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
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2.3.1.21
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peroxisome
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triglyceride
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proliferator-activated
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acyl-coas
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malonyl-coa
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obesity
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carboxylase
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adipose
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high-fat
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acetyl-coa
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beta-oxidation
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cholesterol
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hepatocytes
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cardiac
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palmitate
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sterol
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lipogenesis
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lipoprotein
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steatosis
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lipase
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amp-activated
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adipocytes
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obese
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acyltransferase
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triacylglycerols
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diet-induced
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element-binding
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etomoxir
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leptin
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lipogenic
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lipolysis
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adiponectin
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pparalpha
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srebp-1c
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medium-chain
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nafld
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nonalcoholic
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ketogenesis
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stearoyl-coa
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protein-1c
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hfd-induced
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rhabdomyolysis
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palmitate-induced
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srebf1
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anti-obesity
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muscle-type
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myoglobinuria
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lcfas
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synthesis
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medicine
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vlcad
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acaca
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pharmacology
- 2.3.1.21
- peroxisome
- triglyceride
-
proliferator-activated
- acyl-coas
- malonyl-coa
- obesity
- carboxylase
- adipose
-
high-fat
- acetyl-coa
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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
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hfd-induced
- rhabdomyolysis
-
palmitate-induced
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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 (KM Value
KM Value on EC 2.3.1.21 - carnitine O-palmitoyltransferase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.039
L-carnitine
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purified recombinant L-CPT I, reconstituted in liposomes
0.37
L-carnitine
wild-type protein and P504L/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.4893
L-carnitine
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enzyme from 3 month old animal, at 25°C, pH not specified in the publication
0.5
L-carnitine
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isoform L-CPT I, with 2[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylic acid
0.53
L-carnitine
wild-type protein and F352C/V368I/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.6697
L-carnitine
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enzyme at hatching, at 25°C, pH not specified in the publication
0.69
L-carnitine
enzyme from spleen, at pH 8.0 and 37°C
0.785
L-carnitine
Q7YQR7, Q8SPI7
chimaera in which the distinctive N-terminal segment of ovine m-BPT 1 is replaced with that from rat M-CPT 1
0.93
L-carnitine
enzyme from muscle, at pH 8.0 and 37°C
0.98
L-carnitine
enzyme from heart, at pH 8.0 and 37°C
1.152
L-carnitine
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enzyme from 6 month old animal, at 25°C, pH not specified in the publication
1.16
L-carnitine
enzyme from liver, at pH 8.0 and 37°C
1.201
L-carnitine
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enzyme from 1 month old animal, at 25°C, pH not specified in the publication
1.34
L-carnitine
enzyme from intestine, at pH 8.0 and 37°C
0.0127
palmitoyl-CoA
enzyme from intestine, at pH 8.0 and 37°C
0.0137
palmitoyl-CoA
enzyme from heart, at pH 8.0 and 37°C
0.014
palmitoyl-CoA
enzyme from muscle, at pH 8.0 and 37°C
0.0159
palmitoyl-CoA
enzyme from liver, at pH 8.0 and 37°C
0.0167
palmitoyl-CoA
enzyme from spleen, at pH 8.0 and 37°C
0.028
palmitoyl-CoA
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purified recombinant L-CPT I, reconstituted in liposomes
0.03
palmitoyl-CoA
Q7YQR7, Q8SPI7
chimaera in which the distinctive N-terminal segment of ovine m-BPT 1 is replaced with that from rat M-CPT 1
0.293
palmitoyl-CoA
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mitochondria isolated from 24-h-old, fasted pig, pH 7.2, 30°C
additional information
additional information
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Km values of deletion and chimeric L-CPT I mutants
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additional information
additional information
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Km values of deletion and chimeric L-CPT I mutants
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additional information
additional information
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influence of detergent on Km value
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additional information
additional information
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overview: Km values for several acyl-CoA and acyl-carnitine substrates, both reaction directions, peroxisomal and mitochondrial isozyme
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additional information
additional information
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effects of malonyl-CoA on kinetics
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additional information
additional information
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alterations in long-chain acyl-CoA binding to albumin in the CPT assay appreciablly affect the reaction at commonly used substrate concentrations
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additional information
additional information
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overview: Km values of recombinant chimeric proteins of L-CPT I and M-CPT I
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additional information
additional information
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Km values for carnitine with different acyl-CoA substrates
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additional information
additional information
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L-CPT I behaves like a natural chimera of M-CPT I and L-CPT I due to malonyl-CoA sensitivity and Km values compared to the enzymes of other organisms
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additional information
additional information
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the apparent KM-value in liver increases from birth to 3 weeks and then decreases and remains constant after 6 weeks of age. The highest Km-value is in 3-week old dogs and is about 50% greater than in older dogs. The apparent Km-value for carnitine measured in muscle is relatively constant in dogs of all ages tested. The apparent KM-for carnitine is 27% lower in muscle than in liver. Carnitine may have an important role in the regulation of fatty acid oxidation and incrrased dietary carnitine may improve fatty acid oxidative capacity in developing dogs
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additional information
additional information
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Michaelis-Menten kinetics at different developmental stages of cats, overview
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additional information
additional information
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Michaelis-Menten kinetics at different developmental stages of pigs, overview
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