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Enzyme Nomenclature
Information on EC 1.3.3.6 - acyl-CoA oxidase
for references in articles please use BRENDA:EC1.3.3.6
Word Map on EC 1.3.3.6
- 1.3.3.6
-
beta-oxidation
-
proliferator-activated
- catalase
-
ppars
- carnitine
- triglyceride
- hepatocytes
- cholesterol
-
pparalpha
-
thiolase
-
palmitoyltransferase
-
proliferators
- clofibrate
- steatosis
-
high-fat
- 3-ketoacyl-coa
-
enoyl-coa
- zellweger
-
receptor-alpha
-
medium-chain
- ciprofibrate
- adrenoleukodystrophy
-
hypolipidemic
- fenofibrate
- bezafibrate
- stearoyl-coa
-
fibrates
- refsum
-
cyanide-insensitive
-
phytanic
- 3-hydroxyacyl-coa
-
vlcfas
-
rxralpha
- cyp4a1
-
plasmalogens
-
pristanic
-
very-long-chain
- biotechnology
-
perfluorooctanoic
- 3-oxoacyl-coa
-
clofibrate-treated
-
rhizomelic
-
nafenopin
- nutrition
- degradation
-
2,4-dienoyl-coa
-
l-fabp
-
nongenotoxic
-
di2-ethylhexylphthalate
-
chondrodysplasia
-
peroxisome-proliferator
-
omega-oxidation
-
lignoceric
- medicine
- analysis
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.3.3.6
-
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RECOMMENDED NAME
GeneOntology No.
acyl-CoA oxidase
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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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
pK 233, inducible by growth on alkanes
-
-
Yarrowia lipolytica W29 / ATCC 20460
-
391040, 391041, 391042, 391043, 391044, 391045, 391046, 391071, 657279, 672370, 675738, 685352, 700546
-
-
3 forms: 1. inducible fatty acyl-CoA oxidase, 2. noninducible fatty acyl-CoA oxidase, 3. noninducible trihydroxycoprostanoyl-CoA oxidase
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
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
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
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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
-
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
-
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
?
-
-
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
?
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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
-
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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
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
-
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
-
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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
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
acox1 transcripts diffusely distributed in early-stage embryonic cells; acox1 transcripts diffusely distributed in early-stage embryonic cells
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
-
significant pretranslational up-regulation of acox1 expression in the anterior intestine after feeding
widely present at later stages, high levels of transcript variant ACOX1-3I; widely present at later stages, high levels of transcript variant ACOX1–3II
-
-
391039, 391040, 391042, 391043, 391044, 391045, 391046, 391047, 391048, 391067, 391068, 391071, 674364, 675738, 685352
ACX1 barely detectable; ACX3 expression less prominent compared to ACX2; predominant expression of ACX2
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
391039, 391041, 391042, 391043, 391044, 391045, 391046, 391047, 391048, 391067, 391068, 391071, 657279, 672370, 700546
-
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
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
-
6 * 69000, liver, SDS-PAGE, noninducible trihydroxyprostanoyl-CoA oxidase
homodimer
octamer
tetramer
?
-
? * 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
-
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
-
at 5°C from a 30% saturated ammonium sulfate solution, yellow rod-shaped crystals
-
cocrystallization of ACO-II with lauroyl-CoA by the hanging-drop vapor-diffusion method under oil, to 2.07 A resolution
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
-
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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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
-
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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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)
-
expression as His-tagged protein in Spodoptera frugiperda cells via infection with Baculovirus
-
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
-
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
-
expression of human ACOX1b isoform in a mouse ACOX1b mutant can reverse the null phenotype, overview
-
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
-
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
-
SCOX expression analysis in peroxisomal acyl-coenzyme A oxidase deficiency patients, overview
-
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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ENGINEERING
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
-
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
-
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
-
potential depolluting agent by degradation of oils; several biotechnological applications: production of metabolites, such as citrate, secretion of proteins, degradation of fatty acids
degradation
medicine
nutrition
-
engineering of plants with increased content of monocarboxylic fatty acids in this essential oil crop by enzyme overexpression
additional information
analysis
useful for the determination of free fatty acids
analysis
-
useful for the determination of free fatty acids
-
degradation
-
ACO activity in Beauveria bassiana depends on the carbon source used for growth and the chain length of the substrate utilized for the oxidation reaction
degradation
-
ACO activity in Beauveria bassiana depends on the carbon source used for growth and the chain length of the substrate utilized for the oxidation reaction
-
medicine
-
AOX activity is negatively correlated with postprandial triacylglycerol levels
medicine
-
ACOX1 is a rate-limiting enzyme in peroxisomal fatty acids beta-oxidation and its deficiency is associated with a lethal, autosomal recessive disease, called pseudoneonatal-adrenoleukodystrophy
additional information
-
isomerase activity of rat peroxisomal acyl-CoA oxidase I, is probably due to a spontaneous process driven by thermodynamic equilibrium with formation of a conjugated structure after deprotonation of substrate alpha-proton
additional information
-
nervonic acid is discharged from the spore into the external medium during firing along with the catalase and ACOX enzymes
additional information
-
novel Pex5pM is functional and a seven amino acids-insertion, which is present in the L isoform but absent in the M isoform, plays some role in the process of maturation of Aox
additional information
-
solvent-accessible acyl binding pocket is not required for oxygen reactivity, the oligomeric state plays a role in substrate pocket architecture but is not linked to oxygen reactivity
additional information
-
three distinct ACX genes, ACX1 is upregulated by wounding, both locally and systemically, ACX1 may play a role in the synthesis of jasmonic acid in response to wounding; three distinct ACX genes, expression of ACX2 remains unchanged by wounding, ACX2 may be involved in providing germinating seeds with sugar and energy; three distinct ACX genes, expression of ACX3 remains unchanged by wounding
additional information
three distinct ACX genes, ACX1 is upregulated by wounding, both locally and systemically, ACX1 may play a role in the synthesis of jasmonic acid in response to wounding; three distinct ACX genes, expression of ACX2 remains unchanged by wounding, ACX2 may be involved in providing germinating seeds with sugar and energy; three distinct ACX genes, expression of ACX3 remains unchanged by wounding
additional information
three distinct ACX genes, ACX1 is upregulated by wounding, both locally and systemically, ACX1 may play a role in the synthesis of jasmonic acid in response to wounding; three distinct ACX genes, expression of ACX2 remains unchanged by wounding, ACX2 may be involved in providing germinating seeds with sugar and energy; three distinct ACX genes, expression of ACX3 remains unchanged by wounding
additional information
-
ACOX1 alternative splicing isoforms play a key conserved role in the vertebrate fatty acid metabolism, tissue-specific modulation of ACOX1 activity by exchanging exon 3 duplicated isoforms containing amino acid sequences that are potentially implicated in fatty acyl chain specificity; ACOX1 alternative splicing isoforms play a key conserved role in the vertebrate fatty acid metabolism, tissue-specific modulation of ACOX1 activity by exchanging exon 3 duplicated isoforms containing amino acid sequences that are potentially implicated in fatty acyl chain specificity
additional information
ACOX1 alternative splicing isoforms play a key conserved role in the vertebrate fatty acid metabolism, tissue-specific modulation of ACOX1 activity by exchanging exon 3 duplicated isoforms containing amino acid sequences that are potentially implicated in fatty acyl chain specificity; ACOX1 alternative splicing isoforms play a key conserved role in the vertebrate fatty acid metabolism, tissue-specific modulation of ACOX1 activity by exchanging exon 3 duplicated isoforms containing amino acid sequences that are potentially implicated in fatty acyl chain specificity
additional information
-
inability of ACX1, ACX3, and ACX4 to fully compensate for one another in indole-3-butyric acid-mediated root elongation inhibition and ability of ACX2 and ACX5 to contribute to indole-3-butyric acid response suggests that indole-3-butyric acid-response defects in acx mutants may reflect indirect blocks in peroxisomal metabolism and indole-3-butyric acid beta-oxidation, rather than direct enzymatic activity of ACX isozymes on indole-3-butyric acid-CoA
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