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Information on EC 1.3.3.6 - acyl-CoA oxidase and Organism(s) Rattus norvegicus and UniProt Accession P07872
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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
- hepatocytes
- cholesterol
- pparalpha
-
thiolase
- palmitoyltransferase
- steatosis
- adipose
- proliferators
-
high-fat
- sterol
- clofibrate
-
hypolipidemic
- enoyl-coa
- 3-ketoacyl-coa
- adrenoleukodystrophy
- ciprofibrate
- zellweger
- fenofibrate
- refsum
- bezafibrate
-
very-long-chain
-
perfluorooctanoic
- cyp4a1
- plasmalogens
-
pristanic
- srebp-1c
- 3-hydroxyacyl-coa
-
phytanic
-
fibrates
-
cyanide-insensitive
-
rxralpha
-
vlcfas
-
nafenopin
-
lignoceric
- medicine
- pmp70
-
rhizomelic
- 3-oxoacyl-coa
- nutrition
- degradation
- analysis
-
2,4-dienoyl-coa
-
omega-oxidation
- biotechnology
-
di2-ethylhexylphthalate
-
clofibrate-treated
-
peroxisome-proliferator
-
l-fabp
- peroxins
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acyl-coa oxidase, acox1, fatty acyl-coa oxidase, palmitoyl-coa oxidase, acyl-coa oxidase 1, acox2, peroxisomal fatty acyl-coa oxidase, acyl-coenzyme a oxidase, acyl-coenzyme a oxidase 1, pristanoyl-coa oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3alpha,7alpha, 12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase
-
-
-
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acyl coenzyme A oxidase
-
-
-
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Acyl-CoA oxidase
AOX
BRCACox
-
-
-
-
fatty acyl-CoA oxidase
-
-
-
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fatty acyl-coenzyme A oxidase
-
-
-
-
MCAD Y375K
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Y375K mutant of medium-chain acyl-CoA dehydrogenase that exhibits acyl-CoA oxidase activity
oxidase, acyl-coenzyme A
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-
-
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Peroxisomal fatty acyl-CoA oxidase
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-
-
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Pristanoyl-CoA oxidase
-
-
-
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THCA-CoA oxidase
-
-
-
-
THCCox
-
-
-
-
Trihydroxycoprostanoyl-CoA oxidase
-
-
-
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Acyl-CoA oxidase
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-
-
-
AOX
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
inducible by growth on di-(2-ethylhexyl)phthalate
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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
stereochemistry of the reaction
-
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
mechanism, substrate binding site, and active site structure
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:oxygen 2-oxidoreductase
A flavoprotein (FAD). Acts on CoA derivatives of fatty acids with chain lengths from 8 to 18.
CAS REGISTRY NUMBER
COMMENTARY
61116-22-1
-
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
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
-
-
?
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
-
-
-
?
linoleoyl-CoA + O2
2-trans-9-trans-12-trans-octadecatrienoyl-CoA + H2O2
-
-
-
-
?
palmitoyl-CoA + O2
2-trans-hexadecenoyl-CoA + H2O2
-
-
-
-
?
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
?
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
-
-
?
dec-4-cis-enoyl-CoA + O2
2-trans-4-cis-decadienoyl-CoA + H2O2
-
-
-
?
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
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
oct-2-en-4-ynoyl-CoA
-
irreversible inactivation, pH dependent, higher under basic condition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
perilla oil
-
elevates AOX activity in a 4-day fedding, the effect is gradually decreased in a 4-week feeding
-
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
overview: specific activity of enzyme from several sources with several substrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
physiological function
-
involved in fatty acid oxidation, essential energy generation
physiological function
-
increased expression of isoform ACOX2 in the kidney along with increases in plasma phytanic acid and the altered gut microbiota may be involved in the oxidation in the kidney and the pathogenesis of hypertension
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACOX1_RAT
661
0
74679
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
139000
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
? * 52000 + ? * 22500, liver, SDS-PAGE, inducible fatty acyl-CoA oxidase
dimer
hexamer
-
6 * 69000, liver, SDS-PAGE, noninducible trihydroxyprostanoyl-CoA oxidase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y232F
the mutant shows reduced activity compared to the wild type enzyme
Y232G
the mutant shows reduced activity compared to the wild type enzyme
Y232S
the mutant shows reduced activity compared to the wild type enzyme
Y401F
the mutant shows reduced activity compared to the wild type enzyme
E421A
E421D
E421Q
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, wild-type enzyme and mutant enzymes E421D, E421A, E421Q and E421G are stable for 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the hydrogen peroxide-generating enzyme ACOX1 is inducible under conditions of high-fat diet or exposure to PPARalpha ligands, which results in a net increase of hydrogen peroxide in peroxisomes
increased renal isoform ACOX2 activity is associated with the onset of hypertension
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
inhibition of ACOX1 is an effective approach for the treatment of high fat diet or obesity-induced metabolic diseases by improving mitochondrial lipid and reactive oxygen species metabolism
nutrition
inhibition of ACOX1 is an effective approach for the treatment of high fat diet or obesity-induced metabolic diseases by improving mitochondrial lipid and reactive oxygen species metabolism
medicine
-
AOX activity is negatively correlated with postprandial triacylglycerol levels
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Osumi, T.; Ozasa, H.; Hashimoto, T.
Molecular cloning of cDNA for rat acyl-CoA oxidase
J. Biol. Chem.
259
2031-2034
1984
Rattus norvegicus
Hovik, R.; Osmundsen, H.
A kinetic investigation of the acyl-CoA oxidase reaction with the use of a novel spectrophotometric assay. Inhibition by acetyl-CoA, CoA and FMN
Biochem. J.
263
297-299
1989
Rattus norvegicus
Vamecq, J.; Schepers, L.; Parmentier, G.; Mannaerts, G.P.
Inhibition of peroxisomal fatty acyl-CoA oxidase by antimycin A
Biochem. J.
248
603-607
1987
Rattus norvegicus
Kawaguchi, A.; Tsubotani, S.; Seyama, Y.; Yamakawa, T.; Osumi, T.; Hashimoto, T.; Kikuchi, T.; Ando, M.; Okuda, S.
Stereochemistry of dehydrogenation catalyzed by Acyl-CoA oxidase
J. Biochem.
88
1481-1486
1980
Yarrowia lipolytica, Rattus norvegicus
Osumi, T.; Hashimoto, T.; Ui, N.
Purification and properties of acyl-CoA oxidase from rat liver
J. Biochem.
87
1735-1746
1980
Rattus norvegicus
Reubsaet, F.A.G.; Veerkamp, J.H.; Bukkens, S.G.F.; Trijbels, J.M.F.; Monnens, L.A.H.
Acyl-CoA oxidase activity and peroxisomal fatty acid oxidation in rat tissues
Biochim. Biophys. Acta
958
434-442
1988
Rattus norvegicus
Inestrosa, N.C.; Bronfman, M.; Leighton, F.
Purification of the peroxisomal fatty acyl-CoA oxidase from rat liver
Biochem. Biophys. Res. Commun.
95
7-12
1980
Rattus norvegicus
Osumi, T.; Hashimoto, T.
Acyl-CoA oxidase of rat liver: a new enzyme for fatty acid oxidation
Biochem. Biophys. Res. Commun.
83
479-485
1978
Rattus norvegicus
Suzuki, H.; Yamada, J.; Watanabe, T.; Suga, T.
Compartmentation of dicarboxylic acid beta-oxidation in rat liver: importance of peroxisomes in the metabolism of dicarboxylic acids
Biochim. Biophys. Acta
990
25-30
1989
Rattus norvegicus
Schepers, L.; Van Veldhoven, P.P.; Casteels, M.; Eyssen, H.J.; Mannaerts, G.P.
Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase
J. Biol. Chem.
265
5242-5246
1990
Rattus norvegicus
Nakajima, Y.; Miyahara, I.; Hirotsu, K.; Nishina, Y.; Shiga, K.; Setoyama, C.; Tamaoki, H.; Miura, R.
Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase
J. Biochem.
131
365-374
2002
Rattus norvegicus
Tamaoki, H.; Setoyama, C.; Miura, R.; Hazekawa, I.; Nishina, Y.; Shiga, K.
Spectroscopic studies of rat liver acyl-CoA oxidase with reference to recognition and activation of substrate
J. Biochem.
121
1139-1146
1997
Rattus norvegicus
Chu, C.; Mao, L.F.; Schulz, H.
Estimation of peroxisomal.beta-oxidation in rat heart by a direct assay of acyl-CoA oxidase
Biochem. J.
302
23-29
1994
Rattus norvegicus
-
Zeng, J.; Li, D.
Expression and purification of his-tagged rat peroxisomal acyl-CoA oxidase I wild-type and E421 mutant proteins
Protein Expr. Purif.
38
153-160
2004
Rattus norvegicus
Zeng, J.; Deng, G.; Li, D.
Intrinsic enoyl-CoA isomerase activity of rat acyl-CoA oxidase I
Biochim. Biophys. Acta
1760
78-85
2006
Rattus norvegicus
Tokuoka, K.; Nakajima, Y.; Hirotsu, K.; Miyahara, I.; Nishina, Y.; Shiga, K.; Tamaoki, H.; Setoyama, C.; Tojo, H.; Miura, R.
Three-dimensional structure of rat-liver acyl-CoA oxidase in complex with a fatty acid: insights into substrate-recognition and reactivity toward molecular oxygen
J. Biochem.
139
789-795
2006
Rattus norvegicus (P07872)
Kim, H.K.; Choi, H.
Stimulation of acyl-CoA oxidase by alpha-linolenic acid-rich perilla oil lowers plasma triacylglycerol level in rats
Life Sci.
77
1293-1306
2005
Rattus norvegicus
Zeng, J.; Liu, Y.; Wu, L.; Li, D.
Mutation of Tyr375 to Lys375 allows medium-chain acyl-CoA dehydrogenase to acquire acyl-CoA oxidase activity
Biochim. Biophys. Acta
1774
1628-1634
2007
Rattus norvegicus
Zeng, J.; Wu, L.; Zhang, X.; Liu, Y.; Deng, G.; Li, D.
Oct-2-en-4-ynoyl-CoA as a specific inhibitor of acyl-CoA oxidase
Org. Lett.
10
4287-4290
2008
Rattus norvegicus
Zeng, J.; Deng, S.; Wang, Y.; Li, P.; Tang, L.; Pang, Y.
Specific inhibition of acyl-CoA oxidase-1 by an acetylenic acid improves hepatic lipid and reactive oxygen species (ROS) metabolism in rats fed a high fat diet
J. Biol. Chem.
292
3800-3809
2017
Rattus norvegicus (P07872)
Deng, S.; Li, P.; Wang, Y.; Zeng, J.
tyrosine residues 232 and 401 play a critical role in the binding of the cofactor FAD of acyl-CoA oxidase
Appl. Biochem. Biotechnol.
185
875-883
2018
Rattus norvegicus (P07872)
Okamura, M.; Ueno, T.; Tanaka, S.; Murata, Y.; Kobayashi, H.; Miyamoto, A.; Abe, M.; Fukuda, N.
Increased expression of acyl-CoA oxidase 2 in the kidney with plasma phytanic acid and altered gut microbiota in spontaneously hypertensive rats
Hypertens. Res.
44
651-661
2021
Rattus norvegicus
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