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Information on EC 2.3.1.21 - carnitine O-palmitoyltransferase and Organism(s) Rattus norvegicus and UniProt Accession P18886

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EC Tree
IUBMB Comments
Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine O-acetyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase.
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Rattus norvegicus
UNIPROT: P18886
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cpt1a, carnitine palmitoyltransferase, cpt i, carnitine palmitoyltransferase i, cpt-1, cpt ii, cpt1b, carnitine palmitoyltransferase 1, carnitine palmitoyltransferase-1, cpt1c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carnitine O-palmitoyltransferase
-
carnitine palmitoyltransferase 2
-
acylcarnitine transferase
-
-
-
-
carnitine O-palmitoyltransferase
-
carnitine palmitoyl transferase 1
-
-
carnitine palmitoyl transferase-I
-
-
carnitine palmitoyltransferae 1A
-
-
carnitine palmitoyltransferase
carnitine palmitoyltransferase 1
-
-
carnitine palmitoyltransferase 1A
-
carnitine palmitoyltransferase 2
-
-
carnitine palmitoyltransferase I
carnitine palmitoyltransferase IA
-
-
carnitine palmitoyltransferase II
-
-
-
-
carnitine palmitoyltransferase-1
-
-
carnitine palmitoyltransferase-A
-
-
-
-
carnitine palmitoyltransferase-I
-
CPT I
CPT-A
-
-
-
-
CPT-B
-
-
-
-
CPT-Ialpha
-
liver isoform
CPT1A
CPT1B
CPT1c
L-carnitine palmitoyltransferase
-
-
-
-
palmitoylcarnitine transferase
-
-
-
-
palmitoyltransferase, carnitine
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
Acyl group transfer
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA:L-carnitine O-palmitoyltransferase
Broad specificity to acyl group, over the range C8 to C18; optimal activity with palmitoyl-CoA. cf. EC 2.3.1.7 carnitine O-acetyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-41-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
-
-
?
docosanhexaenoyl-CoA + L-carnitine
CoA + L-docosanhexaenoylcarnitine
show the reaction diagram
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + L-carnitine
CoA + L-oleoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
palmitoyl-CoA + L-carnitine
L-palmitoylcarnitine + CoA
show the reaction diagram
-
forward reaction by CPT I and reverse reaction by CPT II
-
r
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
palmitoyl-CoA + L-carnitine
L-palmitoylcarnitine + CoA
show the reaction diagram
-
forward reaction by CPT I and reverse reaction by CPT II
-
r
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
-
high above micellar concentrations increase conversion of palmitoylcarnitine to palmitoyl-CoA by facilitating the removal of palmitoyl-CoA from the enzyme surface
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
etomoxir
regional differences in brain fatty acid oxidation may be blocked by irreversible CPT1a inhibitor etomoxir
2-bromopalmitoyl-CoA
4-hydroxy phenylglyoxylate
-
CPT I, greatly reduced inhibition of protease treated enzyme
acetyl-CoA
Bile acids
-
e.g. in cholestatic rats
C75-CoA
-
potent competitive inhibition, IC50: 0.0007 mM in liver, IC50: 0.00004 in muscle, IC50: 0.00024 mM recombinant isozyme L-CPT I, IC50: 0.00036 recombinant isozyme M-CPT I, binds tightly but reversibly to CPT I, C75 applied in vivo is transformed to C75-CoA and inhibits fatty acid oxidation, inhibition mechanism, overview, molecular model of docking of C75-CoA to L-CPT I
cardiolipin
-
inhibits conversion of palmitoylcarnitine to palmitoyl-CoA, stimulates palmitoylcarnitine formation
carnitine
-
CPT I, slightly
chenodeoxycholic acid
-
competitive to carnitine
cholate
-
only CPTo
CoA
-
CPT I, inhibition is not affected by proteinase treatment
CoA esters of certain oxirane carboxylic acids
-
irreversible, CPT I but not CPT II
-
Digitonin
-
CPTo and slightly CPTi
dinitrophenyl analogue of etomoxir
-
i.e. 2[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylic acid, DNP-Et, specific inhibitor for liver L-CPT I, identical with the small isoform of heart CPT I, complete inhibition of L-CPT I, but not M-CPT I
etomoxir
regional differences in brain fatty acid oxidation may be blocked by irreversible CPT1a inhibitor etomoxir
etomoxir-CoA
-
CPTo
etomoxiryl-CoA
-
IC50: 0.00025 mM in liver, IC50: 0.000015 in muscle, IC50: 0.0041 mM recombinant isozyme L-CPT I, IC50: 0.0031 recombinant isozyme M-CPT I
gamma-linolenic acid
-
inhibits CPT I in vivo and reduces malonyl-CoA sensitivity, decreases affinity for 16:0 acyl-CoA substrate
Hemipalmitoylcarnitinium bromide
L-aminocarnitine
-
ability to act as substrate or inhibitor of CPT is dependent on the nature of CPT and on the chain length of the acyl-CoA cosubstrate
L-palmitoylcarnitine
-
competitive product inhibition
L-sulfocarnitine
-
ability to act as substrate or inhibitor of CPT is dependent on the nature of CPT and on the chain length of the acyl-CoA cosubstrate
malonyl-CoA
methylmalonyl-CoA
nagarse
-
mitochondria, malonyl-CoA protects
-
octyl glucoside
oxfenicine
-
-
palmitoyl-CoA
palmitoylcarnitine
-
-
Palmitoylcholine
-
competitive in the forward reaction to both substrates
phosphatidylcholine
-
-
propionyl-CoA
-
CPT I, inhibition is not affected by proteinase treatment
Ro 25-0187
S-(4-bromo-2,3-dioxobutyl)-CoA
-
inhibition of malonyl-CoA sensitive enzyme, malonyl-CoA insensitive enzyme is not inhibited
Short chain-length fatty acylcarnitine derivatives
-
-
-
succinyl-CoA
-
partial proteolysis of CPT I slightly diminishes the inhibitory effect
tetradecylglycidyl-CoA
thiolcarnitine
-
ability to act as substrate or inhibitor of CPT is dependent on the nature of CPT and on chain length of the acyl-CoA cosubstrate
Triton X-100
Trypsin
-
mitochondria, malonyl-CoA protects
-
Tween 20
-
only CPTo at 2% and above
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
C-75
-
i.e. 3-carboxy-4-alkyl-2-methylenebutyrolactone, physiologic enzyme stimulation, the stimulation reduces food consumption and weight, regulatory effects, overview
C75
-
a potential drug for the treatment of obesity, a competitive, irreversible inhibitor of fatty acid synthase, and a malonyl-CoA analogue that antagonizes the allosteric inhibitory effect of malonyl-CoA on CPT I
carbacyclin
-
carbacyclin induces CPT-1 mRNA expression through peroxisome proliferator-activated receptor, PPAR
cardiolipin
-
inhibits conversion of palmitoylcarnitine to palmitoyl-CoA, stimulates palmitoylcarnitine formation
cholate
-
activates only CPTi
di(2-ethyl-hexyl)phtalate
-
-
liothyronine
-
-
octyl glucoside
-
only CPTi
palmitoylcarnitine
-
high above micellar concentrations increase conversion of palmitoylcarnitine to palmitoyl-CoA by facilitating the removal of palmitoyl-CoA from the enzyme surface
PGC-1beta
-
peroxisome proliferator activated receptor gamma coactivator
-
Phosphatidylcholine liposomes
-
Phospholipids
-
e.g. phosphatidylcholine, cardiolipin, stimulate
Proteins
-
e.g. albumin, fatty acid-binding protein, lambda-globulin, stimulate
-
salicylic acid
-
activates best at 20 mM, pH changes
Triton X-100
-
only CPTi
Tween 20
-
activates only CPTi
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 127
L-carnitine
0.0017 - 25.35
palmitoyl-CoA
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
chenodeoxycholic acid
-
-
0.0016 - 0.0215
Hemipalmitoylcarnitinium bromide
0.009 - 0.014
palmitoylcarnitine
0.0104 - 0.019
Palmitoylcholine
additional information
additional information
-
tissue-specific inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00004 - 0.0007
C75-CoA
0.000015 - 0.0041
etomoxiryl-CoA
0.00339 - 0.319
malonyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0006
hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.0008
hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.001
hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.0017
hepatocytes transduced with adenovirus encoding CPT-1a exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.0019
hepatocytes transduced with adenovirus encoding CPT-1a exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.0021
hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding beta-galctosidase, incubation with palmitate
0.0029
0.0033
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-2, incubation with palmitate
0.0041
hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate
0.0051
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate
0.0063
hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.00035
-
transfected HEK-293T cell
0.0006
hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.0008
hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.001
0.0013
0.0014
-
CPT I after gamma-linoleic acid treatment
0.0017
hepatocytes transduced with adenovirus encoding CPT-1a exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.0019
hepatocytes transduced with adenovirus encoding CPT-1a exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.00194
-
transfectecd PC-12 cell
0.0021
0.0029
0.0032
0.0033
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-2, incubation with palmitate
0.0036
0.0041
hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate
0.0051
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate
0.0063
hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.0069
-
mitochondrial fraction of recombinant Pichia pastoris expressing CPT II
0.0078
-
recombinant wild-type L-CPT I
0.009
-
CPT I
0.43
-
recombinant CPT II from Sf 9 insect cells
0.473
-
purified recombinant L-CPT I, reconstituted in liposomes
24
-
purified enzyme
29.6
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
assay at
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 8.8
-
L-CPT I
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoforms CPT1a and CPT2 are expressed exclusively by astrocytes
Manually annotated by BRENDA team
brain isoform CPT2 RNA peaks at post-natal day 21 and remains unchanged through post-natal day 50 in all regions studied. CPT2 transcript abundance is highly developmentally regulated in the cortex, midbrain, and cerebellum, and significantly increases with age. The peak of acylcarnitine abundance in all brain regions profiled at post-natal day 21 corresponds to the maximal expression of CPT2 mRNA
Manually annotated by BRENDA team
no age differences are detected in CPT2 mRNA expression in hippocampus
Manually annotated by BRENDA team
isoforms CPT1a and CPT2 are expressed exclusively by astrocytes
Manually annotated by BRENDA team
expression of isoforms CPT1a and CPT2 increases during brain development and is enriched in hippocampus relative to the cortex, midbrain, and cerebellum
Manually annotated by BRENDA team
-
small and large, L-CPT I and CPT II
Manually annotated by BRENDA team
-
muscle cell line
Manually annotated by BRENDA team
-
low content L-CPT I and CPT II
Manually annotated by BRENDA team
-
low content of M-CPT I, and higher content of CPT II ad L-CPT I
Manually annotated by BRENDA team
-
low content of CPT II, no CPT I
Manually annotated by BRENDA team
-
L-CPT I and high content of CPT II and M-CPT I
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CPT2_RAT
658
0
74110
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
CPT I and II, gel filtration
280000 - 320000
-
gel filtration
30000
-
x * 30000, SDS-PAGE
430000
-
CPTo and CPTi, gel filtration
66000
-
gel filtration
68000
-
x * 68000, liver, CTP II
69200
-
x * 69200, SDS-PAGE
70000
-
x * 70000, recombinant CPT II, SDS-PAGE
75000
-
determined by SDS-PAGE and Western Blot analysis
82000
-
x * 82000, M-CPT I, SDS-PAGE
86000
88000
-
x * 88000, recombinant CPT I, SDS-PAGE
90200
-
x * 90200, estimated from SDS-PAGE
94000
-
1 * 94000, liver, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
-
on N-terminal Ala2
phosphoprotein
phosphoralytion of hepatic CPT-I is a mechanism for control of fatty acid oxidation. Phosphorylation of the CKII site in the C-terminal end of CPT-I leads to decreased malonyl-CoA sensitivity and increased catalytic activity
additional information
-
it is suggested that the enzyme contains hydrophobic sites which require phospholipid to prevent spurious binding of palmitoyl-CoA and which normally anchor the enzyme to the mitochondrial membrane
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A381D
-
site-directed mutagenesis, activity is reduced by 86%, Km for acyl-CoA is 6-8fold increased
A478G
3.2fold increase in IC50 for malonyl-CoA, 2.6fold increase in KM-value for carnitine, 3.1fold increase in Km-value for palmitoyl-CoA as compared to wild-type enzyme
A587S/S588A/M592L/R594L
-
inert isoform CPT1c
C608A
2.2fold increase in IC50 for malonyl-CoA, 2.5fold increase in KM-value for carnitine, 5fold increase in Km-value for palmitoyl-CoA as compared to wild-type enzyme
D454G
-
site-directed mutagenesis, loss of activity
E590A
IC50 for malonyl CoA is 16fold lower than the wild-type value, partial decrease in catalytic activity,1.5fold increase in Km-value for carnitine, 2.9fold decrease in KM-value doe palmitoyl-CoA
E590D
inactive mutant enzyme
E590K
IC50 for malonyl CoA is 13.5fold lower than the wild-type value, partial decrease in catalytic activity
E590Q
IC50 for malonyl CoA is 8.7fold lower than the wild-type value, partial decrease in catalytic activity, 1.3fold increase in Km-value for carnitine, 2fold decrease in KM-value doe palmitoyl-CoA
H473A
-
site-directed mutagenesis, active site mutant, no remaining activity
L484P
-
site-directed mutagenesis, loss of activity
M593A
12.6fold increase in IC50 for malonyl-CoA, 2.3fold increase in KM-value for carnitine, 1.2fold increase in Km-value for palmitoyl-CoA as compared to wild-type enzyme
M593E
18fold increase in IC50 for malonyl-CoA, 1.2fold increase in KM-value for carnitine, 1.3fold decrease in Km-value for palmitoyl-CoA as compared to wild-type enzyme
M593S
N464D
1.4fold decrease in IC50 for malonyl-CoA, 1.8fold increase in KM-value for carnitine, 1.2fold decrease in Km-value for palmitoyl-CoA as compared to wild-type enzyme
P479L
-
site-directed mutagenesis, loss of activity
R451A
-
site-directed mutagenesis, loss of activity
T314S
1.2fold increase in IC50 for malonyl-CoA, 1.4fold increase in KM-value for carnitine, 2.9fold decrease in Km-value for palmitoyl-CoA as compared to wild-type enzyme
W391A
W452A
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
stable for 24 h at 4°C, recombinant CPT II
486574
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
fractionation causes rapid loss of CPTo activity, CPTi is relatively stable
-
no loss in activity after 6 freeze/thaw cycles at -70°C or room temeprature, recombinant CPT II
-
quite stable at all steps of purification
-
solubilization causes rapid loss of CPTo activity, CPTi is relatively stable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months
-
4°C, pH 7.0-10.0, 24 h stable, recombinant CPT II
-
room temperature, 6.5 h, no loss in activity, recombinant CPT II
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CPT II, partial
-
CPTo and CPTi, partial
-
liver mitochondria
-
microsomes are prepared
-
native CPT II from liver
-
native enzyme partially by microsome preparation, recombinant isozymes M-CPT I and L-CPT I from Saccharomyces cerevisiae
-
partial, recombinant CPT I and II from Pichia pastoris
-
recombinant CPT II from Sf 9 insect cells
-
recombinant His-tagged L-CPT I from Pichia pastoris
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant adenoviruses containing cDNAs encoding rat CPT1a and rat CPT2 are constructed
a rat promoter CPT-Ialpha luciferase vector is constructed
-
adenovirus-mediated (over)expression in cultured fed rat hepatocyte
-
clonig of CPT I and II from liver, expression in Pichia pastoris
-
cloning and expression of CPT II in Escherichia coli, overexpression of CPT II in Spodoptera frugiperda Sf 9 cells via baculavirus infection, DNA sequence analysis
-
cloning of liver mitochondrial CPT II from genetic library, in vitro transcription and translation, DNA sequence analysis, expression in COS cells
-
construction of 6 chimeric proteins with exchanges structure segments of L-CPT I and M-CPT I, expression of chimeric mutants and wild-type isoforms in Pichia pastoris
-
construction of chimeric L-CPT I with deletions and exchanged C-terminal sequences between rat and pig enzymes, expression in Pichia pastoris
-
COS-1 cells are transiently transfected to express a fusion protein in which enhanced green fluorescent protein is fused to the C-terminus of L-CPT1. This fusion protein is localized to mitochondria, and possibly to peroxisomes, but not to the endoplasmic reticulum
-
CPT1c cDNA is amplified and cloned into the pBlueScript vector, sequenced and subsequently cloned into pEGFP-N3, the coding regions of CPT1a and CPT1c are cloned into vector pIRES2-EGFP, chimeras between CPT1c and CPT1a are constructed
-
expressed in Escherichia coli and COS-7 cells
-
expression in Escherichia coli
expression of carnitine palmitoyltransferase I wild-type and mutant enzymes in Saccharomyces cerevisiae
expression of CPT I in Saccharomyces cerevisiae
-
expression of His-tagged L-CPT I in Pichia pastoris
-
expression of L-CPT I in Saccharomyces cerevisiae, recombinant and native enzyme show the same biochemical properties
-
overexpression of isozymes M-CPT I and L-CPT I in Saccharomyces cerevisiae
-
recombinant adenoviruses containing cDNAs encoding rat CPT1a and rat CPT2 are constructed
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of detergent-inactivated recombinant M-CPT I, purified from Pichia pastoris, by removal of detergents in presence of phospholipids
-
reconstitution of recombinant L-CPT I from Pichia pastoris in phospholipids after purification with detergent extraction
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
the data represent proof in principle that a pharmacological agent that stimulates hepatic fatty acid oxidation, perhaps acting on carnitine palmitoyltransferase 1a, could provide a novel approach to treatment of nonalcoholic fatty liver disease
medicine
pharmacology
synthesis
comparison of COS7 cell and yeast expression of isoform CPT1b. The mitochondrial fraction prepared from yeast cells expressing CPT1b shows 25% higher CPT1 activity than that obtained from COS7 cells. The expression level of CPT1b in the former is 3.8 times lower than that in the latter; and thus the specific activity of CPT1b expressed in yeast cells is estimated to be approximately five times higher than that expressed in COS7 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Sekas, G.; Paul, H.S.
Inhibition of carnitine acyltransferase activities by bile acids in rat liver peroxisomes
Biochim. Biophys. Acta
1125
396-402
1992
Rattus norvegicus
-
Manually annotated by BRENDA team
Miyazawa, S.; Ozaka, H.; Osumi, T.; Hashiomoto, T.
Purification and properties of carnitine octanoyltransferase and carnitine palmitoyltransferase from rat liver
J. Biochem.
94
529-542
1983
Rattus norvegicus
Manually annotated by BRENDA team
Murthy, M.S.R.; Pande, S.V.
Some differences in the properties of carnitine palmitoyltransferase activities of the mitochondrial outer and inner membranes
Biochem. J.
248
727-733
1987
Rattus norvegicus
Manually annotated by BRENDA team
Murthy, M.S.R.; Pande, S.V.
Characterization of a solubilized malonyl-CoA-sensitive carnitine palmitoyltransferase from the mitochondrial outer membrane as a protein distinct from the malonyl-CoA-insensitive carnitine palmitoyltransferase of the inner membrane
Biochem. J.
268
599-604
1990
Rattus norvegicus
Manually annotated by BRENDA team
Halperin, M.L.; Pande, S.V.
Fatty acyl group transport into mitochondria: carnitine palmitoyl transferases EC 2.3.1.23 and the carnitine-acylcarnitine translocase
Methods Enzymol.
56
368-378
1979
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Kolodziej, M.P.; Zammit, V.A.
Sensitivity of inhibition of rat liver mitochondrial outer-membrane carnitine palmitoyltransferase by malonyl-CoA to chemical- and temperature-induced changes in membrane fluidity
Biochem. J.
272
421-425
1990
Rattus norvegicus
Manually annotated by BRENDA team
Woeltje, K.F.; Esser, V.; Weis, B.C.; Sen, A.; Cox, W.F.; McPaul, M.J.; Slaughter, C.A.; Foster, D.W.; McGarry, J.D.
Cloning, sequencing, and expression of a cDNA encoding rat liver mitochondrial carnitine palmitoyltransferase II
J. Biol. Chem.
265
10720-10725
1990
Rattus norvegicus
Manually annotated by BRENDA team
Chung, C.H.; Woldegiorgis, G.; Dai, G.; Shrago, E.; Bieber, L.L.
Conferral of malonyl coenzyme A sensitivity to purified rat heart mitochondrial carnitine palmitoyltransferase
Biochemistry
31
9777-9783
1992
Rattus norvegicus
Manually annotated by BRENDA team
Ghadiminejad, I.; Saggerson, E.D.
Carnitine palmitoyltransferase (CPT2) from liver mitochondrial inner membrane becomes inhibitable by malonyl-CoA if reconstituted with outer membrane malonyl-CoA binding protein
FEBS Lett.
269
406-408
1990
Rattus norvegicus
Manually annotated by BRENDA team
Gavino, G.R.; Gavino, V.C.
Rat liver outer mitochondrial carnitine palmitoyltransferase activity towards long-chain polyunsaturated fatty acids and their CoA esters
Lipids
26
266-270
1991
Rattus norvegicus
Manually annotated by BRENDA team
Woldegiorgis, G.; Fibich, B.; Contreras, L.; Shrago, E.
Restoration of malonyl-CoA sensitivity of soluble rat liver mitochondria carnitine palmitoyltransferase by reconstitution with a partially purified malonyl-CoA binding protein
Arch. Biochem. Biophys.
295
348-351
1992
Rattus norvegicus
Manually annotated by BRENDA team
Ghadiminejad, I.; Saggerson, D.
A simple method for the purification of carnitine palmitoyl transferase 2 from rat liver
Biochem. Soc. Trans.
17
348-349
1989
Rattus norvegicus
-
Manually annotated by BRENDA team
Murthy, M.S.R.; Ramsay, R.R.; Pande, S.V.
Carnitine analogues and carnitine palmitoyltransferases
Biochem. Soc. Trans.
18
604-605
1990
Rattus norvegicus
Manually annotated by BRENDA team
Gandour, R.D.; Colucci, W.J.; Stelly, T.C.; Brady, P.S.; Brady, L.J.
Hemipalmitoylcarnitinium, a strong competitive inhibitor of purified hepatic carnitine palmitoyltransferase
Arch. Biochem. Biophys.
267
515-520
1988
Rattus norvegicus
Manually annotated by BRENDA team
Kashfi, K.; Cook, G.A.
Malonyl-CoA inhibits proteolysis of carnitine palmitoyltransferase
Biochem. Biophys. Res. Commun.
178
600-605
1991
Rattus norvegicus
Manually annotated by BRENDA team
Brindle, N.P.J.; Zammit, V.A.; Pogson, C.I.
Regulation of carnitine palmitoyltransferase activity by malonyl-CoA in mitochondria from sheep liver, a tissue with a low capacity for fatty acid synthesis
Biochem. J.
232
177-182
1985
Cavia porcellus, Ovis aries, Rattus norvegicus
Manually annotated by BRENDA team
Brady, P.S.; Dunker, A.K.; Brady, L.J.
Characterization of hepatic carnitine palmitoyltransferase. Use of bromoacyl derivatives and antibodies
Biochem. J.
241
751-757
1987
Rattus norvegicus
Manually annotated by BRENDA team
Bartlett, K.; Sherratt, H.S.A.; Turnbull, D.M.
Inhibition of hepatic and skeletal muscle carnitine palmitoyltransferase I by 2[5(4-chlorophenyl)pentyl]-oxirane-2-carbonyl-CoA
Biochem. Soc. Trans.
12
688-689
1984
Rattus norvegicus
-
Manually annotated by BRENDA team
Cook, G.A.
Differences in the sensitivity of carnitine palmitoyltransferase to inhibition by malonyl-CoA are due to differences in Ki values
J. Biol. Chem.
259
12030-12033
1984
Rattus norvegicus
Manually annotated by BRENDA team
Brosnan, J.T.; Kopec, B.; Fritz, I.B.
The localization of carnitine palmitoyltransferase on the inner membrane of bovine liver mitochondria
J. Biol. Chem.
248
4075-4082
1973
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Paulson, D.J.; Ward, K.M.; Shug, A.L.
Malonyl CoA inhibition of carnitine palmityltransferase in rat heart mitochondria
FEBS Lett.
176
381-384
1984
Rattus norvegicus
Manually annotated by BRENDA team
Pande, S.V.; Murthy, M.S.R.; Noel, H.
Differential effects of phosphatidylcholine and cardiolipin on carnitine palmitoyltransferase activity
Biochim. Biophys. Acta
877
223-230
1986
Rattus norvegicus
Manually annotated by BRENDA team
Saggerson, E.D.; Carpenter, C.A.
Sensitivity of brown-adipose-tissue carnitine palmitoyltransferase to inhibition by malonyl-CoA
Biochem. J.
204
373-375
1982
Rattus norvegicus
Manually annotated by BRENDA team
Stephens, T.W.; Cook, G.A.; Harris, R.A.
Effect of pH on malonyl-CoA inhibition of carnitine palmitoyltransferase I
Biochem. J.
212
521-524
1983
Rattus norvegicus
Manually annotated by BRENDA team
McCormick, K.; Notar-Francesco, V.J.
Importance of albumin binding in the assay for carnitine palmitoyltransferase
Biochem. J.
216
495-498
1983
Rattus norvegicus
Manually annotated by BRENDA team
McCormick, K.; Notar-Francesco, V.J.; Sriwatanakul, K.
Inhibition by acetyl-CoA of hepatic carnitine acyltransferase and fatty acid oxidation
Biochem. J.
216
499-502
1983
Rattus norvegicus
Manually annotated by BRENDA team
Bergstrom, J.D.; Reitz, R.C.
Studies on carnitine palmitoyl transferase: the similar nature of CPTi (inner form) and CPTo (outer form)
Arch. Biochem. Biophys.
204
71-79
1980
Rattus norvegicus
Manually annotated by BRENDA team
Declercq, P.E.; Falck, J.R.; Kuwajima, M.; Tyminski, H.; Foster, D.W.; McGarry, J.D.
Characterization of the mitochondrial carnitine palmitoyltransferase enzyme system. I. Use of inhibitors
J. Biol. Chem.
262
9812-9821
1987
Rattus norvegicus
Manually annotated by BRENDA team
Woeltje, K.F.; Esser, V.; Weis, B.C.; Cox, W.F.; Schroeder, J.G.; Liao, S.L.; Foster, D.W.; McGarry, J.D.
Inter-tissue and inter-species characteristics of the mitochondrial carnitine palmitoyltransferase enzyme system
J. Biol. Chem.
265
10714-10719
1990
Homo sapiens, Platyrrhini, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Lund, H.
Carnitine palmitoyltransferase: characterization of a labile detergent-extracted malonyl-CoA-sensitive enzyme from rat liver mitochondria
Biochim. Biophys. Acta
918
67-75
1987
Rattus norvegicus
Manually annotated by BRENDA team
Kopec, B.; Fritz, I.B.
Comparison of properties of carnitine palmitoyltransferase I with those of carnitine palmitoyltransferase II, and preparation of antibodies to carnitine palmitoyltransferases
J. Biol. Chem.
248
4069-4074
1973
Rattus norvegicus
Manually annotated by BRENDA team
Woldegiorgis, G.; Bremer, J.; Shrago, E.
Substrate inhibition of carnitine palmitoyltransferase by palmitoyl-CoA and activation by phospholipids and proteins
Biochim. Biophys. Acta
837
135-140
1985
Rattus norvegicus
Manually annotated by BRENDA team
Weis, B.C.; Cowan, A.T.; Brown, N.; Foster, D.W.; McGarry, J.D.
Use of a selective inhibitor of liver carnitine palmitoyltransferase I (CPT I) allows quantification of its contribution to total CPT I activity in rat heart. Evidence that the dominant cardiac CPT I isoform is identical to the skeletal muscle enzyme
J. Biol. Chem.
269
26443-26448
1994
Rattus norvegicus
Manually annotated by BRENDA team
Kashfi, K.; Mynatt, R.L.; Cook, G.A.
Hepatic carnitine palmitoyltransferase-I has two independent inhibitory binding sites for regulation of fatty acid oxidation
Biochim. Biophys. Acta
1212
245-252
1994
Rattus norvegicus
Manually annotated by BRENDA team
Singh, H.; Poulos, A.
Substrate specificity of rat liver mitochondrial carnitine palmitoyl transferase I: evidence against alpha-oxidation of phytanic acid in rat liver mitochondria
FEBS Lett.
359
179-183
1995
Rattus norvegicus
Manually annotated by BRENDA team
Johnson, T.M.; Mann, W.R.; Dragland, C.J.; Anderson, R.C.; Nemecek, G.M.; Bell, P.A.
Over-expression and characterization of active recombinant rat liver carnitine palmitoyltransferase II using baculovirus
Biochem. J.
309
689-693
1995
Rattus norvegicus
-
Manually annotated by BRENDA team
De Vries, Y.; Arvidson, D.N.; Waterham, H.R.; Cregg, J.M.; Woldegiorgis, G.
Functional characterization of mitochondrial carnitine palmitoyltransferases I and II expressed in the yeast Pichia pastoris
Biochemistry
36
5285-5292
1997
no activity in Pichia pastoris, Rattus norvegicus
Manually annotated by BRENDA team
Brown, N.F.; Hill, J.K.; Esser, V.; Kirkland, J.L.; Corkey, B.E.; Foster, D.W.; McGarry, J.D.
Mouse white adipocytes and 3T3-L1 cells display an anomalous pattern of carnitine palmitoyltransferase (CPT) I isoform expression during differentiation. Inter-tissue and inter-species expression of CPT I and CPT II enzymes
Biochem. J.
327
225-231
1997
Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
-
Manually annotated by BRENDA team
Prip-Buus, C.; Cohen, I.; Kohl, C.; Esser, V.; McGarry, J.D.; Girard, J.
Topological and functional analysis of the rat liver carnitine palmitoyltransferase 1 expressed in Saccharomyces cerevisiae
FEBS Lett.
429
173-178
1998
Rattus norvegicus
Manually annotated by BRENDA team
Jackson, V.N.; Cameron, J.M.; Fraser, F.; Zammit, V.A.; Price, N.T.
Use of six chimeric proteins to investigate the role of intramolecular interactions in determining the kinetics of carnitine palmitoyltransferase I isoforms
J. Biol. Chem.
275
19560-19566
2000
Rattus norvegicus
Manually annotated by BRENDA team
Eaton, S.; Fukumoto, K.; Paladio Duran, N.; Pierro, A.; Spitz, L.; Quant, P.A.; Bartlett, K.
Carnitine palmitoyl transferase I and the control of myocardial beta-oxidation flux
Biochem. Soc. Trans.
29
245-250
2001
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Abo-Hashema, K.A.H.; Cake, M.H.; Lukas, M.A.; Knudsen, J.
The interaction of acyl-CoA with acyl-CoA binding protein and carnitine palmitoyltransferase I
Int. J. Biochem. Cell Biol.
33
807-815
2001
Rattus norvegicus
Manually annotated by BRENDA team
Colquhoun, A.
Gamma-linolenic acid alters the composition of mitochondrial membrane subfractions, decreases outer mitochondrial membrane binding of hexokinase and alters carnitine palmitoyltransferase I properties in the Walker 256 rat tumour
Biochim. Biophys. Acta
1583
74-84
2002
Rattus norvegicus
Manually annotated by BRENDA team
Nicot, C.; Relat, J.; Woldegiorgis, G.; Haro, D.; Marrero, P.F.
Pig liver carnitine palmitoyltransferase: chimera studies show that both the N- and C-terminal regions of the enzyme are important for the unusual high malonyl-CoA sensitivity
J. Biol. Chem.
277
10044-10049
2002
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
McGarry, J.D.; Brown, N.F.
Reconstitution of purified, active and malonyl-CoA-sensitive rat liver carnitine palmitoyltransferase I: relationship between membrane environment and malonyl-CoA sensitivity
Biochem. J.
349
179-187
2000
Rattus norvegicus
Manually annotated by BRENDA team
Broadway, N.M.; Pease, R.J.; Birdsey, G.; Shayeghi, M.; Turner, N.A.; David Saggerson, E.
The liver isoform of carnitine palmitoyltransferase 1 is not targeted to the endoplasmic reticulum
Biochem. J.
370
223-231
2003
Rattus norvegicus
Manually annotated by BRENDA team
Napal, L.; Dai, J.; Treber, M.; Haro, D.; Marrero, P.F.; Woldegiorgis, G.
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme
J. Biol. Chem.
278
34084-34089
2003
Rattus norvegicus (P32198)
Manually annotated by BRENDA team
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 (P32198)
Manually annotated by BRENDA team
Kerner, J.; Distler, A.M.; Minkler, P.; Parland, W.; Peterman, S.M.; Hoppel, C.L.
Phosphorylation of rat liver mitochondrial carnitine palmitoyltransferase-I: effect on the kinetic properties of the enzyme
J. Biol. Chem.
279
41104-41113
2004
Rattus norvegicus (P32198)
Manually annotated by BRENDA team
Bentebibel, A.; Sebastian, D.; Herrero, L.; Lopez-Vinas, E.; Serra, D.; Asins, G.; Gomez-Puertas, P.; Hegardt, F.G.
Novel effect of C75 on carnitine palmitoyltransferase I activity and palmitate oxidation
Biochemistry
45
4339-4350
2006
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kuhajda, F.P.; Ronnett, G.V.
Modulation of carnitine palmitoyltransferase-1 for the treatment of obesity
Curr. Opin. Investig. Drugs
8
312-317
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Doh, K.O.; Kim, Y.W.; Park, S.Y.; Lee, S.K.; Park, J.S.; Kim, J.Y.
Interrelation between long-chain fatty acid oxidation rate and carnitine palmitoyltransferase 1 activity with different isoforms in rat tissues
Life Sci.
77
435-443
2005
Rattus norvegicus
Manually annotated by BRENDA team
Stefanovic-Racic, M.; Perdomo, G.; Mantell, B.S.; Sipula, I.J.; Brown, N.F.; ODoherty, R.M.
A moderate increase in carnitine palmitoyltransferase 1a activity is sufficient to substantially reduce hepatic triglyceride levels
Am. J. Physiol. Endocrinol. Metab.
294
E969-E977
2008
Rattus norvegicus (P18886), Rattus norvegicus (P32198)
Manually annotated by BRENDA team
Sorokina, N.; ODonnell, J.M.; McKinney, R.D.; Pound, K.M.; Woldegiorgis, G.; LaNoue, K.F.; Ballal, K.; Taegtmeyer, H.; Buttrick, P.M.; Lewandowski, E.D.
Recruitment of compensatory pathways to sustain oxidative flux with reduced carnitine palmitoyltransferase I activity characterizes inefficiency in energy metabolism in hypertrophied hearts
Circulation
115
2033-2041
2007
Rattus norvegicus
Manually annotated by BRENDA team
Okere, I.C.; Chandler, M.P.; McElfresh, T.A.; Rennison, J.H.; Kung, T.A.; Hoit, B.D.; Ernsberger, P.; Young, M.E.; Stanley, W.C.
Carnitine palmitoyl transferase-I inhibition is not associated with cardiac hypertrophy in rats fed a high-fat diet
Clin. Exp. Pharmacol. Physiol.
34
113-119
2007
Rattus norvegicus
Manually annotated by BRENDA team
Sierra, A.Y.; Gratacos, E.; Carrasco, P.; Clotet, J.; Urena, J.; Serra, D.; Asins, G.; Hegardt, F.G.; Casals, N.
CPT1c is localized in endoplasmic reticulum of neurons and has carnitine palmitoyltransferase activity
J. Biol. Chem.
283
6878-6885
2008
Rattus norvegicus
Manually annotated by BRENDA team
Kuroda, T.; Hirota, H.; Fujio, Y.; Sugiyama, S.; Masaki, M.; Hiramoto, Y.; Shioyama, W.; Okamoto, K.; Hori, M.; Yamauchi-Takihara, K.
Carbacyclin induces carnitine palmitoyltransferase-1 in cardiomyocytes via peroxisome proliferator-activated receptor (PPAR) delta independent of the IP receptor signaling pathway
J. Mol. Cell. Cardiol.
43
54-62
2007
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Sadana, P.; Zhang, Y.; Song, S.; Cook, G.A.; Elam, M.B.; Park, E.A.
Regulation of carnitine palmitoyltransferase I (CPT-Ialpha) gene expression by the peroxisome proliferator activated receptor gamma coactivator (PGC-1) isoforms
Mol. Cell. Endocrinol.
267
6-16
2007
Rattus norvegicus
Manually annotated by BRENDA team
Akkaoui, M.; Cohen, I.; Esnous, C.; Lenoir, V.; Sournac, M.; Girard, J.; Prip-Buus, C.
Modulation of the hepatic malonyl-CoA-carnitine palmitoyltransferase 1A partnership creates a metabolic switch allowing oxidation of de novo fatty acids
Biochem. J.
420
429-438
2009
Rattus norvegicus
Manually annotated by BRENDA team
Rufer, A.C.; Thoma, R.; Hennig, M.
Structural insight into function and regulation of carnitine palmitoyltransferase
Cell. Mol. Life Sci.
66
2489-2501
2009
Rattus norvegicus
Manually annotated by BRENDA team
Roomets, E.; Kivelae, T.; Tyni, T.
Carnitine palmitoyltransferase I and Acyl-CoA dehydrogenase 9 in retina: insights of retinopathy in mitochondrial trifunctional protein defects
Invest. Ophthalmol. Vis. Sci.
49
1660-1664
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Zammit, V.
Carnitine palmitoyltransferase 1: central to cell function
IUBMB Life
60
347-354
2008
Rattus norvegicus
Manually annotated by BRENDA team
Bi, Y.; Cai, M.; Liang, H.; Sun, W.; Li, X.; Wang, C.; Zhu, Y.; Chen, X.; Li, M.; Weng, J.
Increased carnitine palmitoyl transferase 1 expression and decreased sterol regulatory element-binding protein 1c expression are associated with reduced intramuscular triglyceride accumulation after insulin therapy in high-fat-diet and streptozotocin-indu
Metab. Clin. Exp.
58
779-786
2009
Rattus norvegicus
Manually annotated by BRENDA team
Sharma, V.; Abraham, T.; So, A.; Allard, M.; McNeill, J.
Functional effects of protein kinases and peroxynitrite on cardiac carnitine palmitoyltransferase-1 in isolated mitochondria
Mol. Cell. Biochem.
337
223-237
2010
Rattus norvegicus
Manually annotated by BRENDA team
Lee, K.; Kerner, J.; Hoppel, C.L.
Mitochondrial carnitine palmitoyltransferase 1a (CPT1a) is part of an outer membrane fatty acid transfer complex
J. Biol. Chem.
286
25655-25662
2011
Rattus norvegicus (P32198)
Manually annotated by BRENDA team
Hostetler, H.A.; Lupas, D.; Tan, Y.; Dai, J.; Kelzer, M.S.; Martin, G.G.; Woldegiorgis, G.; Kier, A.B.; Schroeder, F.
Acyl-CoA binding proteins interact with the acyl-CoA binding domain of mitochondrial carnitine palmitoyl transferase I
Mol. Cell. Biochem.
355
135-148
2011
Rattus norvegicus (P32198)
Manually annotated by BRENDA team
Hada, T.; Kato, Y.; Obana, E.; Yamamoto, A.; Yamazaki, N.; Hashimoto, M.; Yamamoto, T.; Shinohara, Y.
Comparison of two expression systems using COS7 cells and yeast cells for expression of heart/muscle-type carnitine palmitoyltransferase 1
Protein Expr. Purif.
82
192-196
2012
Rattus norvegicus (Q63704)
Manually annotated by BRENDA team
Hada, T.; Yamamoto, T.; Yamamoto, A.; Ohkura, K.; Yamazaki, N.; Takiguchi, Y.; Shinohara, Y.
Comparison of the catalytic activities of three isozymes of carnitine palmitoyltransferase 1 expressed in COS7 cells
Appl. Biochem. Biotechnol.
172
1486-1496
2014
Rattus norvegicus
Manually annotated by BRENDA team
Console, L.; Giangregorio, N.; Indiveri, C.; Tonazzi, A.
Carnitine/acylcarnitine translocase and carnitine palmitoyltransferase 2 form a complex in the inner mitochondrial membrane
Mol. Cell. Biochem.
394
307-314
2014
Rattus norvegicus
Manually annotated by BRENDA team
Jernberg, J.N.; Bowman, C.E.; Wolfgang, M.J.; Scafidi, S.
Developmental regulation and localization of carnitine palmitoyltransferases (CPTs) in rat brain
J. Neurochem.
142
407-419
2017
Rattus norvegicus (P18886), Rattus norvegicus (P32198)
Manually annotated by BRENDA team