoform, MCOX, and short-chain specific isoform, SCOX
-
-
brenda
-
391040, 391041, 391042, 391043, 391044, 391045, 391046, 391071, 657279, 672370, 675738, 685352, 700546
-
-
brenda
3 forms: 1. inducible fatty acyl-CoA oxidase, 2. noninducible fatty acyl-CoA oxidase, 3. noninducible trihydroxycoprostanoyl-CoA oxidase
-
-
brenda
Yarrowia lipolytica W29 / ATCC 20460
six acyl-CoA oxidase isoenzymes encoded by genes POX1-POX6
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
real-time quantitative PCR enzyme expression analysis in fruit from the different cultivars
brenda
isozyme PpACX1 is the most abundant PpACX protein in fully ripe mesocarp of cultivar Hu Jing Mi Lu
brenda
additional information
discreetly expressed, lower levels of transcript variant ACOX1–3II, the ACOX1–3II transcript variant is expressed seven times more in brain than the ACOX1–3I variant; discreetly expressed, lower levels of transcript variant ACOX1-3I, the ACOX1-3I transcript variant is expressed seven times less in brain than the ACOX1-3II variant
brenda
acox1 transcripts diffusely distributed in early-stage embryonic cells; acox1 transcripts diffusely distributed in early-stage embryonic cells
brenda
widely present at later stages, high levels of transcript variant ACOX1–3II in the anterior intestine, significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding; widely present at later stages, high levels of transcript variants ACOX1-3I in the anterior intestine, significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding
brenda
-
significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding
brenda
widely present at later stages, high levels of transcript variant ACOX1-3I; widely present at later stages, high levels of transcript variant ACOX1–3II
brenda
-
-
391039, 391040, 391042, 391043, 391044, 391045, 391046, 391047, 391048, 391067, 391068, 391071, 674364, 675738, 685352, 745377
brenda
ACX1 barely detectable; ACX3 expression less prominent compared to ACX2; predominant expression of ACX2
brenda
additional information
-
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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
fluorescent protein-tagging points to a peroxisomal location of CrACX2
brenda
-
-
391039, 391041, 391042, 391043, 391044, 391045, 391046, 391047, 391048, 391067, 391068, 391071, 657279, 672370, 700546, 745377
brenda
-
existence of two independent, Pex5p-mediated import pathways into peroxisomes in yeast: 1. a classical peroxisomal targeting signal 1 pathway and a novel, non-PTS1 pathway for Pox1p
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of the acyl-CoA oxidase/dehydrogenase superfamily
malfunction
metabolism
physiological function
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
malfunction
-
deletion of gene aoxA leads to reduced growth on long chain fatty acids, but growth is not abolished by this mutation
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
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
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; mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production; 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
-
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
-
mutations in the acyl-CoA oxidase genes acox-1, -2, and -3 lead to specific defects in ascaroside production
-
metabolism
-
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
-
ACOX1 is the first and rate-limiting enzyme of the peroxisomal beta-oxidation pathway
metabolism
-
the enzyme is involved in the peroxisomal beta-oxidation pathway
metabolism
-
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; 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; 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
-
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
Yarrowia lipolytica W29 / ATCC 20460
-
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
-
physiological function
-
involved in fatty acid oxidation, essential energy generation
physiological function
-
ACOX1b controls the spontaneous hepatic peroxisome proliferation
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
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
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
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; 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; 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
-
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
-
Show AA Sequence and Transmembrane Helices (224 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Yarrowia lipolytica (strain CLIB 122 / E 150)
Yarrowia lipolytica (strain CLIB 122 / E 150)
Yarrowia lipolytica (strain CLIB 122 / E 150)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22500
-
? * 52000 + ? * 22500, liver, SDS-PAGE, inducible fatty acyl-CoA oxidase
45000
52000
-
? * 52000 + ? * 22500, liver, SDS-PAGE, inducible fatty acyl-CoA oxidase
69000
-
6 * 69000, liver, SDS-PAGE, noninducible trihydroxyprostanoyl-CoA oxidase
72000
75000
139000
140000
-
native AtACX1 and AtACX2, and recombinant AtACX1, gel filtration
150000
190000
gel filtration; gel filtration, recombinant enzyme
75000
2 * 75000; 2 * 75000; 2 * 75000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
-
6 * 69000, liver, SDS-PAGE, noninducible trihydroxyprostanoyl-CoA oxidase
homodimer
octamer
tetramer
?
x * 94440, recombinant enzyme including the pET32a vector encoding a 20.10 kDa protein, MALDITOF/TOF secondary mass spectrometry, x * 74340, sequence calculation and SDS-PAGE
?
-
? * 52000 + ? * 22500, liver, SDS-PAGE, inducible fatty acyl-CoA oxidase
homodimer
2 * 75000; 2 * 75000; 2 * 75000
homodimer
-
2 * 75000, SDS-PAGE; 2 * 95000, gel filtration
-
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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
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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
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at 5°C from a 30% saturated ammonium sulfate solution, yellow rod-shaped crystals
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cocrystallization of ACO-II with lauroyl-CoA by the hanging-drop vapor-diffusion method under oil, to 2.07 A resolution
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native ACO-II, hanging-drop vapor-diffusion method with 3% (w/v) polyethylene glycol 20000 as precipitant in 20 mM potassium phosphate, pH 7.4; X-ray structure analysis
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to 2.74 A resolution by vapor diffusion hanging-drop method, unusual packing arrangement of the tomato AXC1 enzyme as compared to other ACX enzymes, three monomers of ACX1 are present in the asymmetric unit
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G432R
-
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
-
naturally occuring apparent homozygous missense mutation c.629G/A of SCOX in a peroxisomal acyl-coenzyme A oxidase deficiency patient
C159T
60% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
C159T/C420S
activity less than one tenth of that of the wild type
C159T/C424V
activity less than one tenth of that of the wild type
C420S
41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
C420S/424V
activity less than one tenth of that of the wild type
C424V
98% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; 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; exhibits 60% activity of the wild-type enzyme, looses more than half of the activity after incubation with N-ethylmaleimide
-
C420S
-
41% activity compared to the wild type enzyme and shows increased sensitivity to N-ethylmaleimide; exhibits 41% activity of the wild-type enzyme, retains about 90% of the activity after incubation with N-ethylmaleimide
-
C424V
-
looses more than half of the activity after incubation with N-Ethylmaleimide
-
E421A
E421D
E421Q
T138I
-
compromised in wound-response signaling owing to a deficiency in jasmonic acid synthesis, FAD is not bound in the mutant protein
additional information
E421D
-
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
-
isomerase activity is decreased for all tested cis- and trans-substrates compared with that of wild-type enzyme
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
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; 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
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; 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
-
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
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
-
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
-
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
-
OAF1-gene disrupted construct with reduced number of peroxisomes, no longer inducible by oleate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
60
-
30 min, with butyryl-CoA and FAD, 50% loss of activity; 30 min, with butyryl-CoA, without FAD, 85% loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, in presence of 35% v/v glycerol, stable for at least 1 year
-80°C, wild-type enzyme and mutant enzymes E421D, E421A, E421Q and E421G are stable for 3 months
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37°C, 0.2 M potassium phosphate (pH 7.5) containing 0.1 M FAD, 4 h, less than 10% loss of activity
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
by gel filtration; Q-Sepharose column chromatography and CM-Sepharose column chromatography
partially
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
ACOX-1, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview; ACOX-2, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview; ACOX-3, quantitative RT-PCR expression analysis, Comparison of ascaroside production and expression levels of acyl-CoA oxidase genes under different conditions, overview
cloned into a bacterial expression vector pLM1 with six continous His codons attached to the 5' end of the gene, overexpression of wild-type ands mutant enzymes E421D, E421A, E421Q and E421G in Escherichia coli
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expressed in Escherichia coli JM109 cells; into vector pUTE300, expression in Escherichia coli JM109
expressed in Escherichia coli strains BL21 and C41, and in COS-7 cells (His-tagged enzyme)
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expression as His-tagged protein in Spodoptera frugiperda cells via infection with Baculovirus
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expression in Escherichia coli
expression in Escherichia coli as an active, N-terminal tagged His6 fusion protein
expression in Escherichia coli of 2 genes: ACX1.1 and ACX1.2, sequence comparison with other species
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expression in Escherichia coli of His-tagged proteins: AtSACX, AtACX1, and AtACX3, sequence analysis also with AtACX2
expression of AtACX1 and AtACX2 in Escherichia coli; plant anti-sense constructs, investigation of substrate specificities and regulation
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expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the null phenotype, overview
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gene ACX1, real-time quantitative PCR enzyme expression analysis in fruit from the different cultivars, recombinant expression of His-tagged enzyme in from vector pET32a in Escherichia coli
gene aoxA, seuence comparisons, recombinant expression from plasmid in Aspergillus nidulans strain MH11036, complementation of enzyme deficient aoxADELTA strain MH11074, expression as GFP-tagged enzyme showing PexE-dependent peroxisomal localisation
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gene Cre05.g232002 or CrACX2, screening of a Chlamydomonas insertional mutant library identifies a strain strongly impaired in oil remobilization and defective in Cre05.g232002 (CrACX2), recombinant expression of CrACX2 in Escherichia coli. Overexpression of GFP-tagged enzyme in Chlamydomonas reinhardtii peroxisomes
genes POX1-POX6, heterologous co-expression of the different isozymes with polyhydroxyalkanoate synthase (phaC) of Pseudomonas aeruginosa in Yarrowia lipolytica strains, subcloning in Escherichia coli
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SCOX expression analysis in peroxisomal acyl-coenzyme A oxidase deficiency patients, overview
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sequence analysis
transformed SK32 cells stably expressing one of the wild type Pex5p isoforms, Pex5pM and S restore the processing of Aox, but Pex5pL does not
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high temperature and low food availability conditions induce the expression of acox-2 and/or acox-3 and lead to corresponding changes in ascaroside production
-
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high temperature and low food availability conditions induce the expression of acox-2 and/or acox-3 and lead to corresponding changes in ascaroside production; high temperature and low food availability conditions induce the expression of acox-2 and/or acox-3 and lead to corresponding changes in ascaroside production