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Information on EC 2.3.1.7 - carnitine O-acetyltransferase and Organism(s) Mus musculus and UniProt Accession P47934
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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: Mus musculus
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
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
-
-
-
-
r
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
-
-
-
-
r
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
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
-
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0035
carnitine
liver homogenate, pH 8.0, temperature not specified in the publication
0.011
carnitine
mitochondria from liver, pH 8.0, temperature not specified in the publication
0.0537
carnitine
heart homogenate, pH 8.0, temperature not specified in the publication
0.0562
carnitine
mitochondria from heart, pH 8.0, temperature not specified in the publication
0.0328
CoA
mitochondria from heart, pH 8.0, temperature not specified in the publication
0.0664
CoA
heart homogenate, pH 8.0, temperature not specified in the publication
0.0888
CoA
mitochondria from liver, pH 8.0, temperature not specified in the publication
0.1134
CoA
liver homogenate, pH 8.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Crat is most highly expressed in heart, brown adipose tissue and white adipose tissue
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the majority of Crat mRNA in mouse is mitochondrial, with only about 120% of Crat mRNA being peroxisomal, except for liver, where peroxisomal Crat represents about 38%of total Crat mRNA
-
the majority of Crat mRNA in mouse is mitochondrial, with only about 120% of Crat mRNA being peroxisomal, except for liver, where peroxisomal Crat represents about 38%of total Crat mRNA
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
-
enzyme deficiency increases tissue acetyl-CoA levels and susceptibility to diet-induced lysine acetylation of broad-ranging mitochondrial proteins, coincident with diminished whole body glucose control
physiological function
physiological function
Crat deletion in Aguoti-related peptide neurons reduces food intake and feeding behavior and increases glycerol supply to the liver during fasting, as a gluconeogenic substrate. Crat deletion increases peripheral fatty acid substrate utilization and attenuates the switch to glucose utilization after refeeding. Crat regulates protein acetylation and metabolic processing
physiological function
in the murine cardiomyocyte cytosol, reverse CrAT activity (producing acetyl-CoA) is higher compared with the liver. The heart displays a lower reverse CrAT Km for CoA compared with the liver. Cytosolic reverse CrAT accounts for 4.6% of total activity in heart tissue and 12.7% in H9C2 cells, while highly purified heart cytosolic fractions show significant CrAT protein levels. Acetyl-CoA carboxylase ACC2-knockout mouse hearts show decreased CrAT protein levels and activity, associated with increased palmitate oxidation and acetyl-CoA/CoA ratio compared with controls. Feeding mice a high-fat diet for 10 weeks increases cardiac CrAT protein levels and activity, associated with a reduced acetyl-CoA/CoA ratio and glucose oxidation
physiological function
-
the enzyme inhibits mitochondrial acetyl-CoA overload by regulating the efflux of acetyl-CoA, thus maintaining PDH activity in skeletal muscle
physiological function
-
the enzyme plays a role in modulating the muscle acetylproteome
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_MOUSE
626
0
70840
Swiss-Prot
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, high resolution crystal structure of wild-type murine carnitine acetyltransferase in a ternary complex with its substrates acetyl-CoA and carnitine, and the structure of the S554A/M564G double mutant in a ternary complex with the substrates CoA and hexanoylcarnitine
crystallized as pure enzyme and in complex with its substrates carnitine and CoA
-
M564G and F565A mutant enzymes crystallized by sitting-drop vapor diffusion method
-
sitting drop vapor diffusion method, space group C2, cell dimensions for the free enzyme crystal a: 158.9 A, b: 89.6 A, c: 119.4 A, beta: 127.5°
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H343E
kcat/KM for acetyl-CoA is 9.8fold lower than wild-type value, mutant enzyme shows mo activity with hexanoyl-CoA as substrate
M564G
kcat/KM for acetyl-CoA is 12.4fold lower than wild-type value, kcat/Km for hexanoyl-CoA is 31.4fold higher than wild-type value
S554A
kcat/KM for acetyl-CoA is 109fold lower than wild-type value, kcat/Km for hexanoyl-CoA is 8fold lower than wild-type value
S554A/M564G
kcat/KM for acetyl-CoA is 196fold lower than wild-type value, kcat/Km for hexanoyl-CoA is 4fold lower than wild-type value
F565A
-
used for crystallization, only minor effect on protein structure, increased activity with acetyl-CoA
M564A
-
used for crystallization, decreased activity with acetyl-CoA and butyryl-CoA
M564G
-
used for crystallization, dramatic changes in protein structure, decreased activity with acetyl-CoA and butyryl-CoA, strongly increased activity with hexanoyl-CoA
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
both L-carnitine and fenofibrate are inducers of carnitine acetyltransferase transcription
-
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
Bieber, L.L.; Fiol, C.
Purification and assay of carnitine acyltransferases
Methods Enzymol.
123
276-284
1986
Candida tropicalis, Mus musculus
Lu, F.J.; Huang, T.S.; Chen, Y.S.
Effects of humic acid-metal complexes on hepatic carnitine palmitoyltransferase, carnitine acetyltransferase and catalase activities
Environ. Toxicol. Chem.
13
435-441
1994
Mus musculus, Mus musculus BALB/c
-
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
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)
-
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)
Jogl, G.; Hsiao, Y.S.; Tong, L.
Structure and function of carnitine acyltransferases
Ann. N. Y. Acad. Sci.
1033
17-29
2004
Mus musculus
Hsiao, Y.S.; Jogl, G.; Tong, L.
Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase
J. Biol. Chem.
279
31584-31589
2004
Mus musculus
Ramsay, R.R.; Naismith, J.H.
A snapshot of carnitine acetyltransferase
Trends Biochem. Sci.
28
343-346
2003
Homo sapiens, Mus musculus
Hsiao, Y.S.; Jogl, G.; Tong, L.
Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates
J. Biol. Chem.
281
28480-28487
2006
Mus musculus (P47934), Mus musculus
Westin, M.A.; Hunt, M.C.; Alexson, S.E.
Short- and medium-chain carnitine acyltransferases and acyl-CoA thioesterases in mouse provide complementary systems for transport of beta-oxidation products out of peroxisomes
Cell. Mol. Life Sci.
65
982-990
2008
Mus musculus, Mus musculus 129/Sv
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
Kienesberger, K.; Pordes, A.G.; Voelk, T.G.; Hofbauer, R.
L-carnitine and PPARalpha-agonist fenofibrate are involved in the regulation of carnitine acetyltransferase (CrAT) mRNA levels in murine liver cells
BMC Genomics
15
514
2014
Mus musculus
Davies, M.N.; Kjalarsdottir, L.; Thompson, J.W.; Dubois, L.G.; Stevens, R.D.; Ilkayeva, O.R.; Brosnan, M.J.; Rolph, T.P.; Grimsrud, P.A.; Muoio, D.M.
The acetyl group buffering action of carnitine acetyltransferase offsets macronutrient-induced lysine acetylation of mitochondrial proteins
Cell Rep.
14
243-254
2016
Mus musculus
Miyata, Y.; Shimomura, I.
Metabolic flexibility and carnitine flux: The role of carnitine acyltransferase in glucose homeostasis
J. Diabetes Investig.
4
247-249
2013
Mus musculus
Altamimi, T.R.; Thomas, P.D.; Darwesh, A.M.; Fillmore, N.; Mahmoud, M.U.; Zhang, L.; Gupta, A.; Al Batran, R.; Seubert, J.M.; Lopaschuk, G.D.
Cytosolic carnitine acetyltransferase as a source of cytosolic acetyl-CoA a possible mechanism for regulation of cardiac energy metabolism
Biochem. J.
475
959-976
2018
Mus musculus (P47934), Mus musculus
Reichenbach, A.; Stark, R.; Mequinion, M.; Denis, R.R.G.; Goularte, J.F.; Clarke, R.E.; Lockie, S.H.; Lemus, M.B.; Kowalski, G.M.; Bruce, C.R.; Huang, C.; Schittenhelm, R.B.; Mynatt, R.L.; Oldfield, B.J.; Watt, M.J.; Luquet, S.; Andrews, Z.B.
AgRP neurons require carnitine acetyltransferase to regulate metabolic flexibility and peripheral nutrient partitioning
Cell Rep.
22
1745-1759
2018
Mus musculus (P47934)
EXTERNAL LINKS (specific for EC-Number 2.3.1.7)
Transporter Classification Database (TCDB): 4.C.2.1.1
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