Information on EC 2.3.1.7 - carnitine O-acetyltransferase

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The expected taxonomic range for this enzyme is: Opisthokonta

EC NUMBER
COMMENTARY
2.3.1.7
-
RECOMMENDED NAME
GeneOntology No.
carnitine O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + carnitine = CoA + O-acetylcarnitine
show the reaction diagram
reaction mechanism
-
acetyl-CoA + carnitine = CoA + O-acetylcarnitine
show the reaction diagram
reaction mechanism
-
acetyl-CoA + carnitine = CoA + O-acetylcarnitine
show the reaction diagram
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
-
-
-
acetyl-CoA + carnitine = CoA + O-acetylcarnitine
show the reaction diagram
mechanism of reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mitochondrial L-carnitine shuttle
-
-
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).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetyl-CoA-carnitine O-acetyltransferase
-
-
-
-
acetylcarnitine transferase
-
-
-
-
acuJ
-
gene name
CARAT
Mus musculus S3T3(ATCC CCL-92)
-
-
-
carnitine acetyl coenzyme A transferase
-
-
-
-
carnitine acetylase
-
-
-
-
carnitine acetyltransferase
-
-
-
-
carnitine acetyltransferase
-
-
carnitine acetyltransferase
-
-
carnitine acetyltransferase
-
-
carnitine acetyltransferase
-
-
carnitine acetyltransferase
P47934
-
carnitine acetyltransferase
-
-
carnitine acetyltransferase
A9JPD4
-
carnitine acetyltransferase CAT2
-
-
carnitine acetyltransferase Cat2p
-
-
carnitine acetyltransferase Yat1p
-
-
carnitine acetyltransferase Yat2p
-
-
carnitine-acetyl-CoA transferase
-
-
-
-
CAT
Rattus norvegicus Sprague-Dawley
-
;
-
CATC
-
-
-
-
CRAT
-
-
H-CAT
-
-
P-CAT
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-90-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A60 MZKIBK (NRLL 2270)
-
-
Manually annotated by BRENDA team
beef; bovine; Holstein bulls
-
-
Manually annotated by BRENDA team
dimorphic yeast, C316
-
-
Manually annotated by BRENDA team
(Castellani) Berkhout strain pK233(ATCC 20336); yeast
-
-
Manually annotated by BRENDA team
ATCC 32113; yeast
-
-
Manually annotated by BRENDA team
guinea pig
-
-
Manually annotated by BRENDA team
commercial preparation, Boehringer Mannheim; pigeon
-
-
Manually annotated by BRENDA team
commercial preparation, Sigma; pigeon
-
-
Manually annotated by BRENDA team
BALB/c; mouse
-
-
Manually annotated by BRENDA team
mouse, cDNA clone MMRNACAR, EMBL data bank accession number
UniProt
Manually annotated by BRENDA team
mouse, Protein Data Bank accession number
UniProt
Manually annotated by BRENDA team
mouse; NIH3T3 (ATCC CRL-1658); S3T3(ATCC CCL-92)
-
-
Manually annotated by BRENDA team
mouse; swiss mice
-
-
Manually annotated by BRENDA team
Sv/129 mice
-
-
Manually annotated by BRENDA team
Mus musculus BALB/c
BALB/c
-
-
Manually annotated by BRENDA team
Mus musculus S3T3(ATCC CCL-92)
S3T3(ATCC CCL-92)
-
-
Manually annotated by BRENDA team
Mus musculus Sv/129
Sv/129 mice
-
-
Manually annotated by BRENDA team
new Zealand white; rabbit
-
-
Manually annotated by BRENDA team
ram; sheep
-
-
Manually annotated by BRENDA team
albino; rat
-
-
Manually annotated by BRENDA team
Fischer 344; rat
-
-
Manually annotated by BRENDA team
rat; Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
porcine
-
-
Manually annotated by BRENDA team
Torulopsis bovina
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
carnitine acetyltransferase Yat1 is cytosolic and contributes to acetyl-CoA transport from the cytosol during growth on ethanol or acetate, but its activity is not required for growth on oleate, mitochondrial carnitine acetyltransferase Cat2 is required for the intramitochondrial conversion of acetylcarnitine to acetyl-CoA, which is essential for a functional tricarboxylic acid cycle during growth on oleate, acetate, ethanol, and citrate. Peroxisomal Cat2 is essential neither for export of acetyl units during growth on oleate nor for the import of acetyl units during growth on acetate or ethanol. Oxidation of fatty acids still takes place in the absence of peroxisomal Cat2, but biomass formation is absent, and the strain displays a growth delay on acetate and ethanol that can be partially rescued by the addition of carnitine
physiological function
-
protein is essential for growth on fatty acids as well as acetate. Mislocalization of the enzyme to the cytoplasm does not result in loss of growth on acetate but prevents growth on fatty acids. The mitochondrial enzyme is essential for the transfer of acetyl units to mitochondria, peroxisomal localization is required only for transfer from peroxisomes to mitochondria. Peroxisomal enzyme is not required for the import of acetyl-CoA into peroxisomes for conversion to malate by malate synthase, and export of acetyl-CoA from peroxisomes to the cytoplasm is independent of FacC when malate synthase is mislocalized to the cytoplasm
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-keto-4-pentenoyl-CoA + L-(-)carnitine
3-keto-4-pentenoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
?
acetoacetyl-CoA + L-(-)carnitine
O-acetoacetyl(-)carnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + (-)-norcarnitine
acetylnorcarnitine + CoASH
show the reaction diagram
-
beta-hydroxy-gamma-dimethylaminobutyrate
-
-
r
acetyl-CoA + (trishydroxymethyl)glycine
acetyl(trishydroxymethyl)glycine + CoASH
show the reaction diagram
-
-
-
-
?
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
P47934
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
P43155
-
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
-
-
-
?
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
P47934
-
-
-
?
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
Q704S8
-
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
P43155
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
Q704S8
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
this reaction is important in transferring activated acetyl groups to the mitochondria and in regulating the acetyl-CoA/CoA pools within the cell
-
-
?
acetyl-CoA + carnitine
CoA + acetylcarnitine
show the reaction diagram
-
-
-
-
r
acetyl-CoA + choline
acetylcholine + CoA
show the reaction diagram
-
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 + choline
acetylcholine + CoASH
show the reaction diagram
-
-
-
-
?
acetyl-CoA + DL-beta-hydroxy-gamma-aminobutyrate
beta-hydroxybutyrate + CoASH
show the reaction diagram
-
non-methylated derivative of carnitine
-
-
r
acetyl-CoA + DL-norcarnitine
acetylnorcarnitine + CoASH
show the reaction diagram
-
beta-hydroxy-gamma-dimethylaminobutyrate
-
-
r
acetyl-CoA + L-(-)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
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
P47934
-
-
-
r
acetyl-CoA + L-(-)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
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-(-)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
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-(-)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
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-(-)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
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
Torulopsis bovina
-
-
-
-
r
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
Mus musculus S3T3(ATCC CCL-92)
-
-
-
-
r
acetyl-CoA + L-(-)carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
r
acetyl-CoA + tris(hydroxymethyl)aminoethansulfonic acid
acetyl-tris(hydroxymethyl)aminoethansulfonic acid + CoASH
show the reaction diagram
-
-
-
-
?
acetyl-CoA + tris(hydroxymethyl)aminomethane
acetyl-tris(hydroxymethyl)aminomethane + CoASH
show the reaction diagram
-
-
-
-
?
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
P47934
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
Torulopsis bovina
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
Mus musculus S3T3(ATCC CCL-92)
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
P47934
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
Torulopsis bovina
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
Mus musculus S3T3(ATCC CCL-92)
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
r
bromoacetyl-CoA + L-(-)carnitine
bromoacetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
?
butyryl-CoA + carnitine
CoA + O-butyrylcarnitine
show the reaction diagram
-
-
-
-
r
butyryl-CoA + carnitine
CoA + O-butyrylcarnitine
show the reaction diagram
Q704S8
-
-
-
r
butyryl-CoA + carnitine
CoA + O-butyrylcarnitine
show the reaction diagram
-
wild-type enzyme shows maximal activity towards butyryl-CoA
-
-
?
decanoyl-CoA + carnitine
decanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
decanoyl-CoA + carnitine
decanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
decanoyl-CoA + carnitine
decanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
decanoyl-CoA + carnitine
decanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
decanoyl-CoA + carnitine
CoA + O-decanoylcarnitine
show the reaction diagram
-
-
-
-
?
decanoylcarnitine + CoASH
decanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
decanoylcarnitine + CoASH
decanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
decanoylcarnitine + CoASH
decanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
decanoylcarnitine + CoASH
decanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
decanoylcarnitine + CoASH
decanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + carnitine
hexanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + carnitine
hexanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + carnitine
hexanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + carnitine
hexanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + carnitine
hexanoylcarnitine + CoASH
show the reaction diagram
P47934
-
-
-
?
hexanoyl-CoA + carnitine
CoA + O-hexanoylcarnitine
show the reaction diagram
Q704S8
very low activity
-
-
r
hexanoyl-CoA + carnitine
CoA + O-hexanoylcarnitine
show the reaction diagram
-
mutant enzymes M564G and D356A/M564G show maximal activity towards hexanoyl-CoA
-
-
?
hexanoylcarnitine + CoASH
hexanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
hexanoylcarnitine + CoASH
hexanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
hexanoylcarnitine + CoASH
hexanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
hexanoylcarnitine + CoASH
hexanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
isobutyryl-CoA + carnitine
isobutyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
isobutyrylcarnitine + CoASH
isobutyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
isovaleryl-CoA + carnitine
isovalerylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
isovalerylcarnitine + CoASH
isovaleryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
malonyl-CoA + L-(-)carnitine
malonylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyryl-CoA + carnitine
n-butyrylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
n-butyrylcarnitine + CoASH
n-butyryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
n-valeryl-CoA + carnitine
n-valerylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
n-valerylcarnitine + CoASH
n-valeryl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetoacetyl(-)carnitine + CoASH
acetoacetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
P47934
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
Torulopsis bovina
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
Mus musculus S3T3(ATCC CCL-92)
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + L-(-)carnitine
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
P47934
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
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
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
acetate metabolism, enzyme transports activated acetyl group from the cytosol into the mitochondrial matrix
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
key enzyme for the translocation of acetyl units between intracellular compartments
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
mitochondrial fatty acid transport
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
Mus musculus S3T3(ATCC CCL-92)
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
r
octanoyl-CoA + carnitine
octanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
octanoyl-CoA + carnitine
octanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
octanoyl-CoA + carnitine
octanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
octanoyl-CoA + carnitine
octanoylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
octanoyl-CoA + carnitine
CoA + O-octanoylcarnitine
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + carnitine
CoA + O-octanoylcarnitine
show the reaction diagram
Q704S8
very low activity
-
-
r
octanoylcarnitine + CoASH
octanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
octanoylcarnitine + CoASH
octanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
octanoylcarnitine + CoASH
octanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
octanoylcarnitine + CoASH
octanoyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
palmitoyl-CoA + carnitine
CoA + O-palmitoylcarnitine
show the reaction diagram
-
wild-type enzyme shows no activity, mutant enzymes M564G and D356A/M564G show activity
-
-
?
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
propionyl-CoA + L-(-)carnitine
propionylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
propionylcarnitine + CoASH
propionyl-CoA + L-(-)carnitine
show the reaction diagram
-
-
-
-
r
malonylcarnitine + CoASH
malonyl-CoA + L-(-)carnitine
show the reaction diagram
-
slight transfer of the acyl group to carnitine
-
-
r
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
palmitoyl-CoA is no substrate
-
-
-
additional information
?
-
-
palmitoyl-CoA is no substrate
-
-
-
additional information
?
-
-
palmityl-CoA does not act as a substrate for the liver enzyme
-
-
-
additional information
?
-
-
hydroxyethylpiperazineethansulfonic acid is no substrate
-
-
-
additional information
?
-
-
O-acetyl-(+)-carnitine and reduced glutathione will not serve as substrates, succinyl-CoA or beta-hydroxy-betamethylglutaryl-CoA are no substrates
-
-
-
additional information
?
-
-
crotonyl-CoA is no substrate
-
-
-
additional information
?
-
-
octanoyl-CoA and palmitoyl-CoA are no substrates
-
-
-
additional information
?
-
Torulopsis bovina
-
no carnitine acyltransferase activity with acyl CoAs of carbon chain lengths greater than 3
-
-
-
additional information
?
-
-
pentanoyl-CoA, hexanoyl-CoA, decanoyl-CoA and palmitoyl-CoA are no substrates
-
-
-
additional information
?
-
-
only (-) optical isomers are substrates, unnatural (+) isomers are competitive inhibitors
-
-
-
additional information
?
-
-
3-hydroxy-5,5-dimethylhexanoic acid, 3-acetoxy-5,5-dimethylhexanoic acid, R-(+)-3-hydroxy-5,5-dimethylhexanoic acid and S-(-)-3-hydroxy-5,5-dimethylhexanoic acid are not substrates
-
-
-
additional information
?
-
-
D-carnitine is no substrate
-
-
-
additional information
?
-
-
D-carnitine is no substrate
-
-
-
additional information
?
-
Q704S8
wild type enzyme is almost inactive towards longer chain fatty acids, some mutations increases activity towards longer chain fatty acids
-
-
-
additional information
?
-
-
carnitine acetyltransferases are required for growth on non-fermentable carbon sources but not for pathogenesis in Candida albicans, carnitine acetyltransferases are required for growth on non-fermentable carbon sources but not for pathogenesis in Candida albicans. Strains lacking CTN1 or CTN2 are unable to grow on ethanol or acetate as sole carbon source
-
-
-
additional information
?
-
P32796
CAT2 contributes to the response to oxidative stress
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
P47934
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
O-acetylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
P43155
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
Q704S8
modulates acetyl-CoA and CoA availability for a wide range of acyl-transfer reactions, involved in fatty acid metabolism
-
-
r
acetyl-CoA + carnitine
CoA + O-acetylcarnitine
show the reaction diagram
-
this reaction is important in transferring activated acetyl groups to the mitochondria and in regulating the acetyl-CoA/CoA pools within the cell
-
-
?
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
P47934
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
Torulopsis bovina
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
Mus musculus S3T3(ATCC CCL-92)
-
-
-
-
r
acyl-CoA + carnitine
acylcarnitine + CoASH
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
P47934
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
Torulopsis bovina
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
Mus musculus S3T3(ATCC CCL-92)
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
P47934
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
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
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
acetate metabolism, enzyme transports activated acetyl group from the cytosol into the mitochondrial matrix
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
key enzyme for the translocation of acetyl units between intracellular compartments
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
-
mitochondrial fatty acid transport
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
Mus musculus S3T3(ATCC CCL-92)
-
-
-
-
r
O-acetylcarnitine + CoASH
acetyl-CoA + carnitine
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
r
acylcarnitine + CoASH
acyl-CoA + carnitine
show the reaction diagram
Mus musculus BALB/c
-
-
-
-
r
additional information
?
-
-
carnitine acetyltransferases are required for growth on non-fermentable carbon sources but not for pathogenesis in Candida albicans, carnitine acetyltransferases are required for growth on non-fermentable carbon sources but not for pathogenesis in Candida albicans. Strains lacking CTN1 or CTN2 are unable to grow on ethanol or acetate as sole carbon source
-
-
-
additional information
?
-
P32796
CAT2 contributes to the response to oxidative stress
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+)-acetylcarnitine
-
competitive inhibition
(+)-carnitine
-
-
(-)-acetylcarnitine
-
noncompetitive inhibition
(2R,6S:2S,6R)-6-carboxymethyl-2-hydroxy-2,4,4-trimethylmorpholinium chloride
-
hemiacetylcarnitinium
2-bromoacetylcarnitine
-
-
3-(2,2,2-trimethylhydrazinium)-propionate
-
mildronate, competitive (binding to the carnitine binding site)
3-acetoxy-5,5-dimethylhexanoic acid
-
-
3-hydroxy-5,5-dimethylhexanoic acid
-
-
3-keto-4-pentenoyl-CoA
-
inhibitor only in presence of L-carnitine
4-hydroxynonenal
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
acetyl-CoA
-
-
acetyl-D-carnitine
-
-
acetyl-L-(-)-carnitine
-
-
acetylcarnitine
-
competitive inhibition, inhibitor for the forward reaction
acetylcarnitine
-
-
acetylcarnitine
-
-
Acetylcholine
-
competitively inhibits formation of acetylcarnitine
Bromoacetyl-CoA
-
-
bromoacetylcarnitine
-
-
carnitine nitrile
-
-
choline
-
-
choline
-
competitively inhibits formation of acetylcarnitine
CoASH
-
-
D-carnitine
-
-
D-carnitine
-
-
D-carnitine
-
-
deoxycarnitine
-
competitive inhibition
DL-acetyl-beta-methylcholine
-
-
DL-acetylcarnitine
-
competitive inhibition
DL-carnitine
-
-
DL-carnitine
-
inhibitor for the reverse reaction
gamma-aminobutyrate
-
-
HgCl2
-
-
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetic acid
-
-
L-(-)-carnitine
-
-
malondialdehyde
-
-
malonyl-CoA
-
-
Methoxycarbonyl-CoA disulfide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoic acid
-
-
p-Chloromercuriphenyl sulfonic acid
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
palmitoyl-CoA
-
-
Prostigmine
-
-
R-(+)-3-hydroxy-5,5-dimethylhexanoic acid
-
-
S-(-)-3-hydroxy-5,5-dimethylhexanoic acid
-
-
tensilon
-
-
Zn2+
-
inhibition only in reverse direction
Zn2+
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Clofibrate
-
-
Clofibrate
-
mitochondrial enzyme increases in specific activity
Clofibrate
-
enzyme is induced by
diethylhexylphthalate
-
enzyme is induced by
humic acid
-
-
streptozotocin
-
increases enzyme in liver
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
(-)-norcarnitine
-
-
0.31
(-)carnitine
-
-
50
(trishydroxymethyl)glycine
-
-
0.012
acetyl-CoA
-
sperm enzyme
0.014
acetyl-CoA
-
peroxisomal enzyme
0.015
acetyl-CoA
-
-
0.0177
acetyl-CoA
-
-
0.02
acetyl-CoA
-
heart enzyme
0.021
acetyl-CoA
-
-
0.021
acetyl-CoA
-
21C, pH 7.8, wild-type enzyme
0.0213
acetyl-CoA
-
-
0.023
acetyl-CoA
Q704S8
recombinant enzyme from yeast, pH 7.8, 30C
0.023
acetyl-CoA
-
mutant enzyme D356A/M564G
0.032
acetyl-CoA
Q704S8
M564G mutant enzyme from yeast, pH 7.8, 30C
0.0324
acetyl-CoA
-
21C, pH 7.8, mutant enzyme H343E
0.036
acetyl-CoA
-
mitochondrial enzyme
0.038
acetyl-CoA
-
mitochondrial enzyme
0.042
acetyl-CoA
-
peroxisomal enzyme
0.042
acetyl-CoA
P43155
wild type enzyme, pH 8.0
0.044
acetyl-CoA
-
-
0.0596
acetyl-CoA
-
21C, pH 7.8, mutant enzyme S554A/M564G
0.064
acetyl-CoA
P43155
F545Y mutant enzyme, pH 8.0
0.0746
acetyl-CoA
-
21C, pH 7.8, mutant enzyme M564G
0.076
acetyl-CoA
-
-
0.087
acetyl-CoA
P43155
Y431A mutant enzyme, pH 8.0
0.0921
acetyl-CoA
-
21C, pH 7.8, mutant enzyme S554A
0.12
acetyl-CoA
P43155
R497Q mutant enzyme, pH 8.0
0.13
acetyl-CoA
-
-
0.178
acetyl-CoA
P43155
F545A mutant enzyme, pH 8.0
0.188
acetyl-CoA
P43155
T444A mutant enzyme, pH 8.0
0.498
acetyl-CoA
P43155
Y431F mutant enzyme, pH 8.0
0.307
acetyl-DL-carnitine
-
-
0.3
acetyl-L-(-)-carnitine
-
heart enzyme
0.36
acetyl-L-(-)-carnitine
-
sperm enzyme
0.019
acetylcarnitine
-
supplementation with R-alpha-lipoic acid
0.28
acetylcarnitine
-
-
0.39
acetylcarnitine
-
enzyme from liver homogenate
0.417
acetylcarnitine
-
peroxisomal enzyme
0.42
acetylcarnitine
-
-
0.6
acetylcarnitine
-
enzyme from mitochondria
0.639
acetylcarnitine
-
mitochondrial enzyme
0.015
Butyryl-CoA
Q704S8
M564G mutant enzyme from yeast, pH 7.8, 30C
0.0166
Butyryl-CoA
-
-
0.029
Butyryl-CoA
-
-
0.03
Butyryl-CoA
Q704S8
recombinant enzyme from yeast, pH 7.8, 30C
0.038
Butyryl-CoA
-
-
0.0435
Butyryl-CoA
-
-
0.044
Butyryl-CoA
-
-
0.48
butyrylcarnitine
-
enzyme from liver homogenate
0.66
butyrylcarnitine
-
enzyme from mitochondria
0.086
carnitine
-
-
0.086
carnitine
-
cosubstrate propionyl-CoA
0.086
carnitine
Q704S8
M564G mutant enzyme from yeast with octanoyl-CoA as second substrate, pH 7.8, 30C
0.097
carnitine
-
cosubstrate acetyl-CoA
0.101
carnitine
-
wild-type enzyme
0.12
carnitine
-
cosubstrate hexanoyl-CoA
0.148
carnitine
-
cosubstrate octanoyl-CoA
0.152
carnitine
-
cosubstrate butyryl-CoA
0.164
carnitine
Q704S8
M564G mutant enzyme from yeast with hexanoyl-CoA as second substrate, pH 7.8, 30C
0.17
carnitine
Q704S8
M564G mutant enzyme from yeast with butyryl-CoA as second substrate, pH 7.8, 30C
0.203
carnitine
Q704S8
recombinant enzyme from yeast with acetyl-CoA as second substrate, pH 7.8, 30C
0.22
carnitine
Q704S8
recombinant enzyme from yeast with butyryl-CoA as second substrate, pH 7.8, 30C
0.339
carnitine
Q704S8
M564G mutant enzyme from yeast with acetyl-CoA as second substrate, pH 7.8, 30C
0.395
carnitine
-
-
0.4
carnitine
-
-
0.567
carnitine
Q704S8
recombinant enzyme from yeast with hexanoyl-CoA as second substrate, pH 7.8, 30C
0.58
carnitine
-
cosubstrate decanoyl-CoA
0.964
carnitine
Q704S8
recombinant enzyme from yeast with octanoyl-CoA as second substrate, pH 7.8, 30C
1
carnitine
-
mitochondrial enzyme
1.1
carnitine
-
cytosolic enzyme
260
carnitine
-
mutant enzyme T465V/T467N/R518N
300
carnitine
-
above, mutant enzyme A106M/T465V/T467N/R518N
1.1
choline
-
brain enzyme
5
choline
-
heart enzyme
8.7
choline
-
-
18.1
choline
-
mutant enzyme A106M/T465V/T467N/R518N
29
choline
-
mutant enzyme T465V/T467N/R518N
86.4
choline
-
wild-type enzyme
0.009
CoASH
-
-
0.0153
CoASH
-
-
0.018
CoASH
-
supplementation with R-alpha-lipoic acid
0.022
CoASH
-
substrate hexanoylcarnitine, enzyme from liver homogenate
0.024
CoASH
-
substrate decanoylcarnitine, enzyme from liver homogenate
0.027
CoASH
-
substrate butyrylcarnitine and octanoylcarnitine, enzyme from liver homogenate; substrate decanoylcarnitine, enzyme from mitochondria
0.0277
CoASH
-
-
0.028
CoASH
-
substrate acetylcarnitine, enzyme from liver homogenate
0.03
CoASH
-
-
0.032
CoASH
-
substrate acetylcarnitine, enzyme from mitochondria
0.032
CoASH
-
-
0.034
CoASH
-
-
0.037
CoASH
-
-
0.038
CoASH
-
substrate butyrylcarnitine, enzyme from mitochondria
0.041
CoASH
-
-
0.044
CoASH
-
substrate hexanoylcarnitine, enzyme from mitochondria
0.054
CoASH
-
substrate octanoylcarnitine, enzyme from mitochondria
0.069
CoASH
-
-
0.09
CoASH
-
mitochondrial enzyme
0.1
CoASH
-
-
0.11
CoASH
-
cytosolic enzyme
0.257
CoASH
-
mitochondrial enzyme
0.304
CoASH
-
peroxisomal enzyme
0.0287
decanoyl-CoA
-
-
0.064
decanoyl-CoA
-
-
0.64
decanoylcarnitine
-
enzyme from mitochondria
0.66
decanoylcarnitine
-
enzyme from liver homogenate
40
DL-beta-hydroxy-gamma-aminobutyrate
-
-
0.72
DL-carnitine
-
-
3.3
DL-carnitine
-
-
3.2
DL-norcarnitine
-
-
0.02
Hexanoyl-CoA
-
-
0.022
Hexanoyl-CoA
Q704S8
M564G mutant enzyme from yeast, pH 7.8, 30C
0.0224
Hexanoyl-CoA
-
21C, pH 7.8, mutant enzyme M564G
0.033
Hexanoyl-CoA
Q704S8
recombinant enzyme from yeast, pH 7.8, 30C
0.0415
Hexanoyl-CoA
-
21C, pH 7.8, mutant enzyme S554A
0.0549
Hexanoyl-CoA
-
-
0.1034
Hexanoyl-CoA
-
21C, pH 7.8, wild-type enzyme
0.112
Hexanoyl-CoA
-
21C, pH 7.8, mutant enzyme S554A/M564G
2.28
hexanoylcarnitine
-
enzyme from liver homogenate
2.51
hexanoylcarnitine
-
enzyme from mitochondria
0.049
isobutyryl-CoA
-
-
0.039
L-(-)-carnitine
-
-
0.12
L-(-)-carnitine
-
-
0.12
L-(-)-carnitine
-
-
0.15
L-(-)-carnitine
-
-
0.17
L-(-)-carnitine
-
-
0.23
L-(-)-carnitine
-
-
0.244
L-(-)-carnitine
-
-
0.11
L-carnitine
P43155
wild type enzyme, pH 8.0
0.121
L-carnitine
-
cosubstrate butanoyl-CoA
0.15
L-carnitine
P43155
F545Y mutant enzyme, pH 8.0
0.344
L-carnitine
-
cosubstrate hexanoyl-CoA
0.395
L-carnitine
-
cosubstrate octanoyl-CoA
0.519
L-carnitine
-
cosubstrate decanoyl-CoA
0.622
L-carnitine
-
mitochondrial enzyme, second substrate acetyl-CoA
0.655
L-carnitine
-
peroxisomal enzyme, second substrate propionyl-CoA
0.719
L-carnitine
-
peroxisomal enzyme, second substrate acetyl-CoA
0.774
L-carnitine
-
mitochondrial enzyme, second substrate propionyl-CoA
2
L-carnitine
P43155
F545A mutant enzyme, pH 8.0
7.5
L-carnitine
P43155
T444A mutant enzyme, pH 8.0
11.1
L-carnitine
P43155
Y431A mutant enzyme, pH 8.0
25.6
L-carnitine
P43155
R497Q mutant enzyme, pH 8.0
0.041
n-Butyryl-CoA
-
-
0.071
n-valeryl-CoA
-
-
0.011
Octanoyl-CoA
Q704S8
M564G mutant enzyme from yeast, pH 7.8, 30C
0.0191
Octanoyl-CoA
-
-
0.025
Octanoyl-CoA
Q704S8
recombinant enzyme from yeast, pH 7.8, 30C
0.0503
Octanoyl-CoA
-
-
1.27
octanoylcarnitine
-
enzyme from mitochondria
1.39
octanoylcarnitine
-
-
1.62
octanoylcarnitine
-
enzyme from liver homogenate
0.0072
palmitoyl-CoA
-
mutant enzyme D356A/M564G
0.014
propionyl-CoA
-
-
0.0173
propionyl-CoA
-
-
0.028
propionyl-CoA
-
-
0.034
propionyl-CoA
-
peroxisomal enzyme
0.037
propionyl-CoA
-
-
0.1
propionyl-CoA
-
peroxisomal enzyme
0.162
propionyl-CoA
-
mitochondrial enzyme
0.185
propionyl-CoA
-
mitochondrial enzyme
0.65
propionylcarnitine
-
-
35.9
L-carnitine
P43155
Y431F mutant enzyme, pH 8.0
additional information
additional information
-
Km acetylcarnitine 1.25 mg/ml
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.24
acetyl-CoA
-
21C, pH 7.8, wild-type enzyme
0.78
acetyl-CoA
P43155
Y431F mutant enzyme, pH 8.0
1.4
acetyl-CoA
-
21C, pH 7.8, mutant enzyme S554A/M564G
4
acetyl-CoA
-
21C, pH 7.8, mutant enzyme S554A
5.76
acetyl-CoA
P43155
T444A mutant enzyme, pH 8.0
8.57
acetyl-CoA
P43155
F545A mutant enzyme, pH 8.0
15.4
acetyl-CoA
-
21C, pH 7.8, mutant enzyme H343E
28.4
acetyl-CoA
-
21C, pH 7.8, mutant enzyme M564G
30.5
acetyl-CoA
P43155
F545Y mutant enzyme, pH 8.0
38.5
acetyl-CoA
P43155
wild type enzyme, pH 8.0
44.2
acetyl-CoA
P43155
Y431A mutant enzyme, pH 8.0
94.8
acetyl-CoA
P43155
R497Q mutant enzyme, pH 8.0
97.6
acetyl-CoA
-
21C, pH 7.8, wild-type enzyme
0.98
carnitine
-
above, mutant enzyme A106M/T465V/T467N/R518N
2.97
carnitine
-
mutant enzyme T465V/T467N/R518N
86.9
carnitine
-
wild-type enzyme
1.58
choline
-
wild-type enzyme
2.43
choline
-
mutant enzyme T465V/T467N/R518N
3.11
choline
-
mutant enzyme A106M/T465V/T467N/R518N
1.42
Hexanoyl-CoA
-
21C, pH 7.8, mutant enzyme S554A
8.2
Hexanoyl-CoA
-
21C, pH 7.8, mutant enzyme S554A/M564G
30.4
Hexanoyl-CoA
-
21C, pH 7.8, wild-type enzyme
89
Hexanoyl-CoA
-
21C, pH 7.8, mutant enzyme M564G
104.7
Hexanoyl-CoA
-
21C, pH 7.8, mutant enzyme M564G
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.25
(+)-acetylcarnitine
-
-
2.1
(+)carnitine
-
-
0.89
(2R,6S:2S,6R)-6-carboxymethyl-2-hydroxy-2,4,4-trimethylmorpholinium chloride
-
-
4.72
(2R,6S:2S,6R)-6-carboxymethyl-2-hydroxy-2,4,4-trimethylmorpholinium chloride
-
-
1.6
3-(2,2,2-trimethylhydrazinium)-propionate
-
0.0625 mM carnitine
4.1
3-acetoxy-5,5-dimethylhexanoic acid
-
reverse direction
8.3
3-hydroxy-5,5-dimethylhexanoic acid
-
-
0.047
acetyl-CoA
-
heart enzyme
0.052
acetyl-CoA
-
sperm enzyme
0.81
acetyl-L-(-)-carnitine
-
heart enzyme
0.98
acetyl-L-(-)-carnitine
-
sperm enzyme
920
acetylcarnitine
-
substrate DL-carnitine
2.6
Ca2+
-
-
27
choline
-
-
0.015
CoASH
-
sperm enzyme
0.021
CoASH
-
heart enzyme
0.0046
Cu2+
-
-
1
D-carnitine
-
-
1.1
D-carnitine
-
-
2.3
deoxycarnitine
-
-
1.2
deoxynorcarnitine
-
-
71
DL-acetyl-beta-methylcholine
-
-
0.39
DL-acetylcarnitine
-
-
0.2
DL-carnitine
-
-
0.62
DL-carnitine
-
-
44
gamma-aminobutyrate
-
-
0.25
L-(-)-carnitine
-
heart enzyme
0.31
L-(-)-carnitine
-
sperm enzyme
1.5
Mg2+
-
-
0.016
palmitoyl-CoA
-
-
8
palmityl-CoA
-
substrate carnitine
18.6
palmityl-CoA
-
substrate acetyl-CoA
12
Prostigmine
-
-
20.3
R-(+)-3-hydroxy-5,5-dimethylhexanoic acid
-
-
7.5
S-(-)-3-hydroxy-5,5-dimethylhexanoic acid
-
-
15
tensilon
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.44
3-(2,2,2-trimethylhydrazinium)-propionate
-
0.0625 mM carnitine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.002
-
carbon source glucose, peroxisomal enzyme
0.005
-
liver
0.04
-
carbon source serum, peroxisomal enzyme
0.06
-
carbon source glucose, mitochondrial enzyme
0.25
-
skeletal muscle
0.27
-
carbon source serum, mitochondrial enzyme
4.5
-
carbon source triolein, mitochondrial enzyme
8.8
-
carbon source triolein, peroxisomal enzyme
71
-
source heart
78.75
-
-
80
-
cytoplasmic CAT
85
-
source spermatozoon
88
-
peroxisomal CAT
88.5
-
peroxisomal enzyme
113
-
mitochondrial CAT
120
-
purified from postmitochondrial fraction
220
-
purified from liver homogenate
240
-
purified from mitochondrial fraction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 7.8
-
peroxisomal enzyme
8
-
mitochondrial enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
-
-
4.5 - 8.5
-
-
5.5 - 10
-
-
6 - 10
-
-
6 - 9
-
activity declines rapidly on either side of the optimum pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
carnitine acetyltransferase is highly active in neuronal tissues and in neuronal cell cultures relative to choline acetyl transferase
Manually annotated by BRENDA team
Mus musculus S3T3(ATCC CCL-92)
-
-
-
Manually annotated by BRENDA team
-
Crat is most highly expressed in heart, brown adipose tissue and white adipose tissue
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Mus musculus S3T3(ATCC CCL-92)
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley, Mus musculus S3T3(ATCC CCL-92), Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
breast muscle
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
fetal rat cerebrocortical neuron culture, strong enzyme activity
Manually annotated by BRENDA team
Mus musculus S3T3(ATCC CCL-92)
-
-
-
Manually annotated by BRENDA team
additional information
-
carnitine acetyltransferase is highly active in neuronal tissues and in neuronal cell cultures relative to choline acetyl transferase
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
isoforms Yat1 and Yat2
Manually annotated by BRENDA team
-
membrane bound
-
Manually annotated by BRENDA team
Torulopsis bovina
-
-
Manually annotated by BRENDA team
Torulopsis bovina
-
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
sequence contains a N-terminal mitochondrial targeting sequence and a C-terminal peroxisomal targeting sequence and protein is localized to both peroxisomes and mitochondria
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
membrane-bound
-
Manually annotated by BRENDA team
Mus musculus S3T3(ATCC CCL-92)
-
-
-
Manually annotated by BRENDA team
Mus musculus Sv/129
-
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
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
sequence contains a N-terminal mitochondrial targeting sequence and a C-terminal peroxisomal targeting sequence and protein is localized to both peroxisomes and mitochondria
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
-
-
487404
55000
-
gel filtration
487397, 487403
56000
-
gel filtration
487403
56000
-
purified from mitochondrial fraction of liver, rats fed on a diet containing ethyl p-chlorophenoxyisobutyrate
487408
58000
-
-
487412, 487423
59000
-
microsomal and peroxisomal enzyme
487404
59000
-
gel filtration, native and SDS-PAGE
487423
59000
-
-
487423
60000
-
gel filtration
486295
60000
-
SDS-PAGE
487405
60000
-
SDS-PAGE
487420
60000
-
-
487423
60500
-
gel filtration
487416
60500
-
-
487423, 487424
61000
-
heart enzyme, gel filtration, SDS-PAGE
487407
61900
-
purified from mitochondrial fraction, gel filtration
487408
62000
-
-
487404
62000
-
sperm enzyme, gel filtration, SDS-PAGE
487407
62000
-
-
487407, 487417
62000
-
-
487424
64000
-
SDS-PAGE
487415, 487426
66000
-
mitochondrial CAT
487425
66100
-
purified from liver homogenate, gel filtration
487408
66450
-
deduced amino acid sequence, mitochondrial enzyme
487426
67000
-
-
487423
67500
-
purified from liver homogenate, SDS-PAGE
487408, 487424
68000
-
peroxisomal and cytosolic CAT
487425
68190
-
deduced amino acid sequence, peroxisomal enzyme
487426
69000
-
post-mitochondrial fraction, 2 polypeptides 67500 Da + 69000 Da cannot be separated from each other; translation product of the enzyme by the reticulocyte lysate protein-synthesizing system
487408
70710
-
nucleotide sequence analysis
487426
75000
-
SDS-PAGE
487403
77000
-
gel filtration
487424
400000
-
-
487418
415000
-
peroxisomal enzyme, meniscus depletion technique
487410
420000
-
gel filtration, analytical ultracentrifugation
487410, 487415
426000
-
mitochondrial enzyme, meniscus depletion technique
487410
540000
-
gel filtration
487415
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q704S8
x * 70800, deduced from amino acid sequence
?
-
x * 68500, calculated
dimer
-
2 * 39000, SDS-PAGE
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
dimer
Rattus norvegicus Sprague-Dawley
-
1 * 34000 + 1 * 25000, purified from mitochondrial fraction of liver, rats fed on a diet containing ethyl p-chlorophenoxyisobutyrate, SDS-PAGE
-
hexamer
-
6 * 65000, SDS-PAGE
monomer
-
-
monomer
-
-
monomer
-
1 * 75000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 59000, SDS-PAGE
monomer
-
1 * 60500, SDS-PAGE
monomer
-
1 * 62000, monomeric in presence of catalytic amounts of substrate, SDS-PAGE
monomer
-
1 * 61000, heart enzyme, SDS-PAGE, 1 * 62000, sperm enzyme, SDS-PAGE
monomer
-
crystal structure analysis
monomer
-
wild type and mutant enzymes
monomer
Rattus norvegicus Sprague-Dawley
-
-
-
octamer
-
8 * 64000, SDS-PAGE, immunoblotting
octamer
-
4 * 64000 + 4 * 57000, peroxisomal enzyme, heterooligomer, SDS-PAGE, 4 * 64000 + 4 * 52000, mitochondrial enzyme, heterooligomer, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
sequence contains a N-terminal mitochondrial targeting sequence and a C-terminal peroxisomal targeting sequence and protein is localized to both peroxisomes and mitochondria
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized in the presence of L-carnitine by vapor diffusion method
P43155
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
-
peroxisomal enzyme
-
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, 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
-
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
P47934
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
-
microsomal transferase is more stable at pH 7.5 than at pH 6.0
487404
6 - 9
-
below pH 6.0 enzyme undergoes irreversible inactivation
487418
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 25
-
stored in a refrigerator for 2 days or incubated at 25C for 5 h, monomeric form remains unchanged
487408
4
-
precipitated enzyme is stable at
487397
37 - 50
-
enzyme retains total activity when kept at 37C for 30 min, rapid loss of activity above 37C, loses half of the activity at 40C for 30 min, but is completely inactivated when kept at 44C for 30 min or 50C for 5 min, 75% loss of activity at 37C for 8 h, only 15% loss when kept at 25C for 8 h
487403
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated under the conditions of freeze/thaw
-
enzyme is abolished by detergents, hypotonic media or freeze-thawing
-
proteolytic degradation can occur during purification from liver
-
enzyme is stable throughout purification procedure
-
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
-
very unstable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, retains 60-80% activity over a period of several months
-
0-4C, loses little activity when stored for months
-
4C, enzyme is abolished by prolonged storage
-
-20C, when stored in 50% glycerol, maintains its activity unaltered for several months
-
-20C, 0.05% bovine albumin, repeated thawing and freezing does not significantly affect enzyme activity over a period of several months
-
-20C, 50 mM potassium phosphate buffer, pH 7.5, purified enzyme can be stored for several months without loss of activity
-
-20C, frozen mitochondrial fraction can be stored for several months without loss of activity
-
-20C, peroxisomal and microsomal fractions from isopycnic sucrose density gradients, activity is stable during storage for at least 3 months
-
-20C, 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
-
0-4C, loses little activity when stored for months
-
4C, peroxisomal and microsomal fractions from isopycnic sucrose density gradients, activity is stable during storage for 10 days
-
4C, 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
mitochondrial and cytosolic enzyme
-
partially
-
mitochondrial and peroxisomal enzyme
-
recombinant protein using His-tag
P43155
recombinant enzyme using His-tag
-
purification of GST-fusion proteins from Escherichia coli
Q704S8
purified from mitochondrial fraction and from homogenate of frozen liver
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both enzymes encoded by one gene, CT-CAT, cloned and expressed in Saccharomyces cerevisiae
-
genomic DNA clone isolated from the yeast lambda EMBL library sequenced and expressed in Saccharomyces cerevisiae
-
cloning, sequencing and heterologous expression of cDNA
-
cDNA cloned, mapping of the corresponding gene to chromosome 9q34.1
-
expressed as His-tag fusion protein in Escherichia coli
P43155
hCAT, cloned and expressed in Escherichia coli
-
single-gene product with multiple targeting signals
-
-
P47934
residues 30-626 expressed as His-tag fusion protein in Escherichia coli
-
sequence analysis of full-length cDNA clone
P47934
expressed in Saccharomyces cerevisiae and Escherichia coli
Q704S8
expression in Escherichia coli or Saccharomyces cerevisiae
-
cDNA cloned and sequenced
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F545A
P43155
increases Km for both substrates
F545Y
P43155
minor effects on Km for both substrates
R497Q
P43155
increases Km for both substrates
T444A
P43155
increases Km for both substrates
Y431A
P43155
increases Km for both substrates
Y431F
P43155
increases Km for both substrates
F565A
-
used for crystallization, only minor effect on protein structure, increased activity with acetyl-CoA
H343A
-
mutant enzymje shows no activity with acetyl-CoA and hexanoyl-CoA
H343E
-
kcat/KM for acetyl-CoA is 9.8fold lower than wild-type value, mutant enzyme shows mo activity with hexanoyl-CoA as substrate
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
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
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
E347A
Q704S8
complete loss of activity
H343A
Q704S8
complete loss of activity
M564A
Q704S8
lowered activity with acetyl-CoA, increased activity with longer chain acyl-CoAs
M564G
Q704S8
lowered activity with acetyl-CoA, increased activity with longer chain acyl-CoAs, 1250-fold increase in activity with myristoyl-CoA
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
specific activity is higher than in commercial preparations from other sources, enzyme prepared from yeast may be used for determination of carnitine in biological materials, this preparation is free of acetyl-CoA-deacetylase activity
analysis
-
determination of free and total carnitine in plasma by an enzymatic reaction and spectrophotometric quantitation spectrophotometric determination of carnitine. the detection limit is 0.0017 mM/l in plasma
analysis
-
in medicine and biochemical practice, the enzyme isolated from breast muscle is used analytically
analysis
-
enzyme in pure form facilitates assay of carnitine and its acyl derivatives in tissues
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
-
-
medicine
-
dysregulation of the enzyme can lead to serious diseases in humans, inherited deficiency in CRAT activity can lead to neurological and heart problems, patients suffering from Alzheimer 's disease also have reduced CRAT activity, promising target for therapeutic development against several human diseases like diabetes
medicine
-
pharmacological applications, patients suffering from CARAT deficiency, serious neurological, motor, repiratory and heart problems observed
medicine
-
CAT is clinically used in evaluating L-CA and its esters in body fluids and tissues
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
food industry
-
modulating aroma compounds during wine fermentation by manipulating carnitine acetyltransferases in Saccharomyces cerevisiae