2.3.1.21: carnitine O-palmitoyltransferase
This is an abbreviated version!
For detailed information about carnitine O-palmitoyltransferase, go to the full flat file.
Word Map on EC 2.3.1.21
-
2.3.1.21
-
peroxisome
-
triglyceride
-
proliferator-activated
-
acyl-coas
-
malonyl-coa
-
obesity
-
carboxylase
-
adipose
-
high-fat
-
acetyl-coa
-
beta-oxidation
-
cholesterol
-
hepatocytes
-
cardiac
-
palmitate
-
sterol
-
lipogenesis
-
lipoprotein
-
steatosis
-
lipase
-
amp-activated
-
adipocytes
-
obese
-
acyltransferase
-
triacylglycerols
-
diet-induced
-
element-binding
-
etomoxir
-
leptin
-
lipogenic
-
lipolysis
-
adiponectin
-
pparalpha
-
srebp-1c
-
medium-chain
-
nafld
-
nonalcoholic
-
ketogenesis
-
stearoyl-coa
-
protein-1c
-
hfd-induced
-
rhabdomyolysis
-
palmitate-induced
-
srebf1
-
anti-obesity
-
muscle-type
-
myoglobinuria
-
lcfas
-
synthesis
-
medicine
-
vlcad
-
acaca
-
pharmacology
- 2.3.1.21
- peroxisome
- triglyceride
-
proliferator-activated
- acyl-coas
- malonyl-coa
- obesity
- carboxylase
- adipose
-
high-fat
- acetyl-coa
-
beta-oxidation
- cholesterol
- hepatocytes
- cardiac
- palmitate
- sterol
-
lipogenesis
- lipoprotein
- steatosis
- lipase
-
amp-activated
- adipocytes
-
obese
- acyltransferase
- triacylglycerols
-
diet-induced
-
element-binding
- etomoxir
- leptin
-
lipogenic
-
lipolysis
- adiponectin
- pparalpha
- srebp-1c
-
medium-chain
- nafld
-
nonalcoholic
-
ketogenesis
- stearoyl-coa
- protein-1c
-
hfd-induced
- rhabdomyolysis
-
palmitate-induced
-
srebf1
-
anti-obesity
-
muscle-type
- myoglobinuria
-
lcfas
- synthesis
- medicine
- vlcad
- acaca
- pharmacology
Reaction
Synonyms
acylcarnitine transferase, carnitine O-palmitoyltransferase, carnitine O-palmitoyltransferase I, carnitine palmitoyl transferase 1, carnitine palmitoyl transferase 1A, carnitine palmitoyl transferase-1A, carnitine palmitoyl transferase-I, carnitine palmitoyl-transferase-1c, carnitine palmitoyltransferae 1A, carnitine palmitoyltransferase, carnitine palmitoyltransferase 1, carnitine palmitoyltransferase 1A, carnitine palmitoyltransferase 1B, carnitine palmitoyltransferase 2, carnitine palmitoyltransferase I, carnitine palmitoyltransferase IA, carnitine palmitoyltransferase II, carnitine palmitoyltransferase-1, carnitine palmitoyltransferase-1c, carnitine palmitoyltransferase-A, carnitine palmitoyltransferase-I, carnitine palmitoyltransferases 2, CPT, CPT I, CPT IA, CPT Ialpha1a, CPT Ialpha1b, CPT Ialpha2a, CPT Ibeta, CPT II, CPT-1, CPT-2, CPT-A, CPT-B, CPT-Ialpha, CPT-IL, CPT1, CPT1-A, CPT1-B, CPT1-C, CPT1A, CPT1B, CPT1c, CPT2, CPTi, CPTI beta, CPTII, CPTo, L-carnitine palmitoyltransferase, L-CPT 1, L-CPT1, M-CPT 1, M-CPTI, muscle carnitine palmitoyltransferase I, palmitoylcarnitine transferase, palmitoyltransferase, carnitine
ECTree
2.3.1.21 carnitine O-palmitoyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.3.1.21 - carnitine O-palmitoyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A305C
-
site-directed mutagenesis, the revertant mutant shows about wild-type activity
A478G
-
site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
C305A
C305D
-
73% of wild-type activity in mitochondrial fraction (COS-7 cell), 81% of wild-type expression in COS-7 cell
C305W
-
8% of wild-type activity in mitochondrial fraction, 30% of wild-type expression in COS-7 cell
C448A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C504A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C526A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity but increased sensitivity to malonyl-CoA compared to the wild-type enzyme
C548S
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C562A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C586A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity but reduced sensitivity to malonyl-CoA compared to the wild-type enzyme
C608A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity and sensitivity to malonyl-CoA compared to the wild-type enzyme
C659A
-
site-directed mutagenesis, the mutant shows unaltered catalytic activity but increased sensitivity to malonyl-CoA compared to the wild-type enzyme
DELTA1-18/V19A/L23A/S24A
-
143fold increase in IC50 for malonyl-CoA, 1.4fold decrease in KM-value for carnitine, 4fold increase in Km-value for palmitoyl-CoA
DELTA563-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA659-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA728-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA752-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA762-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
DELTA763-772
mitochondria from Pichia pastoris expressing the deletion mutant have no CPTI activity
E26K
-
site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
E26K/K561E
-
site-directed mutagenesis, the double mutant shows the same sensitivity to malonyl-CoA compared to the wild-type enzyme
E3A
E3A/H5A/V19A/L23A/S24A
-
97fold increase in IC50 for malonyl-CoA, 1.4fold decrease in KM-value for carnitine, 11fold decrease in Km-value for palmitoyl-CoA
E3A/V19A/L23A/S24A
-
143fold increase in IC50 for malonyl-CoA, 1.3fold decrease in KM-value for carnitine, 8.7fold decrease in Km-value for palmitoyl-CoA
F352C
F352C/V368I
H5A
-
2.1fold increase in IC50 for malonyl-CoA, 1.1fold increase in KM-value for carnitine, 1.7fold decrease in Km-value for palmitoyl-CoA
I66V/E531K
-
naturally occuring mutation, activity is not markedly different from wild-type enzyme, sensitivity toward malonyl-CoA is not markedly different from the sensitivity of wild-type enzyme
I66V/S427C
-
naturally occuring mutation, activity is not markedly different from wild-type enzyme, sensitivity toward malonyl-CoA is not markedly different from the sensitivity of wild-type enzyme
K561E
-
site-directed mutagenesis, the mutant shows decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
L764R
R243T
-
site-directed mutagenesis, the mutant shows highly decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
R243T/A478G
-
site-directed mutagenesis, the mutant shows highly decreased sensitivity to malonyl-CoA compared to the wild-type enzyme
S113L
S427C
-
naturally occuring mutation, activity is not markedly different from wild-type enzyme, sensitivity toward malonyl-CoA is not markedly different from the sensitivity of wild-type enzyme
V368I
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
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
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
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
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
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
C305A
-
5% of wild-type activity in mitochondrial fraction, 30% of wild-type expression in COS-7 cell
E3A
-
57fold increase in IC50 for malonyl-CoA, 1.5fold decrease in KM-value for carnitine, 1.2fold increase in Km-value for palmitoyl-CoA
E3A
-
used as reference mutation, similar activity as the wild-type enzyme, shows high resistance against malonyl-CoA
F352C/V368I
the mutant shows thermal instability, reduced residual enzyme activities and a short half-life compared to the wild type enzyme
S113L
-
natural missense mutation of CPT II, enzyme deficiency leads to myopathic syndroms, metabolic characterization, e.g. insulin resistance, increased content of muscle lipidsreduced lipolysis
S113L
mutant displays an abnormal thermal destabilization at 40°C and 45°C consistent with an increased flexibility at 40°C. Preincubation with L-carnitine and acyl-L-carnitines containing more than 10 carbons in the acyl side-chain stabilizes the mutant
V368I
the mutant shows thermal instability, reduced residual enzyme activities and a short half-life compared to the wild type enzyme
M593S
26fold increase in IC50 for malonyl-CoA, KM-value for carnitine is nearly identical to wild-type value, 1.5fold increase in Km-value for palmitoyl-CoA as compared to wild-type enzyme
W391A
mutation alters secondary structure, leading to decreased binding affinity for long chain fatty acid-CoA, and almost completely abolishes enzymic activity
W452A
mutation alters secondary structure, leading to decreased binding affinity for long chain fatty acid-CoA, and almost completely abolishes enzymic activity
additional information
-
overexpression of CPT I in skeletal muscle in vivo increases fatty acid oxidation, i.e. palmitate oxidation by 28%, and reduces triacylglycerol esterification, overview
additional information
-
screening for mutations in isozymes CPT1 and CPT2 encoding genes, determination of relation between mutations and metabolic disorders, age, onset and prognosis, overview
additional information
-
disruption of the cpt1c gene results in lower body weight and decreased food intake, construction of CPT1c knockout mice, which exhibit decreased rates of fatty acid oxidation, which may contribute to their increased susceptibility to diet-induced obesity, overview
additional information
Q7YQR7
chimaera in which the distinctive N-terminal segmant of ovine m-BPT 1 is replaced with that from rat M-CPT 1. The ovine N-terminal segment influences the kinetics of the enzyme for both its substrates, such that the Km for palmitoyl-CoA is decreased and that for carnitine is increased for the chimera, relative to the parental enzyme M-CPT 1 from Ovis aries
additional information
chimaera in which the distinctive N-terminal segmant of ovine m-BPT 1 is replaced with that from rat M-CPT 1. The ovine N-terminal segment influences the kinetics of the enzyme for both its substrates, such that the Km for palmitoyl-CoA is decreased and that for carnitine is increased for the chimera, relative to the parental enzyme M-CPT 1 from Ovis aries
additional information
-
chimaera in which the distinctive N-terminal segmant of ovine m-BPT 1 is replaced with that from rat M-CPT 1. The ovine N-terminal segment influences the kinetics of the enzyme for both its substrates, such that the Km for palmitoyl-CoA is decreased and that for carnitine is increased for the chimera, relative to the parental enzyme M-CPT 1 from Ovis aries
additional information
-
CPT I mutant with deletion of Arg395 show no activity
additional information
recombinant expression of the cytoplasmic C-terminal region of liver CPTI. The C-terminal 89 residues are sufficient for high affinity binding of long chain fatty acid-CoA and direct interaction with several cytoplasmic long chain fatty acid-CoA binding proteins, leading to enhanced enzymic activity
additional information
-
deletion of residues 1-18, and deletion of residues 1-28, human-pig chimeras
