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Information on EC 2.3.1.137 - carnitine O-octanoyltransferase
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EC Tree
2.3.1.137 carnitine O-octanoyltransferaseIUBMB Comments
Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC 2.3.1.21 (carnitine O-palmitoyltransferase).
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Word Map
- 2.3.1.137
- peroxisomal
- acyl-coas
-
beta-oxidation
- malonyl-coa
- acylcarnitine
- palmitoyl-coa
-
ketogenesis
- decanoyl-coa
-
carnitine-dependent
-
crats
-
arrhythmogenesis
- 2-bromopalmitate
-
cpt-ii
-
malonyl-coa-sensitive
- etomoxir
- palmitoylcarnitine
The enzyme appears in viruses and cellular organisms
Synonyms
carnitine acyltransferase, carnitine octanoyltransferase, carnitine o-octanoyltransferase, medium-chain/long-chain carnitine acyltransferase, medium-chain carnitine acyltransferase, overt mitochondrial carnitine palmitoyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carnitine acyltransferase
Carnitine medium-chain acyltransferase
-
-
-
-
carnitine octanoyltransferase
COT
CRAT
CrOT
easily solubilized mitochondrial carnitine palmitoyltransferase
-
-
-
-
medium-chain/long-chain carnitine acyltransferase
-
-
-
-
overt mitochondrial carnitine palmitoyltransferase
-
-
-
-
additional information
additional information
-
enzyme belongs to the family of carnitine acyltransferases
additional information
the enzyme belongs to the carnitine acyltransferase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
-
-
-
-
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
acyl-binding hydrophobic pocket structure involving residues G553, C323, and Met335, the acyl-CoA substrate chain length specificity is determined by G553, Met335 is important for catalysis
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
acyl-CoA substrate specificity is determined by Gly553, active site structure and substrate positioning modeling
-
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
catalytic mechanism, active site structure, substrate recognition mechanism, amino acid residues 343, 564 and 553 determine the acyl-CoA substrate specificity, catalytic residue is His343
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
Acyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
octanoyl-CoA:L-carnitine O-octanoyltransferase
Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC 2.3.1.21 (carnitine O-palmitoyltransferase).
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CAS REGISTRY NUMBER
COMMENTARY
39369-19-2
-
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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
3-hydroxy-3-methylglutaryl-CoA + L-carnitine
3-hydroxy-3-methylglutaryl-L-carnitine + CoA
-
-
-
-
r
3-methylglutaryl-CoA + L-carnitine
3-methylglutaryl-L-carnitine + CoA
-
little capacity to use this substrate
-
-
r
3-methylglutaryl-L-carnitine + CoA
3-methylglutaryl-CoA + L-carnitine
-
-
-
-
r
4,8-dimethylnonanoyl-CoA + L-carnitine
4,8-dimethylnonanoyl-L-carnitine + CoA
-
-
-
r
4,8-dimethylnonanoyl-L-carnitine + CoA
4,8-dimethylnonanoyl-CoA + L-carnitine
-
-
-
r
beta-hydroxy-beta-methylglutaryl-L-carnitine + CoA
beta-hydroxy-beta-methylglutaryl-CoA + L-carnitine
-
-
-
-
r
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
best substrate
-
-
?
hexadecanoyl-CoA + L-carnitine
CoA + L-hexadecanoylcarnitine
-
low activity
-
-
?
pivaloyl-CoA + L-carnitine
L-pivaloyl-L-carnitine + CoA
-
little capacity to use this substrate
-
-
r
valproyl-CoA + L-carnitine
L-valproyl-L-carnitine + CoA
-
little capacity to use this substrate
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
central role in fatty acid metabolism
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
metabolic pathway of peroxisomal beta-oxidation in yeasts
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
gamma-trimethylamino-beta-hydroxybutyrate
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
486290, 486291, 486292, 486293, 486294, 486295, 486296, 486297, 486298, 486299, 486300, 486301, 486304, 486308, 486309
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
gamma-trimethylamino-beta-hydroxybutyrate
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
beta-oxidation of fatty acids
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
gamma-trimethylamino-beta-hydroxybutyrate
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
-
r
acyl-L-carnitine + CoA
acyl-CoA + L-carnitine
-
-
-
-
r
acyl-L-carnitine + CoA
acyl-CoA + L-carnitine
-
-
-
-
r
decanoyl-CoA + L-carnitine
L-decanoyl-L-carnitine + CoA
-
-
-
-
r
decanoyl-CoA + L-carnitine
L-decanoyl-L-carnitine + CoA
-
-
-
-
r
decanoyl-L-carnitine + CoA
decanoyl-CoA + L-carnitine
-
-
-
-
r
decanoyl-L-carnitine + CoA
decanoyl-CoA + L-carnitine
-
-
-
-
r
dodecanoyl-CoA + L-carnitine
L-dodecanoyl-L-carnitine + CoA
-
-
-
-
r
dodecanoyl-CoA + L-carnitine
L-dodecanoyl-L-carnitine + CoA
-
-
-
-
r
dodecanoyl-L-carnitine + CoA
dodecanoyl-CoA + L-carnitine
-
-
-
-
r
dodecanoyl-L-carnitine + CoA
dodecanoyl-CoA + L-carnitine
-
-
-
-
r
heptanoyl-CoA + L-carnitine
L-heptanoyl-L-carnitine + CoA
-
-
-
-
r
heptanoyl-L-carnitine + CoA
heptanoyl-CoA + L-carnitine
-
-
-
-
r
hexadecanoyl-CoA + L-carnitine
L-hexadecanoyl-L-carnitine + CoA
-
-
-
-
r
hexadecanoyl-CoA + L-carnitine
L-hexadecanoyl-L-carnitine + CoA
-
-
-
-
r
hexadecanoyl-L-carnitine + CoA
hexadecanoyl-CoA + L-carnitine
-
-
-
-
r
hexadecanoyl-L-carnitine + CoA
hexadecanoyl-CoA + L-carnitine
-
-
-
-
r
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
-
-
-
-
r
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
-
-
-
-
r
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
-
best substrate
-
-
?
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
-
-
-
-
r
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
L-hexanoylcarnitine + CoA
hexanoyl-CoA + L-carnitine
-
-
-
-
r
L-hexanoylcarnitine + CoA
hexanoyl-CoA + L-carnitine
-
-
-
-
r
L-hexanoylcarnitine + CoA
hexanoyl-CoA + L-carnitine
-
-
-
-
r
L-hexanoylcarnitine + CoA
hexanoyl-CoA + L-carnitine
-
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
-
step in the transport of fatty acids across the inner mitochondrial membrane, reaction plays a role in balancing cellular CoA:acyl-CoA ratio
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
-
carnitine binding site structure involving the highly conserved R518, Y452 and T465, CoA binding site n the active site tunnel via His343, fatty acid binding site
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
preferred substrate
-
-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
-
-
-
-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
-
-
-
-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
-
-
-
-
r
palmitoyl-CoA + L-carnitine
L-palmitoyl-L-carnitine + CoA
-
-
-
-
r
palmitoyl-CoA + L-carnitine
L-palmitoyl-L-carnitine + CoA
-
-
-
-
r
palmitoyl-CoA + L-carnitine
L-palmitoyl-L-carnitine + CoA
-
-
-
-
r
palmitoyl-L-carnitine + CoA
palmitoyl-CoA + L-carnitine
-
-
-
-
r
palmitoyl-L-carnitine + CoA
palmitoyl-CoA + L-carnitine
-
-
-
-
r
palmitoyl-L-carnitine + CoA
palmitoyl-CoA + L-carnitine
-
-
-
-
r
tetradecanoyl-CoA + L-carnitine
CoA + L-tetradecanoylcarnitine
low activity
-
-
?
additional information
?
-
2,6-dimethyl-heptanoyl-CoA is not a substrate
-
-
?
additional information
?
-
-
2,6-dimethyl-heptanoyl-CoA is not a substrate
-
-
?
additional information
?
-
-
peroxisomal carnitine acyltransferases and acyl-CoA thioesterases are differently expressed to function as complementary enzymes for transport of beta-oxidation metabolites
-
-
?
additional information
?
-
-
peroxisomes contain carnitine acetyltransferase and octanoyltransferase that produce carnitine ester for transport out of the peroxisomes
-
-
?
additional information
?
-
-
peroxisomal carnitine acyltransferases and acyl-CoA thioesterases are differently expressed to function as complementary enzymes for transport of beta-oxidation metabolites
-
-
?
additional information
?
-
-
peroxisomes contain carnitine acetyltransferase and octanoyltransferase that produce carnitine ester for transport out of the peroxisomes
-
-
?
additional information
?
-
-
succinyl-CoA and beta-hydroxy-beta-methylglutaryl-CoA are no substrates
-
-
?
additional information
?
-
-
acyl-CoA substrate specificity is determined by Gly553
-
-
?
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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
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
central role in fatty acid metabolism
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
metabolic pathway of peroxisomal beta-oxidation in yeasts
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
486290, 486291, 486292, 486293, 486294, 486295, 486296, 486297, 486298, 486299, 486300, 486301, 486304, 486308
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
beta-oxidation of fatty acids
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
-
r
acyl-L-carnitine + CoA
acyl-CoA + L-carnitine
-
-
-
-
r
acyl-L-carnitine + CoA
acyl-CoA + L-carnitine
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
-
step in the transport of fatty acids across the inner mitochondrial membrane, reaction plays a role in balancing cellular CoA:acyl-CoA ratio
-
-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
-
-
-
-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
-
-
-
-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
-
-
-
-
r
additional information
?
-
-
peroxisomal carnitine acyltransferases and acyl-CoA thioesterases are differently expressed to function as complementary enzymes for transport of beta-oxidation metabolites
-
-
?
additional information
?
-
-
peroxisomes contain carnitine acetyltransferase and octanoyltransferase that produce carnitine ester for transport out of the peroxisomes
-
-
?
additional information
?
-
-
peroxisomal carnitine acyltransferases and acyl-CoA thioesterases are differently expressed to function as complementary enzymes for transport of beta-oxidation metabolites
-
-
?
additional information
?
-
-
peroxisomes contain carnitine acetyltransferase and octanoyltransferase that produce carnitine ester for transport out of the peroxisomes
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
etomoxir
-
hypoglycaemia-inducing drug, double mutant H131A/H340A is insensitive to etomoxir
malonyl-CoA
-
inhibits the purified enzyme, inhibition is affected by buffer, pH, substrate and presence or absence of bovine serum albumin
malonyl-CoA
-
regulatory role, enzyme belongs to the group of malonyl-CoA inhibitable carnitine acyltransferases with highly conserved residues being involved in the inhibition, i.e. Thr314, Asn464, Ala478, Met593, and Cys608, amino acid sequence comparison with enzymes from other species
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
retains its maximum activity when preincubated at pH 7.0 or 8.5
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cardiomyopathies
Cardiac carnitine acyltransferase activities in exercised normal and dystrophic hamsters.
carnitine o-palmitoyltransferase deficiency
Carnitine acyltransferases in normal human skeletal muscle and in muscle of patients with carnitine palmitoyltransferase deficiency.
Cholestasis
Inhibition of carnitine acyltransferase activities by bile acids in rat liver peroxisomes.
Diabetes Mellitus
[14C]palmitate uptake in isolated rat liver mitochondria: effects of fasting, diabetes mellitus, and inhibitors of carnitine acyltransferase.
Ischemic Contracture
Cellular uncoupling induced by accumulation of long-chain acylcarnitine during ischemia.
Myocardial Ischemia
Delineation of the influence of propionylcarnitine on the accumulation of long-chain acylcarnitines and electrophysiologic derangements evoked by hypoxia in canine myocardium.
Myocardial Ischemia
Selected metabolic alterations in the ischemic heart and their contributions to arrhythmogenesis.
Peroxisomal Disorders
Peroxisomal proliferation in heart and liver of mice receiving chlorpromazine, ethyl 2(5(4-chlorophenyl)pentyl) oxiran-2-carboxylic acid or high fat diet: a biochemical and morphometrical comparative study.
Pregnancy, Prolonged
Hepatic mitochondrial fatty acid oxidation during the perinatal period in the rat.
Starvation
Effect of carnitine on branched-chain amino acid oxidation by liver and skeletal muscle.
Starvation
Hepatic mitochondrial fatty acid oxidation during the perinatal period in the rat.
Starvation
Hormonal control of ketogenesis. Rapid activation of hepatic ketogenic capacity in fed rats by anti-insulin serum and glucagon.
Tachycardia, Ventricular
Recent insights pertaining to sarcolemmal phospholipid alterations underlying arrhythmogenesis in the ischemic heart.
Tachycardia, Ventricular
Selected metabolic alterations in the ischemic heart and their contributions to arrhythmogenesis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0167
acyl-CoA
-
mutant strain expressed in Saccharomyces cerevisiae COT A238D
0.002
decanoyl-CoA
-
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTwt
0.002
decanoyl-CoA
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTwt
0.0026
decanoyl-CoA
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTH340A/H131
0.006
decanoyl-CoA
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTH340
0.013
decanoyl-CoA
-
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTH340A/H131
0.106
L-carnitine
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTH340A
0.117
L-carnitine
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTH340A/H131
0.172
L-carnitine
-
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTwt
0.172
L-carnitine
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTwt
146
L-carnitine
-
recombinant enzyme expressed in Saccharomyces cerevisiae COT238D
160
L-carnitine
recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTH131A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
substrate specificity of wild-type and mutant enzymes, overview
additional information
-
substrate specificity of wild-type and mutant enzymes, overview
additional information
-
acyl-CoA substrate specificity of wild-type and G553M mutant enzymes, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fed lipid-lowering drug diet containing clofibrate, nafenopin or Wy-14,643
-
-
brenda
feeding of phytol results in induction of carnitine O-octanoyltransferase as well as catalase, phytanoyl-CoA hydroxylase, peroxisomal 3-ketoacyl-CoA thiolase, and straight-chain acyl-CoA oxidase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
low in distal intestine epithelium, distal intestine muscle, brain, heart, lung, spleen, brown and white adipose tissue
brenda
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the crat gene contains 2 alternative start codons, translation from the first codon results in a protein of 626 amino acids, with a 21-amino acid leader sequence that targets the CRAT protein to mitochondria
brenda
-
the crat gene contains 2 alternative start codons, translation from the first codon results in a protein of 626 amino acids, with a 21-amino acid leader sequence that targets the CRAT protein to mitochondria
-
brenda
-
-
brenda
-
in the peroxisomal CRAT mRNA, there is an in-frame stop codon and translation starts at a downstream second start codon, resulting in a protein that contains 605 amino acids
brenda
-
in the peroxisomal CRAT mRNA, there is an in-frame stop codon and translation starts at a downstream second start codon, resulting in a protein that contains 605 amino acids
-
brenda
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
overexpression and knock-down of the enzyme gene in a model of hepatic cells. Increase in enzymic activity induces a decrease in medium chain fatty acid and very long chaichain fatty acid levels in the cell. These changes are accompanied by an increase in the level of mRNA encoding enzymes of the peroxisomal beta oxidation, while there is no change in mitochondrial function. A decrease in carnitine ocatanoyltransferase activity has the opposite effect. Results suggest that carnitine ocatanoyltransferase activity, by controlling the peroxisomal amount of medium chain acyls, may control the peroxisomal oxidative pathway
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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_COLLI
627
0
71067
Swiss-Prot
other Location (Reliability: 3)
CACP_HUMAN
626
0
70858
Swiss-Prot
Mitochondrion (Reliability: 2)
CACP_MOUSE
626
0
70840
Swiss-Prot
Mitochondrion (Reliability: 3)
CACP_RAT
626
0
70801
Swiss-Prot
Mitochondrion (Reliability: 3)
OCTC_BOVIN
612
0
70263
Swiss-Prot
other Location (Reliability: 1)
OCTC_HUMAN
612
0
70178
Swiss-Prot
other Location (Reliability: 1)
OCTC_MOUSE
612
0
70264
Swiss-Prot
other Location (Reliability: 1)
OCTC_RAT
612
0
70302
Swiss-Prot
other Location (Reliability: 1)
Q9VB02_DROME
618
0
71213
TrEMBL
other Location (Reliability: 2)
A0A061IKE6_CRIGR
804
0
93071
TrEMBL
other Location (Reliability: 1)
A0A812BEV5_SEPPH
658
0
75647
TrEMBL
Mitochondrion (Reliability: 3)
E0VA16_PEDHC
625
0
72037
TrEMBL
other Location (Reliability: 5)
B7PGB4_IXOSC
144
0
16342
TrEMBL
other Location (Reliability: 3)
G0QWB2_ICHMG
Ichthyophthirius multifiliis (strain G5)
2347
0
276110
TrEMBL
other Location (Reliability: 4)
A0A8B6GWH6_MYTGA
620
0
70778
TrEMBL
other Location (Reliability: 1)
A0A061ILJ9_CRIGR
714
0
82517
TrEMBL
other Location (Reliability: 1)
A0A061INH4_CRIGR
742
0
85814
TrEMBL
other Location (Reliability: 1)
Q503F8_DANRE
612
1
69402
TrEMBL
other Location (Reliability: 2)
B5DEC4_XENTR
481
0
55031
TrEMBL
other Location (Reliability: 1)
B5DEC4_XENTR
481
0
55031
TrEMBL
other Location (Reliability: 1)
A0A8B6GXH2_MYTGA
620
0
70777
TrEMBL
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
active site structure and substrate positioning modeling for wild-type and G553M mutant enzymes
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and mutants M335V and C323M enzymes free or in complex with octanoylcarnitine, sitting drop vapour diffusion method, 4°C, reservoir solution contains 0.1 M HEPES, pH 7.4, 62% v/v 2-methyl-2,4-pentanediol, larger crystals by micro- and macroseeding, cross-seeding of recombinant purified selenomethionine-labeled enzyme, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R518N
-
site-directed mutagenesis, mutant shows 1650fold increased Km for L-carnitine, only slightly affected Km for acyl-CoA and kcat compared to the wild-type enzyme
S552A
-
site-directed mutagenesis, mutant shows 17fold increased Km for L-carnitine compared to the wild-type enzyme
S554X
-
site-directed mutagenesis, mutant shows 10fold decreased kcat compared to the wild-type enzyme
C323M
site-directed mutagenesis, crystal structure comparison with the wild-type enzyme, altered acyl-CoA substrate specificity compared to the wild-type enzyme, highly increased specificity for octanoyl-CoA
G553M
site-directed mutagenesis, highly reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
M335A
site-directed mutagenesis, reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
M335V
site-directed mutagenesis, crystal structure comparison with the wild-type enzyme, highly reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
G553M
-
site-directed mutagenesis, the mutant enzyme shows altered substrate specificity: highly reduced activity with medium- and long-chain acyl-CoAs and increased activity with acetyl-CoA and butanoyl-CoA compared to the wild-type enzyme
additional information
-
the carnitine acetyl-transferase, specific for acetyl-CoA/short-chain acyl-CoAs, can be modified to an enzyme with elevated carnitine octanoyltransferase activity by mutation of Met564 to Gly, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
quite unstable, labile in Triton X-100 and octylglucoside, stable in 8 mM CHAPS, 200 mM guanidium chloride and 0.5% Tween 20
-
stable for at least 1 week in 100 mM phosphate buffer with 0.4 M KCl, pH 5.5-7.5
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
soluble recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA clone from a rat liver library, 2 forms of COT in peroxisomes results of the trans-splicing mechanism in pre-mRNAs
-
cDNA cloning by library screening and recombinant expression in Escherichia coli
-
cDNA PCR amplified, cloned in yeast expression vector pEL26 and expressed in Saccharomyces cerevisiae
expression of wild-type and G553M mutant enzymes in an enzyme-deficient Saccharomyces cerevisiae strain
-
overexpression of the His-tagged enzyme in Escherichia coli as soluble protein, expression of enzyme for selenomethionine-labeling in Escherichia coli strain B834(DE3)
pYES2 plasmid containing the wild-type and the double mutant H131A/H340A of COT expressed in Saccharomyces cerevisiae
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Solberg, H.E.
Different carnitine acyltransferases in calf liver
Biochim. Biophys. Acta
280
422-433
1972
Bos taurus, Canis lupus familiaris, Columba sp., Oryctolagus cuniculus, Homo sapiens, Platyrrhini, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Solberg, H.E.
Acyl group specificity of mitochondrial pools of carnitine acyltransferases
Biochim. Biophys. Acta
360
101-112
1974
Bos taurus, Mus musculus, Rattus norvegicus, Mus musculus NMRI/Bom, Rattus norvegicus Wistar/Moell
brenda
Markwell, M.A.K.; Tolbert, N.E.; Bieber, L.L.
Comparison of the carnitine acyltransferase activities from rat liver peroxisomes and microsomes
Arch. Biochem. Biophys.
176
479-488
1976
Columba sp., Rattus norvegicus, Sus scrofa
-
brenda
Saggerson, E.D.; Carpenter, C.A.
Malonyl CoA inhibition of carnitine acyltransferase activities: effects of thiol-group reagents
FEBS Lett.
137
124-128
1982
Rattus norvegicus
brenda
Farrell, S.O.; Bieber, L.L.
Carnitine octanoyltransferase of mouse liver peroxisomes: properties and effect of hypolipidemic drugs
Arch. Biochem. Biophys.
222
123-132
1983
Bos taurus, Mus musculus, Rattus norvegicus
brenda
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, Canis lupus familiaris, Mus musculus, Rattus norvegicus
brenda
Bird, M.I.; Munday, L.A.; Saggerson, E.D.; Clark, J.B.
Carnitine acyltransferase activities in rat brain mitochondria. Bimodal distribution, kinetic constants, regulation by malonyl-CoA and developmental pattern
Biochem. J.
226
323-330
1985
Mus musculus, Rattus norvegicus, Rattus norvegicus Wistar
brenda
Healy, M.J.; Kerner, J.; Bieber, L.L.
Enzymes of carnitine acylation. Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase?
Biochem. J.
249
231-237
1988
Bos taurus, Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Lilly, K.; Bugaisky, G.E.; Umeda, P.K.; Bieber, L.L.
The medium-chain carnitine acyltransferase activity associated with rat liver microsomes is malonyl-CoA sensitive
Arch. Biochem. Biophys.
280
167-174
1990
Homo sapiens, Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Nic A'Bhaird, N.; Ramsay, R.R.
Malonyl-CoA inhibition of peroxisomal carnitine octanoyltransferase
Biochem. J.
286
637-640
1992
Rattus norvegicus
brenda
Chung, C.D.; Bieber, L.L.
Properties of the medium chain/long chain carnitine acyltransferase purified from rat liver microsomes
J. Biol. Chem.
268
4519-4524
1993
Rattus norvegicus
brenda
Pagot, Y.; Belin, J.M.
Involvement of carnitine acyltransferases in peroxisomal fatty acid metabolism by the yeast Pichia guilliermondii
Appl. Environ. Microbiol.
62
3864-3867
1996
Meyerozyma guilliermondii, Rattus norvegicus
brenda
Cronin, C.N.
The conserved serine-threonine-serine motif of the carnitine acyltransferases is involved in carnitine binding and transition-state stabilization: a site-directed mutagenesis study
Biochem. Biophys. Res. Commun.
238
784-789
1997
Bos taurus (O19094)
brenda
Cronin, C.N.
cDNA cloning, recombinant expression, and site-directed mutagenesis of bovine liver carnitine octanoyltransferase. Arg505 binds the carboxylate group of carnitine
Eur. J. Biochem.
247
1029-1037
1997
Bos taurus
brenda
Caudevilla, C.; Serra, D.; Miliar, A.; Codony, C.; Asins, G.; Bach, M.; Hegardt, F.G.
Processing of carnitine octanoyltransferase pre-mRNAs by cis and trans-splicing
Adv. Exp. Med. Biol.
466
95-102
1999
Bos taurus, Homo sapiens, Rattus norvegicus
brenda
Ferdinandusse, S.; Mulders, J.; IJlst, L.; Denis, S.; Dacremont, G.; Waterham, H.R.; Wanders, R.J.A.
Molecular cloning and expression of human carnitine octanoyltransferase: Evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids
Biochem. Biophys. Res. Commun.
263
213-218
1999
Bos taurus, Bos taurus (O19094), no activity in Saccharomyces cerevisiae, Rattus norvegicus (P11466), Homo sapiens (Q9UKG9), Homo sapiens
brenda
Ramsay, R.R.; Gandour, R.D.
Selective modulation of carnitine long-chain acyltransferase activities: Kinetics, inhibitors, and active sites of COT and CPT-II
Adv. Exp. Med. Biol.
466
103-109
1999
Bos taurus
brenda
Morillas, M.; Clotet, J.; Rubi, B.; Serra, D.; Arino, J.; Hegardt, F.G.; Asins, G.
Inhibition by etomoxir of rat liver carnitine octanoyltransferase is produced through the co-ordinate interaction with two histidine residues
Biochem. J.
351
495-502
2000
Bos taurus, no activity in Saccharomyces cerevisiae, Rattus norvegicus (P11466)
-
brenda
Hegardt, F.G.; Bach, M.; Asins, G.; Caudevilla, C.; Morillas, M.; Codony, C.; Serra, D.
Post-transcriptional regulation of rat carnitine octanoyltransferase
Biochem. Soc. Trans.
29
316-320
2001
Rattus norvegicus
brenda
Morillas, M.; Gomez-Puertas, P.; Roca, R.; Serra, D.; Asins, G.; Valencia, A.; Hegardt, F.G.
Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT). Mutation of CPT 1 histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity
J. Biol. Chem.
276
45001-45008
2001
Rattus norvegicus
brenda
Morillas, M.; Gomez-Puertas, P.; Rubi, B.; Clotet, J.; Arino, J.; Valencia, A.; Hegardt, F.G.; Serra, D.; Asins, G.
Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I. Mutational analysis of a malonyl-CoA affinity domain
J. Biol. Chem.
277
11473-11480
2002
Rattus norvegicus (P11466)
brenda
Jogl, G.; Hsiao, Y.S.; Tong, L.
Structure and function of carnitine acyltransferases
Ann. N. Y. Acad. Sci.
1033
17-29
2004
Bos taurus
brenda
Morillas, M.; Gomez-Puertas, P.; Bentebibel, A.; Selles, E.; Casals, N.; Valencia, A.; Hegardt, F.G.; Asins, G.; Serra, D.
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition
J. Biol. Chem.
278
9058-9063
2003
Rattus norvegicus
brenda
Cordente, A.G.; Lopez-Vinas, E.; Vazquez, M.I.; Swiegers, J.H.; Pretorius, I.S.; Gomez-Puertas, P.; Hegardt, F.G.; Asins, G.; Serra, D.
Redesign of carnitine acetyltransferase specificity by protein engineering
J. Biol. Chem.
279
33899-33908
2004
Rattus norvegicus
brenda
Jogl, G.; Hsiao, Y.S.; Tong, L.
Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity
J. Biol. Chem.
280
738-744
2005
Mus musculus (Q9DC50), Mus musculus
brenda
Gloerich, J.; van Vlies, N.; Jansen, G.A.; Denis, S.; Ruiter, J.P.; van Werkhoven, M.A.; Duran, M.; Vaz, F.M.; Wanders, R.J.; Ferdinandusse, S.
A phytol-enriched diet induces changes in fatty acid metabolism in mice both via PPARalpha-dependent and -independent pathways
J. Lipid Res.
46
716-726
2005
Mus musculus
brenda
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
brenda
Le Borgne, F.; Ben Mohamed, A.; Logerot, M.; Garnier, E.; Demarquoy, J.
Changes in carnitine octanoyltransferase activity induce alteration in fatty acid metabolism
Biochem. Biophys. Res. Commun.
409
699-704
2011
Homo sapiens (Q9UKG9)
brenda
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