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Information on EC 2.3.1.7 - carnitine O-acetyltransferase and Organism(s) Homo sapiens

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IUBMB 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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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
carnitine acetyltransferase, carat, carac, carnitine acetyl transferase, p-cat, carnitine o-acetyltransferase, h-cat, acetylcarnitine transferase, ct-cat, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetyl-CoA-carnitine O-acetyltransferase
-
-
-
-
acetylcarnitine transferase
-
-
-
-
CARAT
-
-
carnitine acetyl coenzyme A transferase
-
-
-
-
carnitine acetyl transferase
-
-
carnitine acetylase
-
-
-
-
carnitine acetyltransferase
carnitine-acetyl-CoA transferase
-
-
-
-
CATC
-
-
-
-
H-CAT
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + carnitine = CoA + O-acetylcarnitine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9029-90-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
-
-
-
?
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + L-carnitine
CoA + O-acylcarnitine
show the reaction diagram
-
-
-
-
?
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
butyryl-CoA + L-carnitine
CoA + O-butyrylcarnitine
show the reaction diagram
-
-
-
-
?
decanoylcarnitine + CoASH
decanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + L-carnitine
CoA + O-hexanoyl-L-carnitine
show the reaction diagram
-
-
-
-
?
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
octanoyl-CoA + carnitine
CoA + O-octanoylcarnitine
show the reaction diagram
-
-
-
?
octanoyl-CoA + carnitine
octanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + O-octanoylcarnitine
show the reaction diagram
-
-
-
-
?
octanoylcarnitine + CoASH
octanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + O-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
propionyl-CoA + carnitine
CoA + O-propionylcarnitine
show the reaction diagram
-
-
-
?
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
propionyl-CoA + L-carnitine
CoA + O-propionylcarnitine
show the reaction diagram
-
-
-
-
?
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + L-carnitine
CoA + O-acylcarnitine
show the reaction diagram
-
-
-
-
?
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-bromoacetylcarnitine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 0.498
acetyl-CoA
0.42
acetylcarnitine
-
-
0.0435 - 0.499
butyryl-CoA
0.086 - 0.58
carnitine
0.064
decanoyl-CoA
-
-
0.0549
hexanoyl-CoA
-
-
0.11 - 35.9
L-carnitine
0.0503
octanoyl-CoA
-
-
1.39
octanoylcarnitine
-
-
0.028
propionyl-CoA
-
-
0.65
propionylcarnitine
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78 - 94.8
acetyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78.75
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
silencing the CrAT gene disrupts cellular carnitine homeostasis, reduces the expression of mitochondrial superoxide dismutase 2 and results in an increase in oxidative stress within the mitochondrion
physiological function
-
the enzyme mitigates metabolic inertia and muscle fatigue during exercise
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CACP_HUMAN
626
0
70858
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60500
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in the presence of L-carnitine by vapor diffusion method
crystals grown by hanging-drop vapor-diffusion belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a: 137.65 A, b: 84.76 A, c: 57.65 A
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peroxisomal enzyme
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F545A
increases Km for both substrates
F545Y
minor effects on Km for both substrates
R497Q
increases Km for both substrates
T444A
increases Km for both substrates
V569M
missense variant idientified in a patient affected by Leigh syndrome. Proband-derived fibroblasts show carnitine acetyltransferase deficiency. The mutation severely impairs catalytic function toward acetyl-CoA, and also toward propionyl-CoA and octanoyl-CoA, reducing the Vmax of acetyl-CoA, propionyl-CoA, and octanoyl-CoA to 24%, 29%, and 27%, respectively, of wild-type
Y110C
missense variant idientified in a patient affected by Leigh syndrome. Proband-derived fibroblasts show carnitine acetyltransferase deficiency. The mutation severely impairs catalytic function toward acetyl-CoA, reducing the Vmax toward acetyl-CoA, propionyl-CoA, and octanoyl-CoA to 32%, 45%, and 61% of wild-type
Y431A
increases Km for both substrates
Y431F
increases Km for both substrates
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, when stored in 50% glycerol, maintains its activity unaltered for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisLink protein purification resin column chromatography
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recombinant protein using His-tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloned, mapping of the corresponding gene to chromosome 9q34.1
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expressed as His-tag fusion protein in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
hCAT, cloned and expressed in Escherichia coli
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single-gene product with multiple targeting signals
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
White, H.L.; Wu, J.C.
Choline and carnitine acetyltransferases of heart
Biochemistry
12
841-846
1973
Columba sp., Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kawachi, H.; Atomi, H.; Ueda, M.; Tanaka, A.
Peroxisomal and mitochondrial carnitine acetyltransferases of the n-alkane-assimilating yeast Candida tropicalis. Analysis of gene structure and translation products
Eur. J. Biochem.
238
845-852
1996
Saccharomyces cerevisiae, Candida tropicalis, Columba sp., Homo sapiens
Manually annotated by BRENDA team
Sheridan, R.; Ratledge, C.
Changes in cell morphology and carnitine acetyltransferase activity in Candida albicans following growth on lipids and serum and after in vivo incubation in mice
Microbiology
142
3171-3180
1996
Candida albicans, Candida tropicalis, Homo sapiens
-
Manually annotated by BRENDA team
Brunner, S.; Kramar, K.; Denhardt, D.T.; Hofbauer, R.
Cloning and characterization of murine carnitine acetyltransferase: evidence for a requirement during cell cycle progression
Biochem. J.
322
403-410
1997
Saccharomyces cerevisiae, Columba sp., Homo sapiens, Mus musculus, Mus musculus (P47934), Sus scrofa, Mus musculus S3T3(ATCC CCL-92)
-
Manually annotated by BRENDA team
Ramsay, R.R.
The carnitine acyltransferases: modulators of acyl-CoA-dependent reactions
Biochem. Soc. Trans.
28
182-186
2000
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Lian, W.; Govindasamy, L.; Gu, Y.; Kukar, T.; Agbandje-McKenna, M.; McKenna, R.; Wu, D.
Crystallization and preliminary X-ray crystallographic studies on recombinant human carnitine acetyltransferase
Acta Crystallogr. Sect. D
58
1193-1194
2002
Columba sp., Homo sapiens
Manually annotated by BRENDA team
Jogl, G.; Tong, L.
Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport
Cell
112
113-122
2003
Homo sapiens, Mus musculus, Mus musculus (P47934)
Manually annotated by BRENDA team
Wu, D.; Govindasamy, L.; Lian, W.; Gu, Y.; Kukar, T.; Agbandje-McKenna, M.; McKenna, R.
Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer
J. Biol. Chem.
278
13159-13165
2003
Homo sapiens
Manually annotated by BRENDA team
Govindasamy, L.; Kukar, T.; Lian, W.; Pedersen, B.; Gu, Y.; Agbandje-McKenna, M.; Jin, S.; McKenna, R.; Wu, D.
Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase
J. Struct. Biol.
146
416-424
2004
Homo sapiens (P43155), Homo sapiens
Manually annotated by BRENDA team
Ramsay, R.R.; Naismith, J.H.
A snapshot of carnitine acetyltransferase
Trends Biochem. Sci.
28
343-346
2003
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
En-Nosse, M.; Hartmann, S.; Trinkaus, K.; Alt, V.; Stigler, B.; Heiss, C.; Kilian, O.; Schnettler, R.; Lips, K.S.
Expression of non-neuronal cholinergic system in osteoblast-like cells and its involvement in osteogenesis
Cell Tissue Res.
338
203-215
2009
Homo sapiens, Mus musculus (P47934), Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Violante, S.; Ijlst, L.; Ruiter, J.; Koster, J.; van Lenthe, H.; Duran, M.; de Almeida, I.T.; Wanders, R.J.; Houten, S.M.; Ventura, F.V.
Substrate specificity of human carnitine acetyltransferase: Implications for fatty acid and branched-chain amino acid metabolism
Biochim. Biophys. Acta
1832
773-779
2013
Homo sapiens
Manually annotated by BRENDA team
Seiler, S.E.; Koves, T.R.; Gooding, J.R.; Wong, K.E.; Stevens, R.D.; Ilkayeva, O.R.; Wittmann, A.H.; DeBalsi, K.L.; Davies, M.N.; Lindeboom, L.; Schrauwen, P.; Schrauwen-Hinderling, V.B.; Muoio, D.M.
Carnitine acetyltransferase mitigates metabolic inertia and muscle fatigue during exercise
Cell Metab.
22
65-76
2015
Homo sapiens
Manually annotated by BRENDA team
Sharma, S.; Sun, X.; Agarwal, S.; Rafikov, R.; Dasarathy, S.; Kumar, S.; Black, S.
Role of carnitine acetyl transferase in regulation of nitric oxide signaling in pulmonary arterial endothelial cells
Int. J. Mol. Sci.
14
255-272
2013
Homo sapiens
Manually annotated by BRENDA team
Berg, S.M.; Beck-Nielsen, H.; Faergeman, N.J.; Gaster, M.
Carnitine acetyltransferase A new player in skeletal muscle insulin resistance?
Biochem. Biophys. Rep.
9
47-50
2017
Homo sapiens (P43155), Homo sapiens
Manually annotated by BRENDA team
Laera, L.; Punzi, G.; Porcelli, V.; Gambacorta, N.; Trisolini, L.; Pierri, C.L.; De Grassi, A.
CRAT missense variants cause abnormal carnitine acetyltransferase function in an early-onset case of Leigh syndrome
Hum. Mutat.
41
110-114
2020
Homo sapiens (P43155), Homo sapiens
Manually annotated by BRENDA team