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Information on EC 2.3.1.7 - carnitine O-acetyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q704S8
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EC Tree
2.3.1.7 carnitine O-acetyltransferaseIUBMB Comments
Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase).
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Word Map
- 2.3.1.7
- peroxisomal
- palmitoyltransferase
-
beta-oxidation
- acyl-coas
- l-carnitine
- acyltransferases
- clofibrate
- palmitoyl-coa
- acylcarnitine
- proliferators
-
hypolipidemic
-
octanoyltransferase
-
cyanide-insensitive
-
propionylation
- cardos
- acetyl-l-carnitine
- carbazole
-
carnitine-dependent
-
cronbach
-
alloy
-
1,9a-dioxygenase
- coash
-
peroxisome-associated
- palmitoylcarnitine
-
nafenopin
- bezafibrate
- ciprofibrate
- food industry
- analysis
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
carnitine acetyltransferase, carat, carac, carnitine acetyl transferase, p-cat, carnitine o-acetyltransferase, acetylcarnitine transferase, h-cat, ct-cat, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-CoA-carnitine O-acetyltransferase
-
-
-
-
acetylcarnitine transferase
-
-
-
-
carnitine acetyl coenzyme A transferase
-
-
-
-
carnitine acetylase
-
-
-
-
carnitine acetyltransferase
carnitine-acetyl-CoA transferase
-
-
-
-
CATC
-
-
-
-
carnitine acetyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:carnitine O-acetyltransferase
Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase).
CAS REGISTRY NUMBER
COMMENTARY
9029-90-7
-
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
hexanoyl-CoA + carnitine
CoA + O-hexanoylcarnitine
very low activity
-
-
r
octanoyl-CoA + carnitine
CoA + O-octanoylcarnitine
very low activity
-
-
r
acetoacetyl-CoA + L-(-)carnitine
O-acetoacetyl(-)carnitine + CoASH
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487418, 487421, 487422, 487423, 487424, 487429, 487430, 487432
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
-
low activity with wild-type enzyme. Mutant enzymes T465V/T467N/R518N and A106M/T465V/T467N/R518N show improved catalytic efficiency toward choline (Kcat/Km) compared with that of the wild type enzyme
-
-
?
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487418, 487421, 487422, 487423, 487424, 487429, 487430, 487432
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487417, 487418, 487421, 487422, 487423, 487424, 487429, 487430, 487432
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487417, 487418, 487421, 487422, 487423, 487424, 487429, 487430, 487432
-
-
r
butyryl-CoA + carnitine
CoA + O-butyrylcarnitine
-
wild-type enzyme shows maximal activity towards butyryl-CoA
-
-
?
butyryl-CoA + L-carnitine
CoA + O-butyrylcarnitine
-
preferred substrate
-
-
r
decanoyl-CoA + carnitine
decanoylcarnitine + CoASH
-
-
-
-
r
decanoylcarnitine + CoASH
decanoyl-CoA + carnitine
-
-
-
-
r
hexanoyl-CoA + carnitine
CoA + O-hexanoylcarnitine
-
mutant enzymes M564G and D356A/M564G show maximal activity towards hexanoyl-CoA
-
-
?
hexanoyl-CoA + carnitine
hexanoylcarnitine + CoASH
-
-
-
-
r
hexanoylcarnitine + CoASH
hexanoyl-CoA + carnitine
-
-
-
-
r
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
-
-
-
-
r
O-acetoacetyl(-)carnitine + CoASH
acetoacetyl-CoA + L-(-)carnitine
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487418, 487421, 487422, 487423, 487424, 487429, 487430, 487432
-
-
r
octanoyl-CoA + carnitine
octanoylcarnitine + CoASH
-
-
-
-
r
octanoylcarnitine + CoASH
octanoyl-CoA + carnitine
-
-
-
-
r
palmitoyl-CoA + carnitine
CoA + O-palmitoylcarnitine
-
wild-type enzyme shows no activity, mutant enzymes M564G and D356A/M564G show activity
-
-
?
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
-
-
-
-
r
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
-
-
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487418, 487421, 487422, 487423, 487424, 487429, 487430
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
-
key mitochondrial enzyme for fuel utilization, essential functions are to regenerate CoA, which allows peroxisomal beta-oxidation to proceed, and to facilitate transport of acetyl moieties to mitochondria for oxidation
-
-
r
additional information
?
-
wild type enzyme is almost inactive towards longer chain fatty acids, some mutations increases activity towards longer chain fatty acids
-
-
?
additional information
?
-
-
palmityl-CoA does not act as a substrate for the liver enzyme
-
-
?
additional information
?
-
-
O-acetyl-(+)-carnitine and reduced glutathione will not serve as substrates, succinyl-CoA or beta-hydroxy-betamethylglutaryl-CoA are no substrates
-
-
?
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
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487418, 487421, 487422, 487423, 487424, 487429, 487430, 487432
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487417, 487418, 487421, 487422, 487423, 487424, 487429, 487430, 487432
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487417, 487418, 487421, 487422, 487423, 487424, 487429, 487430, 487432
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487418, 487421, 487422, 487423, 487424, 487429, 487430
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
-
key mitochondrial enzyme for fuel utilization, essential functions are to regenerate CoA, which allows peroxisomal beta-oxidation to proceed, and to facilitate transport of acetyl moieties to mitochondria for oxidation
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,6S:2S,6R)-6-carboxymethyl-2-hydroxy-2,4,4-trimethylmorpholinium chloride
-
hemiacetylcarnitinium
acetylcarnitine
-
competitive inhibition, inhibitor for the forward reaction
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km acetylcarnitine 1.25 mg/ml
-
0.086
carnitine
M564G mutant enzyme from yeast with octanoyl-CoA as second substrate, pH 7.8, 30°C
0.164
carnitine
M564G mutant enzyme from yeast with hexanoyl-CoA as second substrate, pH 7.8, 30°C
0.17
carnitine
M564G mutant enzyme from yeast with butyryl-CoA as second substrate, pH 7.8, 30°C
0.203
carnitine
recombinant enzyme from yeast with acetyl-CoA as second substrate, pH 7.8, 30°C
0.22
carnitine
recombinant enzyme from yeast with butyryl-CoA as second substrate, pH 7.8, 30°C
0.339
carnitine
M564G mutant enzyme from yeast with acetyl-CoA as second substrate, pH 7.8, 30°C
0.567
carnitine
recombinant enzyme from yeast with hexanoyl-CoA as second substrate, pH 7.8, 30°C
0.964
carnitine
recombinant enzyme from yeast with octanoyl-CoA as second substrate, pH 7.8, 30°C
0.027
CoASH
-
substrate butyrylcarnitine and octanoylcarnitine, enzyme from liver homogenate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.72
(2R,6S:2S,6R)-6-carboxymethyl-2-hydroxy-2,4,4-trimethylmorpholinium chloride
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
486295, 487403, 487404, 487407, 487416, 487417, 487418, 487421, 487422, 487423, 487424, 487429, 487430
-
-
486295, 487403, 487404, 487406, 487407, 487408, 487410, 487414, 487416, 487417, 487418, 487421, 487422, 487424, 487429, 487430
-
-
additional information
-
carnitine acetyltransferase is highly active in neuronal tissues and in neuronal cell cultures relative to choline acetyl transferase
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
486295, 487404, 487406, 487407, 487408, 487410, 487416, 487417, 487421, 487422, 487423, 487424, 487429, 487430, 487432
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). CACP_RAT
626
0
70801
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
-
1 * 34000 + 1 * 25000, purified from mitochondrial fraction of liver, rats fed on a diet containing ethyl p-chlorophenoxyisobutyrate, SDS-PAGE
27000
-
1 * 36500 + 1 * 27000, purified from mitochondrial fraction, monomeric form converted into dimeric by proteolytic modification after disruption of mitochondria, SDS-PAGE
34000
-
1 * 34000 + 1 * 25000, purified from mitochondrial fraction of liver, rats fed on a diet containing ethyl p-chlorophenoxyisobutyrate, SDS-PAGE
36500
-
1 * 36500 + 1 * 27000, purified from mitochondrial fraction, monomeric form converted into dimeric by proteolytic modification after disruption of mitochondria, SDS-PAGE
56000
59000
69000
56000
-
purified from mitochondrial fraction of liver, rats fed on a diet containing ethyl p-chlorophenoxyisobutyrate
69000
-
translation product of the enzyme by the reticulocyte lysate protein-synthesizing system
69000
-
post-mitochondrial fraction, 2 polypeptides 67500 Da + 69000 Da cannot be separated from each other
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
dimer
-
1 * 36500 + 1 * 27000, purified from mitochondrial fraction, monomeric form converted into dimeric by proteolytic modification after disruption of mitochondria, SDS-PAGE
dimer
-
1 * 34000 + 1 * 25000, purified from mitochondrial fraction of liver, rats fed on a diet containing ethyl p-chlorophenoxyisobutyrate, SDS-PAGE
monomer
-
1 * 62000, monomeric in presence of catalytic amounts of substrate, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M564A
lowered activity with acetyl-CoA, increased activity with longer chain acyl-CoAs
M564G
lowered activity with acetyl-CoA, increased activity with longer chain acyl-CoAs, 1250-fold increase in activity with myristoyl-CoA
D356A/M564G
-
shows 6fold higher activity toward palmitoyl-CoA than that of the single mutant M564G and a new activity toward stearoyl-CoA. Mutations convert the enzyme into a pseudo carnitine palmitoyltransferase in terms of substrate specificity
M564G
-
mutant enzyme shows higher activity with medium-chain acyl-CoAs than wild-type enzyme
T465V/T467N/R518N
-
3fold improved catalytic efficiency toward choline (Kcat/Km) compared with that of the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 50
-
enzyme retains total activity when kept at 37°C for 30 min, rapid loss of activity above 37°C, loses half of the activity at 40°C for 30 min, but is completely inactivated when kept at 44°C for 30 min or 50°C for 5 min, 75% loss of activity at 37°C for 8 h, only 15% loss when kept at 25°C for 8 h
4 - 25
-
stored in a refrigerator for 2 days or incubated at 25°C for 5 h, monomeric form remains unchanged
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
retains activity indefinitely when kept frozen, pure enzyme retains activity when kept frozen for long periods of time, inactivation of pure preparations occurs during dialysis
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM potassium phosphate buffer, pH 7.5, purified enzyme can be stored for several months without loss of activity
-
-20°C, frozen mitochondrial fraction can be stored for several months without loss of activity
-
-20°C, peroxisomal and microsomal fractions from isopycnic sucrose density gradients, activity is stable during storage for at least 3 months
-
-20°C, peroxisomes and microsomes stored in 0.4 M KCl, 0.02% sodium azide, 150 mM Tris-HCl, pH, retains at least 95% of their activity when stored for 3 months
-
4°C, peroxisomal and microsomal fractions from isopycnic sucrose density gradients, activity is stable during storage for 10 days
-
4°C, peroxisomes and microsomes stored in 0.4 M KCl, 0.02% sodium azide, 150 mM Tris-HCl, pH, retains at least 95% of their activity when stored for 18 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme specific activity is diminished in muscles from obese and diabetic rodents despite increased protein abundance
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
paper chromatography-based assay for the detection of acetylcholine and L-acetylcarnitine. The assay can be used to measure both choline acetyltransferase and carnitine acetyltransferase activity in the same samples
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Farrell, S.O.; Fiol, C.J.; Reddy, J.K.; Bieber, L.L.
Properties of purified carnitine acyltransferases of mouse liver peroxisomes
J. Biol. Chem.
259
13089-13095
1984
Bos taurus, Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley, Torulopsis bovina
Mittal, B.; Kurup, C.K.R.
Purification of clofibrate-induced carnitine acetyltransferase from rat liver mitochondria
Biochim. Biophys. Acta
619
90-97
1980
Columba sp., Rattus norvegicus, Sus scrofa
Bieber, L.L.; Markwell, M.A.K.
Peroxisomal and microsomal carnitine acetyltransferases
Methods Enzymol.
71
351-358
1981
Bos taurus, Cavia porcellus, Columba sp., Rattus norvegicus, Sus scrofa
-
Ueda, M.; Tanaka, A.; Fukui, S.
Peroxisomal and mitochondrial carnitine acetyltransferases in alkane-grown yeast Candida tropicalis
Eur. J. Biochem.
124
205-210
1982
Candida tropicalis, Columba sp., Rattus norvegicus, Sus scrofa
Huckle, W.R.; Tamblyn, T.M.
Purification and properties of carnitine acetyltransferases from bovine spermatozoa and heart
Arch. Biochem. Biophys.
226
94-110
1983
Bos taurus, Columba sp., Ovis aries, Rattus norvegicus
Miyazawa, S.; Ozasa, H.; Furuta, S.; Osumi, T.; Hashimoto, T.
Purification and properties of carnitine acetyltransferase from rat liver
J. Biochem.
93
439-451
1983
Columba sp., Rattus norvegicus
Ueda, M.; Tanaka, A.; Fukui, S.
Characterization of peroxisomal and mitochondrial carnitine acetyltransferases purified from alkane-grown Candida tropicalis
Eur. J. Biochem.
138
445-449
1984
Candida tropicalis, Columba sp., Rattus norvegicus
Gandour, R.D.; Colucci, W.J.; Stelly, T.C.; Brady, P.S.; Brady, L.J.
Active-site probes of carnitineacyltransferases. Inhibition of carnitine acetyltransferase by hemiacetylcarnitinium, a reaction intermediate analogue
Biochem. Biophys. Res. Commun.
138
735-741
1986
Columba sp., Rattus norvegicus
Bloisi, W.; Colombo, I.; Garavaglia, B.; Giardini, R.; Finocchiaro, G.; Didonato, S.
Purification and properties of carnitine acetyltransferase from human liver
Eur. J. Biochem.
189
539-546
1990
Homo sapiens, Rattus norvegicus, Sus scrofa
Chung, C.; Chung, C.D.; Bieber, L.L.
Purification of heart and liver mitochondrial carnitine acetyltransferase
Protein Expr. Purif.
2
426-431
1991
Rattus norvegicus
Kispal, G.; Cseko, J.; Alkonyi, I.; Sandor, A.
Isolation and characterization of carnitine acetyltransferase from S. cerevisiae
Biochim. Biophys. Acta
1085
217-222
1991
Bos taurus, Saccharomyces cerevisiae, Candida tropicalis, Columba sp., Homo sapiens, Rattus norvegicus, Torulopsis bovina
Alhomida, A.S.
Inhibition studies of the carnitine acetyltransferase from skeletal muscle of the camel (Camelus dromedarius) by sulfhydryl reagents and metal ions
Biochem. Mol. Biol. Int.
39
923-931
1996
Camelus dromedarius, Columba sp., Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae
Alhomida, A.S.; Al-Jafari, A.A.; Duhaiman, A.S.; Rabbani, N.; Junaid, M.A.
Kinetic properties of purified carnitine acetyltransferase from the skeletal muscle of Arabian camel (Camelus dromedarius)
Biochimie
78
204-208
1996
Camelus dromedarius, Columba sp., Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Alhomida, A.S.; Duhaiman, A.S.; Al-Jafari, A.A.; Junaid, M.A.
Purification of carnitine acetyltransferase from skeletal muscle of the camel (Camelus dromedarius)
Mol. Cell. Biochem.
165
95-101
1996
Bos taurus, Camelus dromedarius, Columba sp., Homo sapiens, Mus musculus, Rattus norvegicus
Jernejc, K.; Legisa, M.
Purification and properties of carnitine acetyltransferase from citric acid producing Aspergillus niger
Appl. Biochem. Biotechnol.
60
151-158
1996
Aspergillus niger, Bos taurus, Saccharomyces cerevisiae, Cutaneotrichosporon curvatum, Candida tropicalis, Cyberlindnera jadinii, Columba sp., Homo sapiens, Lipomyces starkeyi, Mus musculus, Rattus norvegicus, Sus scrofa
Abbas, A.S.; Wu, G.; Schulz, H.
Carnitine acetyltransferase is not a cytosolic enzyme in rat heart and therefore cannot function in the energy-linked regulation of cardiac fatty acid oxidation
J. Mol. Cell. Cardiol.
30
1305-1309
1998
Bos taurus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Ramsay, R.R.
The carnitine acyltransferases: modulators of acyl-CoA-dependent reactions
Biochem. Soc. Trans.
28
182-186
2000
Homo sapiens, Rattus norvegicus
Liu, J.; Killilea, D.W.; Ames, B.N.
Age-associated mitochondrial oxidative decay: improvement of carnitine acetyltransferase substrate-binding affinity and activity in brain by feeding old rats acetyl-L-carnitine and/or R-alpha -lipoic acid
Proc. Natl. Acad. Sci. USA
99
1876-1881
2002
Columba sp., Oryctolagus cuniculus, Rattus norvegicus
Cordente, A.G.; Lopez-Vinas, E.; Vazquez, M.I.; Swiegers, J.H.; Pretorius, I.S.; Gomez-Puertas, P.; Hegardt, F.G.; Asins, G.; Serra, D.
Redesign of carnitine acetyltransferase specificity by protein engineering
J. Biol. Chem.
279
33899-33908
2004
Rattus norvegicus (Q704S8)
Cordente, A.G.; Lopez-Vinas, E.; Vazquez, M.I.; Gomez-Puertas, P.; Asins, G.; Serra, D.; Hegardt, F.G.
Mutagenesis of specific amino acids converts carnitine acetyltransferase into carnitine palmitoyltransferase
Biochemistry
45
6133-6141
2006
Rattus norvegicus
Bailey, J.A.; Lahiri, D.K.
Chromatographic separation of reaction products from the choline acetyltransferase and carnitine acetyltransferase assay: differential ChAT and CrAT activity in brain extracts from Alzheimers disease versus controls
J. Neurochem.
122
672-680
2012
Homo sapiens, Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 2.3.1.7)
Transporter Classification Database (TCDB): 4.C.2.1.1
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