Information on EC 2.3.1.21 - carnitine O-palmitoyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.3.1.21
-
RECOMMENDED NAME
GeneOntology No.
carnitine O-palmitoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
random sequential mechanism
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
2 independent inhibitory sites
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
broad sepcificity to acyl group, over the range C8 to C18
-
-
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
sigmoidal kinetics with both substrates
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
rapid-equilibrium random-order mechanism
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
flexible active site
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
active site three-dimensional structure model
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
optimal activity with palmitoyl-CoA
-
-
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
CPT I acts at 2 distinct sites, a regulatory and an active site
-
palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine
show the reaction diagram
the catalytic triad is composed of Cys305, His473, and Asp454, with Cys305 serving as a probable nucleophile, thus acting as a site for covalent attachment of the acyl molecule and formation of a stable acyl-enzyme intermediate, mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
Acyl group transfer
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
carnitine metabolism
-
-
Fatty acid degradation
-
-
mitochondrial L-carnitine shuttle
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acylcarnitine transferase
-
-
-
-
carnitine O-palmitoyltransferase
P18886, P32198
-
carnitine O-palmitoyltransferase I
-
-
carnitine palmitoyl transferase 1
-
-
carnitine palmitoyl transferase 1A
-
-
carnitine palmitoyl transferase 1A
Mus musculus C57BL/6J
-
-
-
carnitine palmitoyl transferase-I
-
-
carnitine palmitoyl-transferase-1c
-
-
carnitine palmitoyltransferae 1A
-
-
carnitine palmitoyltransferase
-
-
-
-
carnitine palmitoyltransferase
-
-
carnitine palmitoyltransferase
-
-
carnitine palmitoyltransferase 1
-
splice variant exon 6A; splice variant exon 6B
carnitine palmitoyltransferase 1
-
-
carnitine palmitoyltransferase 1
-
-
carnitine palmitoyltransferase 1
-
-
carnitine palmitoyltransferase 1A
-
-
carnitine palmitoyltransferase 1A
P32198
-
carnitine palmitoyltransferase 1B
-
-
carnitine palmitoyltransferase 2
-
-
carnitine palmitoyltransferase 2
P18886
-
carnitine palmitoyltransferase I
-
-
-
-
carnitine palmitoyltransferase I
-
-
carnitine palmitoyltransferase I
-
heart/muscle-type isoenzyme; liver-type isoenzyme
carnitine palmitoyltransferase I
Q92523
-
carnitine palmitoyltransferase I
-
-
carnitine palmitoyltransferase I
Q924X2
-
carnitine palmitoyltransferase I
-
-
carnitine palmitoyltransferase I
-
-
carnitine palmitoyltransferase I
P32198
-
carnitine palmitoyltransferase I
-
-
carnitine palmitoyltransferase I
Q5US13
-
carnitine palmitoyltransferase I activity
-
-
carnitine palmitoyltransferase IA
-
-
carnitine palmitoyltransferase IA
-
-
carnitine palmitoyltransferase II
-
-
-
-
carnitine palmitoyltransferase II
-
-
carnitine palmitoyltransferase II
P23786
-
carnitine palmitoyltransferase II
-
-
carnitine palmitoyltransferase-1
-
-
carnitine palmitoyltransferase-1
Q92523
-
carnitine palmitoyltransferase-1
-
-
carnitine palmitoyltransferase-1
-
-
carnitine palmitoyltransferase-1c
-
-
carnitine palmitoyltransferase-A
-
-
-
-
carnitine palmitoyltransferase-I
P32198
-
carnitine palmitoyltransferases 2
P23786
ubiquitous protein
CPT
-
-
-
-
CPT
P18886, P32198
-
CPT I
-
-
CPT I
Q924X2
-
CPT I
-
outer membrane carnitine palmitoyl transferase
CPT I
P32198
-
CPT-1
-
-
CPT-1
-
-
CPT-A
-
-
-
-
CPT-B
-
-
-
-
CPT-Ialpha
-
liver isoform
CPT-IL
P32198
-
CPT1
-
-
CPT1-A
P50416
liver isoenzyme
CPT1-B
-
muscle isoenzyme
CPT1-C
-
brain isoenzyme
CPT1A
Mus musculus C57BL/6J
-
-
-
CPT1A
Q7YQR7
-
CPT1B
Q8SP17
-
CPT1B
Q63704
-
CPT1c
Q8TCG5
-
CPT1c
-
-
CPT1c
Q8BGD5
-
CPT2
-
-
CPT2
P23786
-
CPT2
P18886
-
CPTi
-
inner form, tightly membrane bound
CPTi
-
inner, initially latent carnitine transferase
CPTI beta
Q5US13
-
CPTo
-
-
-
L-carnitine palmitoyltransferase
-
-
-
-
L-carnitine palmitoyltransferase
-
-
L-CPT 1
Q8SP17
-
M-CPT 1
Q7YQR7
-
M-CPTI
-
-
M-CPTI
Q92523
-
muscle carnitine palmitoyltransferase I
-
-
palmitoylcarnitine transferase
-
-
-
-
palmitoyltransferase, carnitine
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9068-41-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 enzyme forms: inner membrane enzyme in mitochondria and soluble enzyme from peroxisomes
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
CPT A, enzyme form on outer surface of the inner mitochondrial membrane, CPT B on the inner surface
-
-
Manually annotated by BRENDA team
CPT II
-
-
Manually annotated by BRENDA team
enzyme forms CPT I and CPT II
-
-
Manually annotated by BRENDA team
enzyme forms CPTi and CPTo
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
2 isoforms M-CPT I and L-CPT I
-
-
Manually annotated by BRENDA team
CPT I; CPT II
-
-
Manually annotated by BRENDA team
CPT II deficient mutant
-
-
Manually annotated by BRENDA team
CPT1-B; CPT1-C
-
-
Manually annotated by BRENDA team
CPT1A; CPT1-A
SwissProt
Manually annotated by BRENDA team
CPT2
SwissProt
Manually annotated by BRENDA team
gene CPT IB
-
-
Manually annotated by BRENDA team
isoform CPT1C
UniProt
Manually annotated by BRENDA team
isoform CPT2
SwissProt
Manually annotated by BRENDA team
isozyme CPT1A
-
-
Manually annotated by BRENDA team
isozyme M-CPT I
-
-
Manually annotated by BRENDA team
isozymes L-CPT1 and M-CPT1
-
-
Manually annotated by BRENDA team
Japanese population, isozymes CPT1 and CPT2
-
-
Manually annotated by BRENDA team
M-CPT I
-
-
Manually annotated by BRENDA team
obese NIDDM patients
-
-
Manually annotated by BRENDA team
tissue-specific isozymes L-CPT1 and M-CPT1
-
-
Manually annotated by BRENDA team
2 isoforms L-CPT I and M-CPT I
-
-
Manually annotated by BRENDA team
2 isoforms L-CPT I and M-CPT I
-
-
Manually annotated by BRENDA team
C57BL/6J mice
-
-
Manually annotated by BRENDA team
gene cpt1c, brain-specific isozyme CPT1c
-
-
Manually annotated by BRENDA team
isoform CPT1C
UniProt
Manually annotated by BRENDA team
male C57BL/6J mice, tissue-specific isozymes L-CPT1 and M-CPT1
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6J
C57BL/6J mice
-
-
Manually annotated by BRENDA team
no activity in Pichia pastoris
-
-
-
Manually annotated by BRENDA team
CPT I
-
-
Manually annotated by BRENDA team
2 isoforms CPTo (I) and CPTi (II)
-
-
Manually annotated by BRENDA team
2 isoforms L-CPT I and M-CPT I
-
-
Manually annotated by BRENDA team
2 isoforms L-CPT I and M-CPT I; 2 isoforms of CPT I in heart mitochondria, liver L-CPT I, skeletal muscle M-CPT I
-
-
Manually annotated by BRENDA team
2 isoforms of CPT I in heart mitochondria, liver L-CPT I, skeletal muscle M-CPT I; enzyme form CPT I
-
-
Manually annotated by BRENDA team
enzyme form CPT I; enzyme form CPT II
-
-
Manually annotated by BRENDA team
enzyme form CPT I; Walker 256 tumour rat
-
-
Manually annotated by BRENDA team
enzyme form CPT II
-
-
Manually annotated by BRENDA team
enzyme forms CPTo and CPTi from outer and inner mitochondrial membrane
-
-
Manually annotated by BRENDA team
iisoform CPT1a
SwissProt
Manually annotated by BRENDA team
isoform CPT1a
SwissProt
Manually annotated by BRENDA team
isoform CPT1b
UniProt
Manually annotated by BRENDA team
isozymes L-CPT1 and M-CPT1
-
-
Manually annotated by BRENDA team
male Sprague-Dawley rat
UniProt
Manually annotated by BRENDA team
male Sprague-Dawley rat
SwissProt
Manually annotated by BRENDA team
male Sprague-Dawley rat
-
-
Manually annotated by BRENDA team
male Sprague-Dawley rats, tissue-specific isozymes L-CPT I and M-CPT I
-
-
Manually annotated by BRENDA team
male wistar rat
-
-
Manually annotated by BRENDA team
recombinant liver CPT I
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats, tissue-specific isozymes L-CPT1 and M-CPT1
-
-
Manually annotated by BRENDA team
Wistar rat
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
2 isoforms of CPT I in liver mitochondria, liver L-CPT I, skeletal muscle M-CPT I
-
-
Manually annotated by BRENDA team
CPT I
-
-
Manually annotated by BRENDA team
Valanga nigricornis
Burm., grasshopper
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Q8BGD5
CPT1C expression correlates inversely with mammalian target of rapamycin pathway activation, and contributes to rapamycin resistance in murine primary tumors. Tumor cells constitutively expressing CPT1C show increased fatty acid oxidation, ATP production, and resistance to glucose deprivation or hypoxia. Cancer cells lacking CPT1C produce less ATP and are more sensitive to metabolic stress. CPT1C depletion via siRNA suppresses xenograft tumor growth and metformin responsiveness in vivo
physiological function
Q8TCG5
isoform CPT1C expression is frequently up-regulated in human lung tumors. Tumor cells constitutively expressing CPT1C show increased fatty acid oxidation, ATP production, and resistance to glucose deprivation or hypoxia. Conversely, cancer cells lacking CPT1C produce less ATP and are more sensitive to metabolic stress. CPT1Cdepletion via siRNA suppresses xenograft tumor growth and metformin responsiveness in vivo. CPT1C can be induced by hypoxia or glucose deprivation and is regulated by AMPKalpha
physiological function
-
measurements of enzyme activity in mitochondria isolated from newborn, 24-h-old, fed or fasted, and 5-months-old pigs. Acetate rather than ketone bodies is the predominant radiolabeled product, and its production increases twofold with increasing fatty acid oxidation during the first 24-h suckling period. The rate of acetogenesis is directly proportional to isoform CPT I activity. The high activity of CPT I in 24-h-suckling piglets is not attributable to an increase in CPT I gene expression, but rather to a large decrease in the sensitivity of CPT I to malonyl-CoA inhibition, which offsets a developmental decrease in affinity of CPT I for palmitoyl-CoA. Acetate is the primary product of hepatic mitochondrial beta-oxidation in Sus scrofa and regulation during early development is mediated primarily via kinetic modulation of isoform CPT I.
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4,8-dimethylnonanoyl-CoA+ L-carnitine
CoA + 4,8-dimethylnonanoyl-L-carnitine
show the reaction diagram
P23786
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
Valanga nigricornis
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
reverse reaction with palmitoylcarnitine, reverse reaction: myristoylcarnitine
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity
-
?, r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity
reverse reaction: acyl-CoA substrates are C4 to C18 acylcarnitines
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
preference for desaturated long-chain acyl CoAs
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
substrate specificity at early developmental stages in skeletal muscle
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT II shows greater chain-length substrate specificity for transfer of long chain fatty acyl groups from (-)-acylcarnitine derivatives to CoA-SH with greatest activity being obtained in the transfer of stearoyl and palmitoyl groups
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
C4 to C18 acyl-CoAs
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
C4 to C18 acyl-CoAs
reverse reaction: acyl-CoA substrates are C4 to C18 acylcarnitines
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
overview: activity towards long-chain polyunsaturated fatty acids and their CoA esters
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT II requires preincubation with CoA-SH for manifestation of catalytic activity, isozyme CPT II catalyzes the reaction only in the direction towards long-chain fatty acyl-CoA formation, CPT I catalyzes reaction in both directions
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I unlike CPT II requires membrane integrity for catalytic function
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
effect of octylglucoside and Triton X-100 on specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
activity with different substrates of wild-type CPT I with and without gamma-linoleic acid treatment
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I activity is involved in cardiac mitochondrial beta-oxidation flux control
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme is involved in apoptosis induction
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I is the rate-limiting enzyme in beta-oxidation of long-chain fatty acids
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I, involved in regulation of fatty acid oxidation
-
?
arachidoyl-CoA + L-carnitine
CoA + L-arachidoylcarnitine
show the reaction diagram
-
-
-
-
?
butyryl-CoA + L-carnitine
CoA + L-butyrylcarnitine
show the reaction diagram
-
-
-
-
?
butyryl-CoA + L-carnitine
CoA + L-butyrylcarnitine
show the reaction diagram
-
-
-
-
-
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
-
-
r
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
-
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
-
-
-
-
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
-
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
-
-
r
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
P23786
-
-
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
best substrate
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
best substrate
-
r
docosanhexaenoyl-CoA + L-carnitine
CoA + L-docosanhexaenoylcarnitine
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + L-carnitine
CoA + L-dodecanoylcarnitine
show the reaction diagram
P23786
-
-
-
?
erucoyl-CoA + L-carnitine
CoA + L-erucoylcarnitine
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
show the reaction diagram
-
-
-
r
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
show the reaction diagram
-
-
-
-
-
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
show the reaction diagram
-
-
-
r
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
P23786
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
show the reaction diagram
-
-
-
-
?
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
show the reaction diagram
-
-
-
r
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
show the reaction diagram
-
-
-
-
-
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
show the reaction diagram
P23786
-
-
-
?
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
show the reaction diagram
-
best substrate
-
r
linoleoyl-CoA + L-carnitine
CoA + L-linoleoylcarnitine
show the reaction diagram
-
-
-
-
?
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
show the reaction diagram
-
-
-
r
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
show the reaction diagram
-
-
-
?
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
show the reaction diagram
-
-
-
?
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
show the reaction diagram
P23786
-
-
-
?
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
show the reaction diagram
-
best substrate
-
-
?
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
P23786
-
-
-
?
oleoyl-CoA + L-carnitine
CoA + L-oleoylcarnitine
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + L-carnitine
CoA + L-oleoylcarnitine
show the reaction diagram
-
activity is 264% higher than with stearoyl-CoA
-
-
?
palmitoleoyl-CoA + L-carnitine
CoA + L-palmitoleoylcarnitine
show the reaction diagram
-
activity is 47% higher than with palmitoyl-CoA
-
-
?
palmitoyl-CoA + DL-carnitine
CoA + DL-palmitoylcarnitine
show the reaction diagram
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
-
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
Valanga nigricornis
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
P23786
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
Q92523
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
Q7YQR7, Q8SP17
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
Q5US13
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
P32198
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
P18886, P32198
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
Q924X2
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
best substrate
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
chimeric L-CPT I with exchanged C-terminals between pig and rat enzymes
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
CPT I catalyzes the conversion of long-chain fatty acyl-CoAs to acyl carnitines in the presence of L-carnitine, a rate-limiting step in the transport of long-chain fatty acids from the cytoplasm to the mitochondrial matrix
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
CPT I is considered the rate-limiting step in the oxidation of long-chain fatty acids and is an important site in the regulation of flux through beta-oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
enzyme inhibition reduces hepatic glucose production and plasma lipids in non-insulin-dependent diabetes mellitus, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
regulation, mechanism, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
the enzyme is important in mitochondrial fatty acid beta-oxidation, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
the enzyme is the main regulatory enzyme involved in fatty acid oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
deuterium-labeled L-carnitine substrate
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
the enzyme catalyzes the transfer of an acyl-CoA moiety from a long-chain acyl-CoA ester to carnitine to form acylcarnitine
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
Mus musculus C57BL/6J
-
regulation, mechanism, overview
-
-
?
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
-
-
-
-
?
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
show the reaction diagram
-
-
-
-
r
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
show the reaction diagram
-
-
-
?
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
show the reaction diagram
-
-
-
-
-
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
show the reaction diagram
-
-
-
-
?
trans-2-hexadecenoyl-CoA + L-carnitine
CoA + trans-2-hexadecenoyl-L-carnitine
show the reaction diagram
P23786
-
-
-
?
linoleoyl-CoA + L-carnitine
CoA + L-linoleoylcarnitine
show the reaction diagram
-
preference for
-
r
additional information
?
-
-
the branched chain fatty acid CoA-thioesters pristanoyl-CoA and phytanoyl-CoA, i.e. 2,6,10,14-tetramethylhexadecanoyl-CoA and 3,7,11,15-tetramethylhexadecanoyl-CoA, are no substrates in vivo, since they cannot be transported into mitochondria of liver
-
-
-
additional information
?
-
-
acyl-CoA binding protein ACBP forms binary complexes with acyl-CoA and possibly transfers acyl-CoA to CPT I, CPT I induces conformational changes in ACBP leading to release of acyl-CoA
-
-
-
additional information
?
-
-
participates in fatty acyl group transport into mitochondria
-
-
-
additional information
?
-
-
participates in fatty acyl group transport into mitochondria
-
-
-
additional information
?
-
-
gamma-linolenic acid diet leads to several physiological effects during cancer therapy, e.g. reduction of mitochondrial metabolic activity, modification of mitochondrial outer membrane composition, increase in lipid peroxidation, cytoplasmic accumulation of acyl-CoA, reduction of CPT I activity, and malonyl-CoA sensitivity
-
-
-
additional information
?
-
-
responsible for transferase activity on the outer side of the inner mitochondrial membrane
-
-
-
additional information
?
-
P23786, P50416
CPT1-A defificiency presents as recurrent attacks of fasting hypoketotic hypoglycemia
-
-
-
additional information
?
-
P23786, P50416
the adult form of CPT2 deficiency is characterized by episodes of rhabdomyolysis triggered by prolonged exercise. The prevalent S113L mutation is found in about 50% of mutant alleles. The infantile-type CPT2 deficiency presents as severe attacks of hypoketptic hypoglycemia, occasionally associated with cardiac damage commonly responsible for sudden death before 1 year of age. In addition to theses symptoms features of brain and kidney dysorganogenesis are frequently seen in the neonatal-onset CPT2 deficiency, almost always lethal during the first month of life. 40 mutations habe been characterized in patients with the adult, infantile or neonatal form of CPT2 deficiency
-
-
-
additional information
?
-
-
CPT1c is necessary for the regulation of energy homeostasis, and does not catalyze acyl transfer from various fatty acyl-CoAs to carnitine
-
-
-
additional information
?
-
-
CPT2 deficiency and glutaric aciduria type 2 are related
-
-
-
additional information
?
-
-
the enzyme is involved in long-chain fatty acid oxidation, overview
-
-
-
additional information
?
-
-
the enzyme is rate-limiting in the mitochondrial fatty axid oxidation pathway, physiologic regulation, inhibition of fatty acid oxidation increases food intake, overview
-
-
-
additional information
?
-
-
the enzyme is rate-limiting in the mitochondrial fatty axid oxidation pathway, physiologic regulation, overview
-
-
-
additional information
?
-
-
the brain-specific isozyme CPT1c has a unique function or activation mechanism, and does not catalyze acyl transfer from various fatty acyl-CoAs to carnitine, no activity with diverse acyl-CoAs, overview
-
-
-
additional information
?
-
-
activity with unsaturated fatty acyl-CoA substrates is significantly higher or trended higher than that with their saturated counterparts of the same chain length, and activity is higher with shorter fatty acyl-CoAs for a given number of double bonds. The pattern of substrate preference is not different between captive white-throated sparrows in a migratory or non-migratory state
-
-
-
additional information
?
-
P23786
isoform CPT2 is active with medium and long-chain acyl-CoA esters, whereas virtually no activity is found with short- and very long-chain acyl-CoAs or with branched-chain amino acid oxidation intermediates. Trans-2-enoyl-CoA intermediates are poor substrates, too. Isoform CPT2 is able to reverse its physiological mechanism for medium and long-chain acyl-CoAs contributing to the abnormal acylcarnitines profiles characteristic of most mitochondrial fatty acid beta-oxidation disorders, no substrates are: isovaleryl-CoA, isobutyryl-CoA, acetoacetyl-CoA, DL-3-hydroxybutyryl-CoA, 3-hydroxyisobutyryl-CoA, 2-methylacetoacetyl-CoA, methylcrotonyl-CoA, glutaryl-CoA, 3-hydroxy-3-methylglutaryl-CoA, 2-methylbutyryl-CoA, 2-methyl-3-hydroxybutyryl-CoA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
Valanga nigricornis
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I activity is involved in cardiac mitochondrial beta-oxidation flux control
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme is involved in apoptosis induction
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I is the rate-limiting enzyme in beta-oxidation of long-chain fatty acids
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I, involved in regulation of fatty acid oxidation
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
P18886, P32198
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
Q924X2
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
CPT I catalyzes the conversion of long-chain fatty acyl-CoAs to acyl carnitines in the presence of L-carnitine, a rate-limiting step in the transport of long-chain fatty acids from the cytoplasm to the mitochondrial matrix
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
CPT I is considered the rate-limiting step in the oxidation of long-chain fatty acids and is an important site in the regulation of flux through beta-oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
enzyme inhibition reduces hepatic glucose production and plasma lipids in non-insulin-dependent diabetes mellitus, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
regulation, mechanism, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
the enzyme is important in mitochondrial fatty acid beta-oxidation, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
-
the enzyme is the main regulatory enzyme involved in fatty acid oxidation
-
-
?
palmitoyl-CoA + L-carnitine
L-palmitoylcarnitine + CoA
show the reaction diagram
-
forward reaction by CPT I and reverse reaction by CPT II
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
show the reaction diagram
Mus musculus C57BL/6J
-
regulation, mechanism, overview
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
show the reaction diagram
-
CPT I, involved in regulation of fatty acid oxidation
-
?
additional information
?
-
-
participates in fatty acyl group transport into mitochondria
-
-
-
additional information
?
-
-
participates in fatty acyl group transport into mitochondria
-
-
-
additional information
?
-
-
gamma-linolenic acid diet leads to several physiological effects during cancer therapy, e.g. reduction of mitochondrial metabolic activity, modification of mitochondrial outer membrane composition, increase in lipid peroxidation, cytoplasmic accumulation of acyl-CoA, reduction of CPT I activity, and malonyl-CoA sensitivity
-
-
-
additional information
?
-
-
responsible for transferase activity on the outer side of the inner mitochondrial membrane
-
-
-
additional information
?
-
P23786, P50416
CPT1-A defificiency presents as recurrent attacks of fasting hypoketotic hypoglycemia
-
-
-
additional information
?
-
P23786, P50416
the adult form of CPT2 deficiency is characterized by episodes of rhabdomyolysis triggered by prolonged exercise. The prevalent S113L mutation is found in about 50% of mutant alleles. The infantile-type CPT2 deficiency presents as severe attacks of hypoketptic hypoglycemia, occasionally associated with cardiac damage commonly responsible for sudden death before 1 year of age. In addition to theses symptoms features of brain and kidney dysorganogenesis are frequently seen in the neonatal-onset CPT2 deficiency, almost always lethal during the first month of life. 40 mutations habe been characterized in patients with the adult, infantile or neonatal form of CPT2 deficiency
-
-
-
additional information
?
-
-
CPT1c is necessary for the regulation of energy homeostasis, and does not catalyze acyl transfer from various fatty acyl-CoAs to carnitine
-
-
-
additional information
?
-
-
CPT2 deficiency and glutaric aciduria type 2 are related
-
-
-
additional information
?
-
-
the enzyme is involved in long-chain fatty acid oxidation, overview
-
-
-
additional information
?
-
-
the enzyme is rate-limiting in the mitochondrial fatty axid oxidation pathway, physiologic regulation, inhibition of fatty acid oxidation increases food intake, overview
-
-
-
additional information
?
-
-
the enzyme is rate-limiting in the mitochondrial fatty axid oxidation pathway, physiologic regulation, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
-
activates peroxisomal enzyme
KCl
-
high above micellar concentrations increase conversion of palmitoylcarnitine to palmitoyl-CoA by facilitating the removal of palmitoyl-CoA from the enzyme surface
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11-trimethylamino-undecanoyl-DL-carnitine
-
-
-
2-bromoacetyl-CoA
-
-
2-Bromopalmitoyl-CoA
-
irreversible
2-Bromopalmitoyl-CoA
-
-
2-Bromopalmitoyl-CoA
-
no inhibition
2-Bromopalmitoyl-CoA
-
with addition of carnitine
2-Bromopalmitoyl-CoA
-
-
2-Bromopalmitoyl-CoA
-
irreversible; with addition of carnitine
2-[5(4-Chlorophenyl)pentyl]-oxirane-2-carboxyl-CoA
-
-
4-hydroxy phenylglyoxylate
-
CPT I, greatly reduced inhibition of protease treated enzyme
acetyl-CoA
-
-
acetyl-CoA
-
-
acetyl-CoA
-
CPT I, inhibition is not affected by proteinase treatment
Bile acids
-
e.g. in cholestatic rats
Bromoacetyl-CoA
-
-
C75-CoA
-
potent competitive inhibition, IC50: 0.00025 mM in INS(832/13) cells, IC50: 0.00046 in L6E9 myotubes, binds tightly but reversibly to CPT I, C75 applied in vivo is transformed to C75-CoA and inhibits fatty acid oxidation, e.g. in pancreatic INS(823/13), muscle L6E9, or kidney HEK293 cell lines, inhibition mechanism, overview, molecular model of docking of C75-CoA to L-CPT I
C75-CoA
-
potent competitive inhibition, binds tightly but reversibly to CPT I, C75 applied in vivo is transformed to C75-CoA and inhibits fatty acid oxidation, a single intraperitoneal injection of C75 in mice produced short-term inhibition of CPT I activity in mitochondria from the liver, soleus, and pancreas, inhibition mechanism, overview
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
-
deoxycarnitine
-
-
diethyl dicarbonate
-
CPT II, strong, linear pseudo-first order kinetic, modification of a histidine residue, reversible by hydroxylamine, decanoyl-CoA and L-carnitine
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
-
-
etomoxir
-
etomoxir is a racemate of two optically active phenoxyalkyloxirane carboxylic acid ethyl esters, of which only the (+), but not the (-)-enantiomer, inhibits CPT-I
Etomoxir-CoA
-
CPTo
Etomoxiryl-CoA
-
IC50: 0.00121 mM in INS(832/13) cells, IC50: 0.00287 in L6E9 myotubes
Etomoxiryl-CoA
-
-
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
-
competitve to palmitoyl-carnitine in the reverse reaction; i.e. HPC, 2S,6R:2R,6S-6-carboxymethyl-2-hydroxy-2-pentadecyl-4,4-dimethylmorpholinium bromide
Hemipalmitoylcarnitinium bromide
-
CPT I, strong, active-site-directed, inhibition not altered by protease treatment; i.e. HPC, 2S,6R:2R,6S-6-carboxymethyl-2-hydroxy-2-pentadecyl-4,4-dimethylmorpholinium 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-aminocarnitine
-
inhibition of CPT II not CPT I
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
-
similar inhibition of wild-type CPT I and mutants A381D and H473A
malonyl-CoA
-
no inhibition
malonyl-CoA
-
inhibition of soluble peroxisomal form, no inhibition of enzyme from inner mitochondrial membrane
malonyl-CoA
-
-
malonyl-CoA
-
CPT I
malonyl-CoA
-
Triton X-100 protects
malonyl-CoA
-
CPTo
malonyl-CoA
-
benzyl alcohol, isoamyl alcohol and 2-(2-methoxyethoxy)ethyl-8-(cis-2-n-octylpropyl)octanoate decrease the ability of malonyl-CoA to inhibit CPT I; inhibition is temperature dependent
malonyl-CoA
-
mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive
malonyl-CoA
-
CPT II not inhibited; mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive
malonyl-CoA
-
a malonyl-CoA insensitive enzyme and a malonyl-CoA sensitive enzyme; enzyme from liver mitochondrial inner membrane becomes inhibitable by malonyl-CoA if reconstituted with outer membrane malonyl-CoA binding protein; mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive; no inhibition
malonyl-CoA
-
mitochondrial isozyme CPT I, sensitivity against malonyl-CoA is mediated by a 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation, detergent and salt sensitive; regulatory role in vivo
malonyl-CoA
-
CPT I
malonyl-CoA
-
CPT I; regulatory role in vivo
malonyl-CoA
-
differences in sensitivity of hepatic and heart enzyme
malonyl-CoA
-
CPT I
malonyl-CoA
-
CPT I; inhibition is very pH-dependent: malonyl-CoA concentrations causing 50% inhibition at pH 6.0, 6.5, 7.0, 7.5 and 8.0 are 0.00004, 0.001, 0.009, 0.04 and 0.2 mM, respectively
malonyl-CoA
-
no inhibition
malonyl-CoA
-
reversible inhibition
malonyl-CoA
-
CPT I; CPT II not inhibited; reversible inhibition
malonyl-CoA
-
a malonyl-CoA insensitive enzyme and a malonyl-CoA sensitive enzyme
malonyl-CoA
-
inhibition of isoform L-CPT I is increased by 2[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylic acid
malonyl-CoA
-
partial proteolysis of CPT I greatly diminishes the inhibitory effect
malonyl-CoA
-
inhibition is pH-dependent; inhibition is temperature dependent
malonyl-CoA
-
CPT II not inhibited; CPT I, native and reconstituted in phospholipid micelles
malonyl-CoA
-
CPT I; CPT I catalytic activity and malonyl-CoA sensitivity is located on 1 single polypeptide; CPT II not inhibited; recombinant CPT I is highly sensitive, recombinant CPT II not
malonyl-CoA
-
CPT I; isoforms L-CPT I and M-CPT I
malonyl-CoA
-
CPT I; CPT I, inhibition depends on age; inhibition is temperature dependent; regulatory role in vivo
malonyl-CoA
-
L-CPT I, recombinant enzyme from Saccharomyces cerevisiae is inhibited only in intact mitochondria, not as solubilized enzyme
malonyl-CoA
-
CPT I; CPT II not inhibited; regulatory role in vivo
malonyl-CoA
-
overview: recombinant chimeric proteins of L-CPT I and M-CPT I
malonyl-CoA
-
inhibits CPT I not CPT II; regulatory role in vivo
malonyl-CoA
-
inhibits CPT I not CPT II; isoforms L-CPT I and M-CPT I
malonyl-CoA
-
differences in sensitivity of hepatic and heart enzyme; inhibits CPT I not CPT II; isoforms L-CPT I and M-CPT I
malonyl-CoA
-
L-CPT I
malonyl-CoA
-
CPT I, sensitivity is reduced in vivo during gamma-linolenic acid treatment; membrane or micelle composition and properties influence the sensitivity of CPT I to inhibition
malonyl-CoA
-
sensitivity to inhibition of deletion and chimeric L-CPT I mutants
malonyl-CoA
-
CPT I; membrane or micelle composition and properties influence the sensitivity of CPT I to inhibition; regulatory role in vivo
malonyl-CoA
-
Glu3, Leu23, and Ser24 in M-CPTI are important for malonyl-CoA inhibition and binding but not for calalysis. IC50: 0.00007 mM for wild-type enzyme, 0.01 mM for mutant enzyme E3A, 0.00015 for mutant enzyme H5A, 0.01 mM for mutant enzyme E3A/V19A/L23A/S24A, 0.0068 mM for mutant enzyme E3A/H5A/V19A/L23A/S24A
malonyl-CoA
Q7YQR7, Q8SP17
IC50 for wild-type L-CPT-1 is 0.0298 mM; IC50 for wild-type M-CPT-1 is 0.010 mM
malonyl-CoA
Q5US13
IC50: 906 nM
malonyl-CoA
-
IC50: 0.00339 mM for wild-type enzyme, 0.00021 mM for mutant enzyme E590A, 0.00039 mM for mutant enzyme E590Q, 0.00025 mM for mutant enzyme E590K
malonyl-CoA
-
IC50: 0.0123 for wild-type enzyme, 0.015 mM for mutant enzyme T314S, 0.0087 mM for mutant enzyme N464D, 0.0395 mM for mutant enzyme A478G, 0.0275 mM for mutant enzyme C608A, 0.319 mM for mutant enzyme M593 mM, 0.155 mM for mutant enzyme M593A, 0.22 mM for mutant enzyme M593E
malonyl-CoA
-
phosphorylation of the CKII site in the C-terminal end of CPT-I leads to decreased malonyl-CoA sensitivity
malonyl-CoA
-
the activity of CPT I is largely controlled by cytosolic levels of its biological inhibitor malonyl-CoA, being a key regulator of fatty acid partitioning in skeletal muscle by virtue of its ability to inhibit CPT I
malonyl-CoA
-
allosteric inhibition
malonyl-CoA
-
has a regulatory role in vivo
malonyl-CoA
-
IC50: 0.0005 mM for the recombinant wild-type enzyme, IC50: 0.00052 mM for the recombinant revertant A305C, IC50 values of recombinant mutant isozymes M-CPT I, overview
malonyl-CoA
-
IC50: 0.0073 mM for the recombinant wild-type isozyme CPT1A, IC50: 0.0384 mM for CPT1A mutant R243T, IC50 values of other mutants, overview, determination of two binding sites, the A site and the O site, the latter involved residue Arg243, binding structure, interactions between N- and C-terminal residues are involved in malonyl-CoA binding to the A site, isozyme CPT1A in malonyl-CoA molecular docking, overview
malonyl-CoA
-
-
malonyl-CoA
-
-
malonyl-CoA
-
-
methylmalonyl-CoA
-
CPT I
methylmalonyl-CoA
-
inhibits sheep liver CPT I, no inhibition of rat liver and guinea-pig liver mitochondrial CPT I
nagarse
-
mitochondria, malonyl-CoA protects
-
octyl glucoside
-
with octanoyl-CoA as substrate, competitive
octyl glucoside
-
only CPTo
octyl glucoside
-
complete loss of CPT I activity, no loss of CPT II activity
octyl-glucoside
-
-
oxfenicine
-
-
oxfenicine
-
-
palmitoyl-CoA
-
product inhibition, reverse reaction
palmitoyl-CoA
-
substrate inhibition
palmitoyl-CoA
-
CPT I, slightly
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
-
CPT I, strong, inhibitory effect is drastically reduced by protease treatment of outer mitochondrial membrane; malonyl-CoA analogue
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
-
CPTo
Tetradecylglycidyl-CoA
-
and analogues, irreversible
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
trans-2-hexadecenoyl-CoA
P23786
competitive
Triton X-100
-
mutant CPT
Triton X-100
-
only CPTo
Triton X-100
-
erythrocyte enzyme is not affected
Triton X-100
-
complete loss of CPT I activity, no loss of CPT II activity
Triton X-100
-
recombinant CPT I, complete inactivation at 5%, at least partly reversible
Trypsin
-
peroxisomal and mitochondrial isozymes
-
Trypsin
-
mitochondria, malonyl-CoA protects
-
Tween 20
-
-
Tween 20
-
only CPTo at 2% and above
methylmalonyl-CoA
-
partial proteolysis of CPT I slightly diminishes the inhibitory effect
additional information
-
different sites of inhibition of carnitine palmitoyltransferase by malonyl-CoA, acetyl-CoA and CoA
-
additional information
-
no inhibition by choline, hemiacetylcarnitinium
-
additional information
-
CPT I, 2 independent binding sites for acyl-CoA inhibitors and regulation of fatty acid oxidation, the malonyl-CoA site is located on the cytoplasmic face of the outer mitochondrial membrane, the site for monocarboxylic acids and free CoA is located in the mitochondrial intermembrane space
-
additional information
-
physiological role of malonyl-CoA in the heart
-
additional information
-
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
-
additional information
-
enzyme inhibitors are used to shift the heart's reliance away from fatty acid oxidation to glucose as energy source to increase cardiac efficiency, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
C-75
-
i.e. 3-carboxy-4-alkyl-2-methylenebutyrolactone, physiologic enzyme stimulation, regulatory effects, overview
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
daidzein
-
activates 5.5fold, induces the enzyme expression
daidzein
-
-
di(2-ethyl-hexyl)phtalate
-
-
genistein
-
activates 3fold alone, and about 6fold in concert with L-carnitine, induces the enzyme expression
genistein
-
-
L-carnitine
-
activates 3fold alone, and about 6fold in concert with genistein, induces the enzyme expression
L-carnitine
-
-
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
-
only CPTi
-
Phosphatidylcholine liposomes
-
high above micellar concentrations increase conversion of palmitoylcarnitine to palmitoyl-CoA by facilitating the removal of palmitoyl-CoA from the enzyme surface
-
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 peroxisomal enzyme
Tween 20
-
activates only CPTi
liothyronine
-
-
additional information
-
clofibrate induces the enzyme expression in transfected Huh-7 cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.022
acetyl-CoA
-
-
0.0051
Butyryl-CoA
-
-
0.03
Butyryl-CoA
-
-
0.0055
CoA
-
-
0.0009
decanoyl-CoA
-
-
0.017
decanoyl-CoA
-
-
0.004
Dodecanoyl-CoA
-
-
0.0018
Hexanoyl-CoA
-
-
0.152
Hexanoyl-CoA
-
-
0.0017
L-carnitine
-
mutant T314S
0.0041
L-carnitine
-
mutant N464D
0.0049
L-carnitine
-
wild-type
0.0061
L-carnitine
-
mutant M593A
0.0063
L-carnitine
-
mutant M593E
0.0074
L-carnitine
-
mutant M593S
0.0151
L-carnitine
-
mutant A478G
0.0243
L-carnitine
-
mutant C608A
0.039
L-carnitine
-
purified recombinant L-CPT I, reconstituted in liposomes
0.042
L-carnitine
-
-
0.056
L-carnitine
-
30C, recombinant CPT1A mutant R243T
0.0593
L-carnitine
-
wild-type enzyme
0.0748
L-carnitine
-
mutant enzyme E590Q
0.0876
L-carnitine
-
mutant enzyme E590A
0.092
L-carnitine
-
CPT I
0.093
L-carnitine
-
mutant A381D
0.098
L-carnitine
-
CPT I after gamma-linoleic acid treatment
0.1
L-carnitine
-
recombinant wild-type L-CPT I
0.105
L-carnitine
-
recombinant CPT II
0.108
L-carnitine
-
with C8-CoA
0.12
L-carnitine
-
with C12-CoA
0.12
L-carnitine
P23786
wild-type protein, COS-7 cell lysate
0.126
L-carnitine
-
recombinant wild-type L-CPT I
0.129
L-carnitine
-
recombinant wild-type CPT I
0.13
L-carnitine
P23786
V368I mutant protein, COS-7 cell lysate
0.135
L-carnitine
-
30C, recombinant wildtype isozyme CPT1A
0.14
L-carnitine
P23786
M647V mutant protein, COS-7 cell lysate
0.147 - 0.28
L-carnitine
-
liver CPT 1
0.147
L-carnitine
-
3 wk old pig, liver
0.17
L-carnitine
-
peroxisomal soluble enzyme
0.179
L-carnitine
-
1 wk old pig, liver
0.18
L-carnitine
-
-
0.185
L-carnitine
-
with C16-CoA
0.197
L-carnitine
Q5US13
pH 7.0, recombinant enzyme
0.1976
L-carnitine
-
wild-type protein, mitochondrial preparation
0.2
L-carnitine
-
isoform L-CPT I
0.215
L-carnitine
Q7YQR7, Q8SP17
wild-type L-CPT 1
0.218
L-carnitine
-
adult pig, liver
0.228 - 0.46
L-carnitine
-
skeletal muscle CPT 1
0.228
L-carnitine
-
1 wk old pig, skeletal muscle
0.244
L-carnitine
-
8 wk old pig, liver
0.245
L-carnitine
-
24 h old pig, skeletal muscle
0.254
L-carnitine
-
24 h old pig, liver
0.278
L-carnitine
-
newborn pig, liver
0.28
L-carnitine
-
5 wk old pig, liver; adult pig, skeletal muscle
0.314
L-carnitine
-
3 wk old pig, skeletal muscle
0.326
L-carnitine
-
8 wk old pig, skeletal muscle
0.35
L-carnitine
P23786
P504L mutant protein, COS-7 cell lysate; V605L mutant protein, COS-7 cell lysate
0.36
L-carnitine
P23786
F352C mutant protein, COS-7 cell lysate
0.37
L-carnitine
P23786
F352C/V368I mutant protein, COS-7 cell lysate; wild-type protein and P504L/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.38
L-carnitine
P23786
P504L/V605L mutant protein, COS-7 cell lysate
0.381
L-carnitine
-
newborn pig, skeletal muscle
0.406
L-carnitine
-
-
0.424 - 0.534
L-carnitine
-
pH 7.2, 30C, skeletal muscle CPT 1
0.431 - 0.527
L-carnitine
-
pH 7.2, 30C, liver CPT 1
0.45
L-carnitine
-
-
0.46
L-carnitine
-
5 wk old pig, skeletal muscle
0.5
L-carnitine
-
isoform L-CPT I, with 2[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylic acid
0.52
L-carnitine
P23786
F352C/V368I/V605L mutant protein, COS-7 cell lysate
0.53
L-carnitine
P23786
wild-type protein and F352C/V368I/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.56
L-carnitine
Q7YQR7, Q8SP17
wild-type M-CPT 1
0.59 - 1
L-carnitine
-
-
0.6059
L-carnitine
-
E17D mutant protein, mitochondrial preparation
0.617
L-carnitine
-
mutant enzyme E3A
0.63
L-carnitine
-
mutant enzyme DELTA1-18/V19A/L23A/S24A
0.652
L-carnitine
-
mutant enzyme E3A/H5A/V19A/L23A/S24A
0.679
L-carnitine
-
wild-type enzyme
0.683
L-carnitine
-
wild-type protein, mitochondrial preparation
0.706
L-carnitine
-
mutant enzyme E3A/V19A/L23A/S24A
0.7695
L-carnitine
-
D17E mutant protein, mitochondrial preparation
0.785
L-carnitine
Q7YQR7, Q8SP17
chimaera in which the distinctive N-terminal segment of ovine m-BPT 1 is replaced with that from rat M-CPT 1
0.824
L-carnitine
-
pH 8.0, 37C, recombinant wild-type enzyme
0.913
L-carnitine
-
wild-type enzyme
0.92
L-carnitine
-
pH 8.0, 37C, recombinant revertant A305C
0.95
L-carnitine
-
recombinant CPT II
0.968
L-carnitine
-
mutant enzyme H5A
1.588
L-carnitine
-
mutant enzyme L764R
2.18
L-carnitine
-
-
2.8
L-carnitine
-
inner mitochondrial membrane
58.53
L-carnitine
-
microsomes of PC-12 cells overexpressing CPT1c
127
L-carnitine
-
microsomes, PC-12 cell, CPT1a
1.139
L-octanoylcarnitine
-
-
0.123
L-palmitoylcarnitine
-
-
0.14
L-palmitoylcarnitine
-
-
0.011
Lauroyl-CoA
-
-
0.0012
myristoyl-CoA
-
-
0.031
myristoyl-CoA
-
-
0.0085
Octanoyl-CoA
-
-
0.023
Octanoyl-CoA
-
-
0.0008
palmitoyl-CoA
-
-
0.0008
palmitoyl-CoA
-
with C8-CoA
0.0017
palmitoyl-CoA
-
mutant T314S
0.0041
palmitoyl-CoA
-
mutant N464D
0.0049
palmitoyl-CoA
-
recombinant wild-type CPT I
0.0049
palmitoyl-CoA
-
wild-type
0.0052
palmitoyl-CoA
-
-
0.0061
palmitoyl-CoA
-
mutant M593A
0.0062
palmitoyl-CoA
-
mutant enzyme E3A/H5A/V19A/L23A/S24A
0.0063
palmitoyl-CoA
-
mutant M593E
0.007
palmitoyl-CoA
-
30C, recombinant CPT1A mutant R243T
0.0071
palmitoyl-CoA
P23786
pH 7.4, 37C
0.0074
palmitoyl-CoA
-
mutant M593S
0.0078
palmitoyl-CoA
-
mutant enzyme E3A/V19A/L23A/S24A
0.011
palmitoyl-CoA
-
CPT I
0.0122
palmitoyl-CoA
-
-
0.0151
palmitoyl-CoA
-
mutant A478G
0.017
palmitoyl-CoA
-
CPT I after gamma-linoleic acid treatment
0.018
palmitoyl-CoA
-
-
0.0242
palmitoyl-CoA
-
-
0.0243
palmitoyl-CoA
-
mutant C608A
0.028
palmitoyl-CoA
-
purified recombinant L-CPT I, reconstituted in liposomes
0.03
palmitoyl-CoA
Q7YQR7, Q8SP17
chimaera in which the distinctive N-terminal segment of ovine m-BPT 1 is replaced with that from rat M-CPT 1
0.033
palmitoyl-CoA
-
mutant A381D
0.034
palmitoyl-CoA
-
recombinant CPT II
0.035
palmitoyl-CoA
-
recombinant wild-type L-CPT I
0.0374
palmitoyl-CoA
Q7YQR7, Q8SP17
wild-type L-CPT1
0.039
palmitoyl-CoA
-
-
0.0404
palmitoyl-CoA
-
mutant enzyme H5A
0.043
palmitoyl-CoA
-
recombinant wild-type L-CPT I
0.0448
palmitoyl-CoA
-
mutant enzyme L764R
0.0466
palmitoyl-CoA
-
wild-type enzyme
0.047
palmitoyl-CoA
-
-
0.055
palmitoyl-CoA
-
-
0.0622
palmitoyl-CoA
-
mutant enzyme E590A
0.066
palmitoyl-CoA
-
pH 8.0, 37C, recombinant revertant A305C
0.0676
palmitoyl-CoA
Q7YQR7, Q8SP17
wild-type M-CPT1
0.0679
palmitoyl-CoA
-
wild-type enzyme
0.073
palmitoyl-CoA
-
pH 8.0, 37C, recombinant wild-type enzyme
0.0744
palmitoyl-CoA
-
mutant enzyme E590Q
0.079
palmitoyl-CoA
-
mitochondria isolated from newborn pig, pH 7.2, 30C
0.0823
palmitoyl-CoA
-
mutant enzyme E3A
0.083
palmitoyl-CoA
Q5US13
pH 7.0, recombinant enzyme
0.0989
palmitoyl-CoA
-
-
0.104
palmitoyl-CoA
-
-
0.142
palmitoyl-CoA
-
mitochondria isolated from 24-h-old, fed pig, pH 7.2, 30C
0.1535
palmitoyl-CoA
-
wild-type enzyme
0.273
palmitoyl-CoA
-
mutant enzyme DELTA1-18/V19A/L23A/S24A
0.293
palmitoyl-CoA
-
mitochondria isolated from 24-h-old, fasted pig, pH 7.2, 30C
0.4
palmitoyl-CoA
-
30C, recombinant wildtype isozyme CPT1A
0.461
palmitoyl-CoA
-
mitochondria isolated from adult pig, pH 7.2, 30C
0.52
palmitoyl-CoA
-
-
4.9
palmitoyl-CoA
-
microsomes, PC-12 cell, CPT1a
25.35
palmitoyl-CoA
-
microsomes of PC-12 cells overexpressing CPT1c
0.0017
stearoyl-CoA
-
-
0.018
stearoyl-CoA
-
-
0.0081
trans-2-hexadecenoyl-CoA
P23786
pH 7.4, 37C
0.013
Lauroyl-CoA
-
-
additional information
additional information
-
effects of malonyl-CoA on kinetics
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
influence of detergent on Km value
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
overview: Km values for several acyl-CoA and acyl-carnitine substrates, both reaction directions, peroxisomal and mitochondrial isozyme
-
additional information
additional information
-
alterations in long-chain acyl-CoA binding to albumin in the CPT assay appreciablly affect the reaction at commonly used substrate concentrations
-
additional information
additional information
-
-
-
additional information
additional information
-
Km values for carnitine with different acyl-CoA substrates
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
overview: Km values of recombinant chimeric proteins of L-CPT I and M-CPT I
-
additional information
additional information
-
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
-
additional information
additional information
-
Km values of deletion and chimeric L-CPT I mutants
-
additional information
additional information
-
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
-
additional information
additional information
-
Michaelis-Menten kinetics at different developmental stages of pigs, overview
-
additional information
additional information
-
Michaelis-Menten kinetics at different developmental stages of cats, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
11-trimethylamino-undecanoyl-DL-carnitine
-
-
-
0.9
2-bromoacetyl-CoA
-
-
0.00066
2-Bromopalmitoyl-CoA
-
-
0.045
acetyl-CoA
-
-
0.6
chenodeoxycholic acid
-
-
0.045
CoA
-
-
0.0016
Hemipalmitoylcarnitinium bromide
-
with palmitoyl-carnitine, reverse reaction
0.0051
Hemipalmitoylcarnitinium bromide
-
with carnitine, forward reaction
0.0215
Hemipalmitoylcarnitinium bromide
-
with palmitoyl-CoA, forward reaction
0.0035
L-aminocarnitine
-
CPT II
0.00022
malonyl-CoA
-
-
0.00067
malonyl-CoA
-
KI-values: 0.00064 mM and 0.0007 mM malony-CoA (from secondary Dixon plots)
15
octyl-glucoside
-
with octanoyl-CoA as substrate
0.009
palmitoylcarnitine
-
versus palmitoyl-CoA
0.014
palmitoylcarnitine
-
versus carnitine
0.0104
Palmitoylcholine
-
versus palmitoyl-CoA
0.019
Palmitoylcholine
-
versus carnitine
0.0188
trans-2-hexadecenoyl-CoA
P23786
pH 7.4, 37C
0.17
malonyl-CoA
-
-
additional information
additional information
-
tissue-specific inhibition kinetics
-
additional information
additional information
-
inhibition kinetics with malonyl-CoA
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
C75-CoA
-
IC50: 0.00004 mM in muscle
0.00024
C75-CoA
-
IC50: 0.00024 mM recombinant isozyme L-CPT I
0.00025
C75-CoA
-
potent competitive inhibition, IC50: 0.00025 mM in INS(832/13) cells, binds tightly but reversibly to CPT I, C75 applied in vivo is transformed to C75-CoA and inhibits fatty acid oxidation, e.g. in pancreatic INS(823/13), m
0.00036
C75-CoA
-
IC50: 0.00036 mM recombinant isozyme M-CPT I, binds tightly but reversibly to CPT I, C75 applied in vivo is transformed to C75-CoA
0.00046
C75-CoA
-
IC50: 0.00046 mM in L6E9 myotubes, binds tightly but reversibly to CPT I, C75 applied in vivo is transformed to C75-CoA and inhibits fatty acid oxidation, e.g. in pancreatic INS(823/13), m
0.0007
C75-CoA
-
potent competitive inhibition, IC50: 0.0007 mM in liver
0.000015
Etomoxiryl-CoA
-
IC50: 0.000015 mM in muscle
0.00025
Etomoxiryl-CoA
-
IC50: 0.00025 mM in liver
0.00121 - 0.00287
Etomoxiryl-CoA
-
IC50: 0.00121 mM in INS(832/13) cells, IC50: 0.00287 in L6E9 myotubes
0.0031
Etomoxiryl-CoA
-
IC50: 0.0031 mM recombinant isozyme M-CPT I
0.0041
Etomoxiryl-CoA
-
IC50: 0.0041 mM recombinant isozyme L-CPT I
0.00003
malonyl-CoA
-
-
0.00007
malonyl-CoA
-
Glu3, Leu23, and Ser24 in M-CPTI are important for malonyl-CoA inhibition and binding but not for calalysis. IC50: 0.00007 mM for wild-type enzyme, 0.01 mM for mutant enzyme E3A, 0.00015 for mutant enzyme H5A, 0.01 mM for mutant enzyme E3A/V19A/L23A/S24A,
0.00007
malonyl-CoA
-
mitochondrial isolate from liver, high polyunsaturated fat diet
0.000079
malonyl-CoA
-
CPT I, liver
0.000096
malonyl-CoA
-
wild-type protein, 1 mM carnitine, mitochondrial preparation
0.00011
malonyl-CoA
-
mitochondrial isolate from liver, high saturated fat diet
0.000117
malonyl-CoA
-
wild-type protein, 0.683 mM carnitine, mitochondrial preparation
0.00012
malonyl-CoA
-
mitochondrial isolate from liver, control diet
0.00019
malonyl-CoA
-
chimeric protein: residues 1-50 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.00019
malonyl-CoA
-
mitochondria isolated from newborn pig, pH 7.2, 30C
0.00021
malonyl-CoA
-
mitochondria isolated from adult pig, pH 7.2, 30C
0.000246
malonyl-CoA
-
D17E mutant protein, 0.770 mM carnitine, mitochondrial preparation
0.00026
malonyl-CoA
-
mitochondria isolated from 24-h-old, fed pig, pH 7.2, 30C
0.000279
malonyl-CoA
-
D17E mutant protein, 1 mM carnitine, mitochondrial preparation
0.000284
malonyl-CoA
-
E17D mutant protein, 0.606 mM carnitine, mitochondrial preparation
0.000297
malonyl-CoA
-
E17D mutant protein, 1 mM carnitine, mitochondrial preparation
0.000325
malonyl-CoA
-
chimeric protein: residues 1-128 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.00035
malonyl-CoA
-
mitochondrial isolate from red muscle, high polyunsaturated fat diet
0.000359
malonyl-CoA
-
chimeric protein: residues 1-128 of human enzyme recombined with pig enzyme, mitochondrial preparation
0.00037
malonyl-CoA
-
CPT I, white muscle
0.0004
malonyl-CoA
-
CPT I, heart
0.000457
malonyl-CoA
-
chimeric protein: residues 1-50 of human enzyme recombined with pig enzyme, mitochondrial preparation
0.0005
malonyl-CoA
-
IC50: 0.0005 mM for the recombinant wild-type enzyme
0.00052
malonyl-CoA
-
IC50: 0.00052 mM for the recombinant revertant A305C, IC50 values of recombinant mutant isozymes M-CPT I overview
0.00053
malonyl-CoA
-
mitochondria isolated from 24-h-old, fasted pig, pH 7.2, 30C
0.00055
malonyl-CoA
-
CPT I, red muscle
0.00055
malonyl-CoA
-
wild-type protein, 0.198 mM carnitine, mitochondrial preparation
0.00074
malonyl-CoA
-
at 0.035 mM palmitoyl-CoA
0.00076
malonyl-CoA
-
at 0.035 mM palmitoyl-CoA
0.000804
malonyl-CoA
-
wild-type protein, 1 mM carnitine, mitochondrial preparation
0.000906
malonyl-CoA
Q5US13
IC50: 906 nM
0.00101
malonyl-CoA
-
at 0.07 mM palmitoyl-CoA
0.00119
malonyl-CoA
-
mitochondrial isolate from red muscle, control diet
0.00183
malonyl-CoA
-
mitochondrial isolate from red muscle, high saturated fat diet
0.00232
malonyl-CoA
-
at 0.07 mM palmitoyl-CoA
0.00339
malonyl-CoA
-
IC50: 0.00339 mM for wild-type enzyme, 0.00021 mM for mutant enzyme E590A, 0.00039 mM for mutant enzyme E590Q, 0.00025 mM for mutant enzyme E590K
0.0073 - 0.0384
malonyl-CoA
-
IC50: 0.0073 mM for the recombinant wild-type isozyme CPT1A, IC50: 0.0384 mM for CPT1A mutant R243T, IC50 values of other mutants, overview, determination of two binding sites, the A site and the O site, the latter involved residue Arg243, binding struct
0.0087
malonyl-CoA
-
IC50 0.0087 mM for mutant enzyme N464D
0.01
malonyl-CoA
Q7YQR7, Q8SP17
IC50 for wild-type M-CPT-1 is 0.010 mM
0.0123
malonyl-CoA
-
IC50: 0.0123 for wild-type enzyme
0.015
malonyl-CoA
-
IC50 0.015 mM for mutant enzyme T314S
0.0252
malonyl-CoA
-
10 min pre-incubation with malonyl-CoA
0.0275
malonyl-CoA
-
IC50 0.0275 mM for mutant enzyme C608A
0.0298
malonyl-CoA
Q7YQR7, Q8SP17
IC50 for wild-type L-CPT-1 is 0.0298 mM
0.03556
malonyl-CoA
-
protein with deletion of residue 1-18, mitochondrial preparation
0.03919
malonyl-CoA
-
protein with deletion of residue 1-28, mitochondrial preparation
0.0395
malonyl-CoA
-
IC50 0.0395 mM for mutant enzyme A478G
0.0768
malonyl-CoA
-
mitochondrial isolate
0.1058
malonyl-CoA
-
without pre-incubation with malonyl-CoA
0.1103
malonyl-CoA
-
mitochondrial isolate, after incubation with protein kinase A
0.155
malonyl-CoA
-
IC50 0.155 mM for mutant enzyme M593A
0.319
malonyl-CoA
-
IC50 0.319 mM for mutant enzyme M593 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00035
-
transfected HEK-293T cell
0.0006
P18886, P32198
hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period; hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.00062
P23786
F352C/V368I/V605L mutant protein, COS-7 cell lysate
0.00063
P23786
wild-type protein and F352C/V368I/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.00071
P23786
P504L/V605L mutant protein, COS-7 cell lysate
0.00072
P23786
F352C/V368I mutant protein, COS-7 cell lysate; wild-type protein and P504L/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.00073
P23786
F352C mutant protein, COS-7 cell lysate
0.00076
P23786
P504L mutant protein, COS-7 cell lysate
0.00078
P23786
V605L mutant protein, COS-7 cell lysate
0.0008
P18886, P32198
hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period; hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.00081
P23786
M647V mutant protein, COS-7 cell lysate
0.00085
P23786
V368I mutant protein, COS-7 cell lysate
0.00087
P23786
wild-type protein, COS-7 cell lysate
0.001
P18886, P32198
hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period; hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.0013
-
cell line 3T3-L1, CPT I, 6 days after differentiation
0.0013
-
native L-CPT I in liver mitochondria
0.0014
-
CPT I after gamma-linoleic acid treatment
0.0017
P18886, P32198
hepatocytes transduced with adenovirus encoding CPT-1a exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period; 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
P18886, P32198
hepatocytes transduced with adenovirus encoding CPT-1a exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period; 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
0.002
-
CPT II, red muscle
0.0021
P18886, P32198
hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding beta-galctosidase, incubation with palmitate; hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding beta-galctosidase, incubation with palmitate
0.0021
-
rat primary hepatocytes infected with adenovirus vectors expressing Ad-GFP
0.00227
-
mitochondrial fraction, wild-type protein expressed in COS-7 cell
0.00279
-
wild-type protein, mitochondrial preparation
0.0028
-
recombinant revertant A305C
0.0029
-
recombinant wild-type enzyme
0.0029
P18886, P32198
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding beta-galctosidase, incubation with palmitate; hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding beta-galctosidase, incubation with palmitate; hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding CPT-2, incubation with palmitate; hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding CPT-2, incubation with palmitate
0.0032
-
mitochondrial fraction of recombinant Pichia pastoris expressing CPT I
0.0032
-
mitochondrial fraction of recombinant Saccharomyces cerevisiae expressing L-CPT I
0.0033
P18886, P32198
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-2, incubation with palmitate; hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-2, incubation with palmitate
0.0036
-
CPT I
0.0036
-
rat primary hepatocytes infected with adenovirus vectors expressing Ad-PGC-1beta
0.0041
P18886, P32198
hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate; hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate
0.00416
-
chimeric protein: residues 1-128 of human enzyme recombined with pig enzyme, mitochondrial preparation
0.00443
-
wild-type protein, mitochondrial preparation
0.00449
-
chimeric protein: residues 1-50 of human enzyme recombined with pig enzyme, mitochondrial preparation
0.0046
-
CPT II, liver
0.0047
-
CPT I, heart, plus 50 microM malonyl-CoA
0.0051
P18886, P32198
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate; hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate
0.0052
-
recombinant wild-type L-CPT I
0.0054
-
CPT I, liver, plus 50 microM malonyl-CoA; CPT I, white muscle, plus 50 microM malonyl-CoA
0.0062
-
cell line 3T3-L1, CPT II, 6 days after differentiation
0.0063
P18886, P32198
hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period; 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
0.0073
-
solubilized CPT
0.0078
-
recombinant wild-type L-CPT I
0.0081
-
CPT I, liver
0.0083
-
CPT II, white muscle
0.009
-
CPT I
0.00942
-
protein with deletion of residue 1-28, mitochondrial preparation
0.00943
-
chimeric protein: residues 1-50 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.01059
-
chimeric protein: residues 1-128 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.0106
-
CPT II, heart
0.0128
-
CPT I, red muscle, plus 50 microM malonyl-CoA
0.0148
-
CPT I, white muscle
0.01528
-
protein with deletion of residue 1-18, mitochondrial preparation
0.0168
-
CPT I, heart
0.0263
-
CPT I, red muscle
0.0367
-
mitochondrial fraction, 1 mM palmitoyl-CoA
0.0565
-
mitochondrial fraction
0.43
-
recombinant CPT II from Sf 9 insect cells
0.473
-
purified recombinant L-CPT I, reconstituted in liposomes
4.65
-
purified mitochondrial enzyme
13.2
-
purified peroxisomal enzyme
24
-
purified enzyme
29.6
-
purified enzyme
40
-
purified enzyme
42
-
purified enzyme
47.5
-
purified enzyme
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
activity at early developmental stages in skeletal muscle
additional information
-
CPT I and II activities in muscle biopsis
additional information
-
activities of deletion and chimeric L-CPT I mutants
additional information
-
quantitative expression analysis
additional information
-
activity of mutant enzymes
additional information
-
plasma and free carnitine levels at different developmental stages of pigs, overview
additional information
-
plasma and free carnitine levels and enzyme activity at different developmental stages, overview
additional information
-
activity of tissue-specific isozymes L-CPT1 and M-CPT1, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
-
6.5 - 8
-
mitochondrial
6.8
-
assay at
7 - 8.2
-
-
7
-
activity assay
7
-
activity assay
7.1
-
assay at
7.2
-
assay at
7.2
-
assay at
7.2
-
activity assay
7.4
-
assay at
7.4
-
assay at
7.4
-
assay at
7.5
-
assay at
7.5
-
assay at
7.6
-
assay at
8
-
assay at
8.5
-
peroxisomal
additional information
-
pI: 8.5
additional information
-
pI: 6.0
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 8.8
-
L-CPT I
6 - 8
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
activity assay at room temperature
22
-
assay at
25
-
assay at
25
-
assay at
25
-
assay at
27
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
assay at
30
-
activity assay
37
-
assay at
37
-
assay at
37
-
activity assay
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
-
two-dimensional electrophoresis
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
CPT I and CPT II
Manually annotated by BRENDA team
P23786, P50416
CPT1-B
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
-
Manually annotated by BRENDA team
-
low content L-CPT I and CPT II
Manually annotated by BRENDA team
-
brain-specific isozyme
Manually annotated by BRENDA team
P23786, P50416
CPT1-C is predominantly expressed in
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
high level of mRNA
Manually annotated by BRENDA team
Q8TCG5
brain-specific enzyme
Manually annotated by BRENDA team
Q8BGD5
brain-specific enzyme
Manually annotated by BRENDA team
P23786, P50416
low level of expression of CPT1-C
Manually annotated by BRENDA team
-
present to a significant greater extent in flight muscle than in fat body
Manually annotated by BRENDA team
Valanga nigricornis
-
-
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
-
Manually annotated by BRENDA team
-
CPT II, M-CPT I and low content of L-CPT I
Manually annotated by BRENDA team
-
L-CPT I
Manually annotated by BRENDA team
-
2 isoforms of CPT I
Manually annotated by BRENDA team
-
M-CPT I
Manually annotated by BRENDA team
P23786, P50416
CPT1-B
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
high level of mRNA
Manually annotated by BRENDA team
-
isozyme M-CPT I
Manually annotated by BRENDA team
-
kidney cell line
Manually annotated by BRENDA team
-
pancreatic cell line
Manually annotated by BRENDA team
-
small and large, L-CPT I and CPT II
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
-
Manually annotated by BRENDA team
-
cortex and medulla, L-CPT I and CPT II
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
high level of mRNA
Manually annotated by BRENDA team
-
muscle cell line
Manually annotated by BRENDA team
-
CPT I and CPT II
Manually annotated by BRENDA team
-
L-CPT I
Manually annotated by BRENDA team
-
M-CPT I
Manually annotated by BRENDA team
-
activity is low at birth, increases by 100% during the suckling period and declines after weaning to adult levels
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
high level of mRNA
Manually annotated by BRENDA team
-
isozyme CPT1A
Manually annotated by BRENDA team
-
isozyme L-CPT I
Manually annotated by BRENDA team
-
L-CPT1 isozyme
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
CPT1A
-
Manually annotated by BRENDA team
-
low content L-CPT I and CPT II
Manually annotated by BRENDA team
P23786, P50416
-
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
lactating, high level of mRNA
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
non-lactating, high level of mRNA
Manually annotated by BRENDA team
-
isozyme M-CPT I
Manually annotated by BRENDA team
-
isozyme M-CPT I
Manually annotated by BRENDA team
-
white and red gastrocnemius muscles
Manually annotated by BRENDA team
-
red, white and heart muscle
Manually annotated by BRENDA team
-
present to a significant greater extent in flight muscle than in fat body
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
P23786, P50416
low level of expression of CPT1-C
Manually annotated by BRENDA team
-
low content of CPT II, no CPT I
Manually annotated by BRENDA team
-
Musculus vastus lateralis
Manually annotated by BRENDA team
-
intermyofibrillar and subsarcolemmal
Manually annotated by BRENDA team
-
activity continues to increase with age, reaching adult levels after 9 weeks. Concentration in adult is 10fold the apparent Km-value for carnitine
Manually annotated by BRENDA team
P23786, P50416
CPT1-B
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
high level of mRNA
Manually annotated by BRENDA team
P23786, P50416
low level of expression of CPT1-C
Manually annotated by BRENDA team
Q7YQR7, Q8SP17
-
Manually annotated by BRENDA team
-
L-CPT I, not M-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
P23786, P50416
expression of CPT1-B
Manually annotated by BRENDA team
P23786, P50416
low level of expression of CPT1-C
Manually annotated by BRENDA team
additional information
-
not in spleen
Manually annotated by BRENDA team
additional information
-
liver L-CPT I is identical with the small isoform CPT I from heart, the large isoform of CPT I from heart resembles M-CPT I from skeletal muscle
Manually annotated by BRENDA team
additional information
Q7YQR7, Q8SP17
no activity in spleen
Manually annotated by BRENDA team
additional information
P23786, P50416
ubiquitous expression of CPT2
Manually annotated by BRENDA team
additional information
-
activity of tissue-specific isozymes L-CPT1 and M-CPT1, overview
Manually annotated by BRENDA team
additional information
-
ontogeny and activity in liver and muscle throughout growth and development of the domestic felid, overview
Manually annotated by BRENDA team
additional information
-
ontogeny, enzyme activity, and tenzyme expression throughout growth and development, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
inner envelope membrane with isoform CPT I on the outer, cytosolic side and isoform CPT II on the inner, stromal side of the membrane
Manually annotated by BRENDA team
-
peroxisomal, liver
Manually annotated by BRENDA team
-
membrane-bound
Manually annotated by BRENDA team
-
inner face of inner membrane
Manually annotated by BRENDA team
-
inner face of inner membrane
Manually annotated by BRENDA team
-
enzyme is present on both sides of the inner membrane, not on the outer membrane
Manually annotated by BRENDA team
-
enzyme from outer and from inner membrane have different properties
Manually annotated by BRENDA team
-
outer face of inner membrane
Manually annotated by BRENDA team
-
enzyme from outer and from inner membrane have different properties
Manually annotated by BRENDA team
-
L-CPT I in outer membrane, native and recombinant in Saccharomyces cerevisiae
Manually annotated by BRENDA team
-
CPT I is located in the outer membrane
Manually annotated by BRENDA team
-
CPT I is located in the outer membrane
Manually annotated by BRENDA team
-
CPT I is located in the outer membrane
Manually annotated by BRENDA team
-
of subsarcolemmal mitochondria, transmembrane enzyme
Manually annotated by BRENDA team
Valanga nigricornis
-
-
Manually annotated by BRENDA team
-
2 isoforms of CPT I, L-CPT I and M-CPT I
Manually annotated by BRENDA team
-
2 isoforms of CPT I, L-CPT I and M-CPT I
Manually annotated by BRENDA team
-
2 isoforms of CPT I, L-CPT I and M-CPT I
Manually annotated by BRENDA team
-
2 isoforms of CPT I, L-CPT I and M-CPT I
Manually annotated by BRENDA team
-
recombinant L-CPT I and M-CPT I in Pichia pastoris
Manually annotated by BRENDA team
P32198
mitochondrial outer membrane, enzyme is found in large molecular mass complexes that also contain long chain acyl-CoA synthetase and the voltage-dependent anion channel, with strong interaction between the three proteins
Manually annotated by BRENDA team
-
of newborn, 24-h old, fed or fasted, and 5-months-old pigs
Manually annotated by BRENDA team
Mus musculus C57BL/6J
-
-
-
Manually annotated by BRENDA team
additional information
-
transport mechanism for acylcaritine and carnitine through the mitochondrial inner membrane
-
Manually annotated by BRENDA team
additional information
-
transport mechanism for acylcaritine and carnitine through the mitochondrial inner membrane
-
Manually annotated by BRENDA team
additional information
-
forward reaction by CPT I at outer mitochondrial membrane, transport of acylcarnitine through mitochondrial membrane, reverse reaction at inner face of inner membrane by CPT II, overview
-
Manually annotated by BRENDA team
additional information
-
forward reaction by CPT I at outer mitochondrial membrane, transport of acylcarnitine through mitochondrial membrane, reverse reaction at inner face of inner membrane by CPT II, overview
-
Manually annotated by BRENDA team
additional information
-
composition of the outer mitochondrial membrane is important for functionality and activity of CPT I
-
Manually annotated by BRENDA team
additional information
-
liver isoform of carnitine palmitoyltransferase 1, L-CPT 1, is not targeted to the endoplasmic reticulum
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63000
-
gel filtration
486523
63500
-
gel filtration, sucrose density gradient sedimentation
486528
66000
-
peroxisomes, gel filtration
486549
67000
-
gel filtration
486522
75000
-
determined by SDS-PAGE and Western Blot analysis
686125
150000
-
CPT I and II, gel filtration
486569
260000
-
mitochondria, gel filtration
486549
274000
-
gel filtration
486565
280000 - 320000
-
gel filtration
486529
430000
-
CPTo and CPTi, gel filtration
486564
660000
-
about, gel filtration
486530
additional information
-
3-dimensional structural model of CPT I active site based on X-ray diffraction analysis data from similar rat enoyl-CoA hydratase; amino acid sequence, alignment
486309
additional information
-
enzyme migrates as part of a detergent micelle with MW of 510000 on gel filtration
486526
additional information
-
amino acid composition
486528
additional information
-
amino acid sequence, alignment
486541
additional information
-
mitochondrial enzyme, 86 kDa malonyl-CoA binding protein complexed with CPT and other proteins of the beta-oxidation
486542
additional information
-
-
486543
additional information
-
amino acid sequence of peptides
486565
additional information
-
CPT I is composed of different structural segments: 1. a cytosolic N-terminal domain of 46 amino acid residues, 2. 2 transmembranal parts TM1 and TM2, 3. a 27-residue loop between TM1 and 2, 4. a cytosolic catalytic C-terminal domain, amino acid sequences
486582
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 67000, SDS-PAGE
?
-
x * 68000, SDS-PAGE
?
-
x * 69200, SDS-PAGE
?
-
x * 68000, liver, CTP II
?
-
x * 82000, L-CPT I, SDS-PAGE
?
-
x * 20000, CPT I and II, SDS-PAGE
?
-
x * 82000, M-CPT I, SDS-PAGE
?
-
x * 88000, recombinant CPT I, SDS-PAGE, x * 70000, recombinant CPT II, SDS-PAGE
?
-
x * 88200, isozymes L-CPT1 and M-CPT1
?
-
x * 66000, SDS-PAGE, Western blot analysis
monomer
-
1 * 62500, SDS-PAGE
monomer
-
1 * 64000, peroxisomes, SDS-PAGE
monomer
-
1 * 94000, liver, SDS-PAGE, 1 * 86000, muscle, SDS-PAGE
tetramer
-
4 * 66000, SDS-PAGE
tetramer
-
4 * 69000, mitochondria
monomer
-
1 * 63500, SDS-PAGE
additional information
-
CPTo and CPTi are distinct proteins, 90000 MW subunit of liver and 86000 MW subunit of muscle constitutes a component of their respective CPTo system, the 66000 MW subunit of CPTi does not constitute a part of the CPTo system
additional information
-
CPTo and CPTi are associated with a complex that contains beta-oxidation enzymes
additional information
-
86000 MW malonyl-CoA binding protein is a regulatory subunit of the carnitine palmitoyltransferase complex
additional information
-
rat liver mitochondria carnitine palmitoyltransferase may be composed of an easily dissociable catalytic unit and a malonyl-CoA sensitivity conferring regulatory component
additional information
P32198
enzyme is found in large molecular mass complexes that also contain long chain acyl-CoA synthetase and the voltage-dependent anion channel, with strong interaction between the three proteins
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
18.9 mol of bound phospholipid per mol of enzyme, cardiolipin phosphatidylethanolamine and phosphatidylcholine
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
acetylation
-
on N-terminal Ala2
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
-
stable for 24 h at 4C, recombinant CPT II
486574
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
P23786
mutant proteins V605L, F352C, and P504L: enzyme activities of transfected cells are significantly reduced to 59.5 to 43.6% during incubation for 2 hours at 41C, mutant protein F352C/V368I/V605L: enzyme activity of transfected cells is reduced to 19.4% during incubation for 2 hours at 41C
703967
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes
-
glycerol, 20%, stabilizes
-
Triton X-100: erythrocyte plasma membrane enzyme is stable, enzyme from microsomes and mitochondrial outer membrane not
-
fractionation causes rapid loss of CPTo activity, CPTi is relatively stable
-
no loss in activity after 6 freeze/thaw cycles at -70C 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
-20C, several months
-
4C, 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
calf liver
-
CPT II
-
peroxisomal
-
native enzyme partially by microsome preparation
-
recombinant M-CPT I from Pichia pastoris
-
native enzyme partially by microsome preparation
-
mitochondria are preparated
-
partial, CPT I and II
-
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
-
mitochondria are prepared
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
-
expressed in COS-7 cell
-
expressed in Pichia pastoris
-
expressed in the distal hindlimb muscles of Rattus norvegicus
-
expression in Saccharomyces cerevisiae
P23786
expression of wild-type and mutant isozyme CPT1A in Saccharomyces cerevisiae
-
expression of wild-type and mutant isozymes M-CPT I in Pichia pastoris strain GS115
-
gene CPT 1B, overexpression in isolated extensor digitorum longus, EDL, muscle strips, electrotransfection
-
isozymes CPT1 and CPT2
-
mutant enzymes expressed in Pichia pastoris
-
overexpression of M-CPT I in Pichia pastoris, containing about 24 copies of the expression vector
-
quantitative expression analysis, expression in Huh-7 cells, treatment with clofibrate induces the enzyme expression
-
gene cpt1c, expression in HEK-293T cells
-
quantitative expression analysis
-
expression in Pichia pastoris; expression in Pichia pastoris
Q7YQR7, Q8SP17
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
-
expression in Escherichia coli
P32198
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; recombinant adenoviruses containing cDNAs encoding rat CPT1a and rat CPT2 are constructed
P18886, P32198
2 isoforms of CPT I, liver L-CPT I, skeletal muscle M-CPT I, cloned from liver, expression in Pichia pastoris GS115, DNA sequence determination; in vitro transcription and translation of L-CPT I
-
construction of chimeric L-CPT I with deletions and exchanged C-terminal sequences between rat and pig enzymes, expression in Pichia pastoris
-
CPTI beta is expressed in Pichia pastoris
Q5US13
expressed in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform CPT1C expression is frequently up-regulated in human lung tumors. CPT1C can be induced by hypoxia or glucose deprivation and is regulated by AMPKalpha
Q8TCG5
isoform CPT1C can be induced by hypoxia or glucose deprivation and is regulated by AMPKalpha
Q8BGD5
ENGINEERING
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
C304A
-
reduced expression in COS-7 cell, reduced activity
C304W
-
reduced expression in COS-7 cell, reduced activity
C305A
-
site-directed mutagenesis, inactive mutant
C305A
-
5% of wild-type activity in mitochondrial fraction, 30% of wild-type expression in COS-7 cell
C305D
-
73% of wild-type activity in mitochondrial fraction (COS-7 cell), 81% of wild-type expression in COS-7 cell
C305E
-
50% of wild-type expression in COS-7 cell
C305F
-
about 20% of wild-type expression in COS-7 cell
C305G
-
about 5% of wild-type expression in COS-7 cell
C305H
-
38% of wild-type activity in mitochondrial fraction in COS-7 cell
C305I
-
4% of wild-type activity in mitochondrial fraction in COS-7 cell
C305K
-
about 25% of wild-type expression in COS-7 cell
C305L
-
about 20% of wild-type expression in COS-7 cell
C305M
-
about 20% of wild-type expression in COS-7 cell
C305N
-
about 10% of wild-type expression in COS-7 cell
C305P
-
about 20% of wild-type expression in COS-7 cell
C305Q
-
about 30% of wild-type expression in COS-7 cell
C305R
-
about 20% of wild-type expression in COS-7 cell
C305S
-
about 20% of wild-type expression in COS-7 cell
C305T
-
about 10% of wild-type expression in COS-7 cell
C305V
-
about 25% 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
C305Y
-
about 20% 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
D17E
-
pig protein: Glu in this position
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
DELTA766-772
-
activity of the mutant is similar to wild-type enzyme
DELTA769-772
-
activity of the mutant is similar to wild-type enzyme
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
-
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
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
E531K
-
naturally occuring mutation
F352C
-
naturally occuring mutation
F352C/V368I
P23786
double mutant with naturally occuring mutations
F352C/V368I/V605L
P23786
triple mutant with naturally occuring mutations
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
-
naturally occuring mutation
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
L264A
-
60.4% of the wild-type activity
L764R
-
16.3% of the wild-type activity
L764R
-
used as reference mutation, negligible activity
L764V
-
as active as the wild-type enzyme
M593S
-
site-directed mutagenesis, the mutant is insensitive to malonyl-CoA
P479L
-
naturally occuring mutation, reduced enzyme activity
P504L
P23786
naturally occuring mutation
P504L/V605L
P23786
double mutant with naturally occuring mutations
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
-
natural missense mutation of CPT II, enzyme deficiency leads to myopathic syndroms, metabolic characterization, e.g. insulin resistance, increased content of muscle lipidsreduced lipolysis
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
P23786
naturally occuring mutation
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
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
-
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
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
-
site-directed mutagenesis, loss of activity
W391A
P32198
mutation alters secondary structure, leading to decreased binding affinity for long chain fatty acid-CoA, and almost completely abolishes enzymic activity
W452A
-
site-directed mutagenesis, loss of activity
W452A
P32198
mutation alters secondary structure, leading to decreased binding affinity for long chain fatty acid-CoA, and almost completely abolishes enzymic activity
M647V
P23786
naturally occuring mutation
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
-
pig-human chimeras
V605L
P23786
naturally occuring mutation
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, Q8SP17
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
M593S
-
malonyl-CoA-insensitive mutant
additional information
-
CPT I mutant with deletion of Arg395 show no activity
additional information
P32198
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
E17D
-
human protein: Asp in this position
additional information
-
deletion of residues 1-18, and deletion of residues 1-28, human-pig chimeras
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 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
LITERATURE
medicine
P23786, P50416
treatment of CPT2 deficiency is based upon avoidance of fasting and/or exercise, a low fat diet enriched with medium chain triglycerides and carnitine
medicine
-
enzyme inhibitors are used to shift the heart's reliance away from fatty acid oxidation to glucose as energy source to increase cardiac efficiency, overview
medicine
Q8TCG5
isoform CPT1C expression is frequently up-regulated in human lung tumors. Tumor cells constitutively expressing CPT1C show increased fatty acid oxidation, ATP production, and resistance to glucose deprivation or hypoxia. Conversely, cancer cells lacking CPT1C produce less ATP and are more sensitive to metabolic stress. CPT1Cdepletion via siRNA suppresses xenograft tumor growth and metformin responsiveness in vivo. CPT1C can be induced by hypoxia or glucose deprivation and is regulated by AMPKalpha
medicine
-
hypertrophied myocardium displays a significant shift in the relative isoform distribution of CPT1 isoforms, L-CPT1 expression dramatically increases relative to M-CPT1 expression
medicine
-
the data suggest that consuming a high-fat diet or inhibiting CPT-I do not result in cardiac hypertrophy or cardiac dysfunction in normal rats
pharmacology
-
CPT I, model enzyme for studies of fatty acid-induced apoptosis in cancer therapy
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
synthesis
Q63704
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