Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4,8-dimethylnonanoyl-CoA + L-carnitine
?
-
-
-
?
4,8-dimethylnonanoyl-CoA + L-carnitine
CoA + 4,8-dimethylnonanoyl-L-carnitine
-
-
-
?
acetyl-CoA + L-carnitine
CoA + L-acetylcarnitine
-
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
arachidoyl-CoA + L-carnitine
CoA + L-arachidoylcarnitine
-
-
-
-
?
butyryl-CoA + L-carnitine
CoA + L-butyrylcarnitine
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
docosanhexaenoyl-CoA + L-carnitine
CoA + L-docosanhexaenoylcarnitine
-
-
-
-
?
dodecanoyl-CoA + L-carnitine
CoA + L-dodecanoylcarnitine
-
-
-
?
erucoyl-CoA + L-carnitine
CoA + L-erucoylcarnitine
-
-
-
-
?
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
linoleoyl-CoA + L-carnitine
CoA + L-linoleoylcarnitine
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
oleoyl-CoA + L-carnitine
CoA + L-oleoylcarnitine
palmitoleoyl-CoA + L-carnitine
CoA + L-palmitoleoylcarnitine
-
activity is 47% higher than with palmitoyl-CoA
-
-
?
palmitoyl-CoA + DL-carnitine
CoA + DL-palmitoylcarnitine
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
palmitoyl-CoA + L-carnitine
L-palmitoylcarnitine + CoA
-
forward reaction by CPT I and reverse reaction by CPT II
-
r
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
trans-2-hexadecenoyl-CoA + L-carnitine
CoA + trans-2-hexadecenoyl-L-carnitine
-
-
-
?
additional information
?
-
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
reverse reaction with palmitoylcarnitine, reverse reaction: myristoylcarnitine
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity
-
?, r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
effect of octylglucoside and Triton X-100 on specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity
reverse reaction: acyl-CoA substrates are C4 to C18 acylcarnitines
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
C4 to C18 acyl-CoAs
reverse reaction: acyl-CoA substrates are C4 to C18 acylcarnitines
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I activity is involved in cardiac mitochondrial beta-oxidation flux control
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
preference for desaturated long-chain acyl CoAs
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
C4 to C18 acyl-CoAs
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
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
-
overview: activity towards long-chain polyunsaturated fatty acids and their CoA esters
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT II requires preincubation with CoA-SH for manifestation of catalytic activity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
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
-
CPT I unlike CPT II requires membrane integrity for catalytic function
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
activity with different substrates of wild-type CPT I with and without gamma-linoleic acid treatment
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I activity is involved in cardiac mitochondrial beta-oxidation flux control
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme is involved in apoptosis induction
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I is the rate-limiting enzyme in beta-oxidation of long-chain fatty acids
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
substrate specificity at early developmental stages in skeletal muscle
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
Valanga nigricornis
-
-
-
?
butyryl-CoA + L-carnitine
CoA + L-butyrylcarnitine
-
-
-
-
?
butyryl-CoA + L-carnitine
CoA + L-butyrylcarnitine
-
-
-
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
-
-
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
-
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
-
-
r
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
best substrate
-
r
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
-
-
r
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
-
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
best substrate
-
?
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
-
-
-
?
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
-
-
-
-
?
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
-
-
-
r
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
-
-
-
r
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
-
-
-
-
?
L-carnitine + palmitoyl-CoA
L-palmitoylcarnitine + CoA
-
-
-
-
?
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
-
-
-
-
?
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
-
best substrate
-
r
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
-
-
-
-
?
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
-
-
-
r
lauroyl-CoA + L-carnitine
CoA + L-lauroylcarnitine
-
-
-
?
linoleoyl-CoA + L-carnitine
CoA + L-linoleoylcarnitine
-
-
-
-
?
linoleoyl-CoA + L-carnitine
CoA + L-linoleoylcarnitine
-
preference for
-
r
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
-
-
-
?
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
-
-
-
?
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
-
best substrate
-
-
?
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
-
-
-
r
myristoyl-CoA + L-carnitine
CoA + L-myristoylcarnitine
-
-
-
?
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
-
-
-
-
?
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
-
-
-
?
oleoyl-CoA + L-carnitine
CoA + L-oleoylcarnitine
-
-
-
-
?
oleoyl-CoA + L-carnitine
CoA + L-oleoylcarnitine
-
activity is 264% higher than with stearoyl-CoA
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
best substrate
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
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
-
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
-
enzyme inhibition reduces hepatic glucose production and plasma lipids in non-insulin-dependent diabetes mellitus, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
regulation, mechanism, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
the enzyme is important in mitochondrial fatty acid beta-oxidation, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
the enzyme is the main regulatory enzyme involved in fatty acid oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
deuterium-labeled L-carnitine substrate
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
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
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
regulation, mechanism, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
the enzyme is the main regulatory enzyme involved in fatty acid oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
deuterium-labeled L-carnitine substrate
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
regulation, mechanism, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
486309, 486551, 486558, 486560, 486562, 486568, 486569, 486570, 486573, 486574, 486580, 486582, 486589, 486591, 673216, 675740, 686125, 686180, 687793, 688449, 688981, 735458, 736793 -
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
r
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
chimeric L-CPT I with exchanged C-terminals between pig and rat enzymes
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
the enzyme is the main regulatory enzyme involved in fatty acid oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
deuterium-labeled L-carnitine substrate
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
chimeric L-CPT I with exchanged C-terminals between pig and rat enzymes
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
Valanga nigricornis
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
-
-
-
-
?
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
-
-
-
-
?
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
-
-
-
-
r
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
-
-
-
?
stearoyl-CoA + L-carnitine
CoA + L-stearoylcarnitine
-
-
-
-
?
additional information
?
-
-
participates in fatty acyl group transport into mitochondria
-
-
?
additional information
?
-
-
participates in fatty acyl group transport into mitochondria
-
-
?
additional information
?
-
-
responsible for transferase activity on the outer side of the inner mitochondrial membrane
-
-
?
additional information
?
-
-
CPT1-A defificiency presents as recurrent attacks of fasting hypoketotic hypoglycemia
-
-
?
additional information
?
-
CPT1-A defificiency presents as recurrent attacks of fasting hypoketotic hypoglycemia
-
-
?
additional information
?
-
CPT1-A defificiency presents as recurrent attacks of fasting hypoketotic hypoglycemia
-
-
?
additional information
?
-
-
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
?
-
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
?
-
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
?
-
-
CPT2 deficiency and glutaric aciduria type 2 are related
-
-
?
additional information
?
-
-
the enzyme is rate-limiting in the mitochondrial fatty axid oxidation pathway, physiologic regulation, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme is inactive with short-chain acyl-CoAs and intermediates of the branched-chain amino acid oxidation pathway
-
-
?
additional information
?
-
-
the enzyme is inactive with short-chain acyl-CoAs and intermediates of the branched-chain amino acid oxidation pathway
-
-
?
additional information
?
-
no activity with 2,6-dimethylheptanoyl-CoA
-
-
?
additional information
?
-
-
no activity with 2,6-dimethylheptanoyl-CoA
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
isozyme CPT1c is inert
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
palmitoyl-CoA + L-carnitine
L-palmitoylcarnitine + CoA
-
forward reaction by CPT I and reverse reaction by CPT II
-
r
additional information
?
-
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I activity is involved in cardiac mitochondrial beta-oxidation flux control
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I activity is involved in cardiac mitochondrial beta-oxidation flux control
-
r
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme is involved in apoptosis induction
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I is the rate-limiting enzyme in beta-oxidation of long-chain fatty acids
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
enzyme has a key function in regulation of fatty acid beta-oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
CPT I, involved in regulation of fatty acid oxidation
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
-
-
-
?
acyl-CoA + L-carnitine
CoA + L-acylcarnitine
Valanga nigricornis
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
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
-
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
-
enzyme inhibition reduces hepatic glucose production and plasma lipids in non-insulin-dependent diabetes mellitus, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
regulation, mechanism, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
the enzyme is important in mitochondrial fatty acid beta-oxidation, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
the enzyme is the main regulatory enzyme involved in fatty acid oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
regulation, mechanism, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
the enzyme is the main regulatory enzyme involved in fatty acid oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
regulation, mechanism, overview
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
the enzyme is the main regulatory enzyme involved in fatty acid oxidation
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
-
?
palmitoyl-CoA + L-carnitine
CoA + L-palmitoylcarnitine
-
-
-
?
additional information
?
-
-
participates in fatty acyl group transport into mitochondria
-
-
?
additional information
?
-
-
participates in fatty acyl group transport into mitochondria
-
-
?
additional information
?
-
-
responsible for transferase activity on the outer side of the inner mitochondrial membrane
-
-
?
additional information
?
-
-
CPT1-A defificiency presents as recurrent attacks of fasting hypoketotic hypoglycemia
-
-
?
additional information
?
-
CPT1-A defificiency presents as recurrent attacks of fasting hypoketotic hypoglycemia
-
-
?
additional information
?
-
CPT1-A defificiency presents as recurrent attacks of fasting hypoketotic hypoglycemia
-
-
?
additional information
?
-
-
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
?
-
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
?
-
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
?
-
-
CPT2 deficiency and glutaric aciduria type 2 are related
-
-
?
additional information
?
-
-
the enzyme is rate-limiting in the mitochondrial fatty axid oxidation pathway, physiologic regulation, overview
-
-
?
additional information
?
-
the enzyme is inactive with short-chain acyl-CoAs and intermediates of the branched-chain amino acid oxidation pathway
-
-
?
additional information
?
-
-
the enzyme is inactive with short-chain acyl-CoAs and intermediates of the branched-chain amino acid oxidation pathway
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11-trimethylamino-undecanoyl-DL-carnitine
-
-
2-[5(4-chlorophenyl)pentyl]-oxirane-2-carboxyl-CoA
-
-
4-hydroxy phenylglyoxylate
-
CPT I, greatly reduced inhibition of protease treated enzyme
arachidonic acid
-
the enzymatic activity significantly declines by treatment with 0.1 mM for 1 h
Bile acids
-
e.g. in cholestatic rats
cardiolipin
-
inhibits conversion of palmitoylcarnitine to palmitoyl-CoA, stimulates palmitoylcarnitine formation
carnitine
-
CPT I, slightly
chenodeoxycholic acid
-
competitive to carnitine
CoA esters of certain oxirane carboxylic acids
-
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
gamma-linolenic acid
-
inhibits CPT I in vivo and reduces malonyl-CoA sensitivity, decreases affinity for 16:0 acyl-CoA substrate
H2O2
-
the enzymatic activity significantly and reversibly declines by 1 mM H2O2
Hemipalmitoylcarnitinium bromide
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
-
a physiological CPT1 inhibitor
nagarse
-
mitochondria, malonyl-CoA protects
-
Palmitoylcholine
-
competitive in the forward reaction to both substrates
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
rotenone
-
the enzymatic activity significantly declines by treatment with 0.001 mM for 2 h
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
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
competitive
tumor necrosis factor-alpha
-
the enzymatic activity significantly declines by treatment with 25 ng/ml for 30 min
-
2-bromopalmitoyl-CoA
-
irreversible
2-bromopalmitoyl-CoA
-
with addition of carnitine
2-bromopalmitoyl-CoA
-
no inhibition
2-bromopalmitoyl-CoA
-
irreversible; with addition of carnitine
acetyl-CoA
-
-
acetyl-CoA
-
CPT I, inhibition is not affected by proteinase treatment
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
CoA
-
-
CoA
-
CPT I, inhibition is not affected by proteinase treatment
CoA esters of certain oxirane carboxylic acids
-
irreversible, CPT I but not CPT II
-
CoA esters of certain oxirane carboxylic acids
-
irreversible, CPT I but not CPT II
-
CoA esters of certain oxirane carboxylic acids
-
irreversible, CPT I but not CPT II
-
CoA esters of certain oxirane carboxylic acids
-
irreversible, CPT I but not CPT II
-
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
high concentrations of etomoxir (200 microM) have an off-target effect of inhibiting complex I of the electron transport chain. When fatty acid oxidation is reduced approximately 90% by low concentrations of etomoxir, the proliferation rate of various cancer cells is unaffected
etomoxir
regional differences in brain fatty acid oxidation may be blocked by irreversible CPT1a inhibitor etomoxir; regional differences in brain fatty acid oxidation may be blocked by irreversible CPT1a inhibitor etomoxir
etomoxiryl-CoA
-
IC50: 0.00121 mM in INS(832/13) cells, IC50: 0.00287 in L6E9 myotubes
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
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
-
inhibition of CPT II not CPT I
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
malonyl-CoA
-
no inhibition
malonyl-CoA
-
inhibition of soluble peroxisomal form, no inhibition of enzyme from inner mitochondrial membrane
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
-
Triton X-100 protects
malonyl-CoA
-
no inhibition
malonyl-CoA
-
CPT I; CPT II not inhibited; reversible inhibition
malonyl-CoA
-
CPT II not inhibited; CPT I, native and reconstituted in phospholipid micelles
malonyl-CoA
-
CPT I; isoforms L-CPT I and M-CPT I
malonyl-CoA
-
CPT I; CPT II not inhibited; regulatory role in vivo
malonyl-CoA
-
inhibits CPT I not CPT II; isoforms L-CPT I and M-CPT I
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
-
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
-
CPT I; CPT II not inhibited; reversible inhibition
malonyl-CoA
-
CPT I; isoforms L-CPT I and M-CPT I
malonyl-CoA
-
allosteric inhibition
malonyl-CoA
-
CPT I; regulatory role in vivo
malonyl-CoA
IC50 for wild-type L-CPT-1 is 0.0298 mM; IC50 for wild-type M-CPT-1 is 0.010 mM
malonyl-CoA
-
inhibits CPT I not CPT II; regulatory role in vivo
malonyl-CoA
-
CPT I; CPT II not inhibited; reversible inhibition
malonyl-CoA
-
similar inhibition of wild-type CPT I and mutants A381D and H473A
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
-
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; regulatory role in vivo
malonyl-CoA
-
differences in sensitivity of hepatic and heart enzyme
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
-
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 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
-
L-CPT I, recombinant enzyme from Saccharomyces cerevisiae is inhibited only in intact mitochondria, not as solubilized enzyme
malonyl-CoA
-
overview: recombinant chimeric proteins of 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
-
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
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
-
allosteric inhibition
malonyl-CoA
-
has a regulatory role in vivo
malonyl-CoA
-
CPT I; CPT I, inhibition depends on age; inhibition is temperature dependent; regulatory role in vivo
malonyl-CoA
-
sensitivity to inhibition of deletion and chimeric L-CPT I mutants
malonyl-CoA
complete inhibition at 0.05 mM; complete inhibition at 0.05 mM; complete inhibition at 0.05 mM; complete inhibition at 0.05 mM
methylmalonyl-CoA
-
inhibits sheep liver CPT I, no inhibition of rat liver and guinea-pig liver mitochondrial CPT I
methylmalonyl-CoA
-
CPT I
methylmalonyl-CoA
-
inhibits sheep liver CPT I, no inhibition of rat liver and guinea-pig liver mitochondrial CPT I
methylmalonyl-CoA
-
inhibits sheep liver CPT I, no inhibition of rat liver and guinea-pig liver mitochondrial CPT I
methylmalonyl-CoA
-
partial proteolysis of CPT I slightly diminishes the inhibitory effect
octyl glucoside
-
with octanoyl-CoA as substrate, competitive
octyl glucoside
-
complete loss of CPT I activity, no loss of CPT II activity
octyl glucoside
-
complete loss of CPT I activity, no loss of CPT II activity
octyl glucoside
-
complete loss of CPT I activity, no loss of CPT II activity
octyl glucoside
-
only CPTo
octyl glucoside
-
complete loss of CPT I activity, no loss of CPT II activity
oxfenicine
-
-
palmitoyl-CoA
thermally destabilizes bith wild-type and mutant S113L
palmitoyl-CoA
-
product inhibition, reverse reaction
palmitoyl-CoA
-
substrate inhibition
palmitoyl-CoA
-
CPT I, slightly
tetradecylglycidyl-CoA
-
CPTo
tetradecylglycidyl-CoA
-
and analogues, irreversible
Triton X-100
-
mutant CPT
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
Triton X-100
-
complete loss of CPT I activity, no loss of CPT II activity
Triton X-100
-
complete loss of CPT I activity, no loss of CPT II activity
Triton X-100
-
complete loss of CPT I activity, no loss of CPT II activity
Trypsin
-
peroxisomal and mitochondrial isozymes
-
Trypsin
-
mitochondria, malonyl-CoA protects
-
Tween 20
-
-
Tween 20
-
only CPTo at 2% and above
additional information
-
different sites of inhibition of carnitine palmitoyltransferase by malonyl-CoA, acetyl-CoA and CoA
-
additional information
-
physiological role of malonyl-CoA in the heart
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0051 - 0.03
butyryl-CoA
0.0009 - 0.017
decanoyl-CoA
0.0018 - 0.152
hexanoyl-CoA
1.139
L-octanoylcarnitine
-
-
0.123 - 0.14
L-palmitoylcarnitine
0.011 - 0.013
lauroyl-CoA
0.0012 - 0.031
myristoyl-CoA
0.0085 - 0.023
octanoyl-CoA
0.0008 - 25.35
palmitoyl-CoA
0.0017 - 0.018
stearoyl-CoA
0.0081
trans-2-hexadecenoyl-CoA
pH 7.4, 37°C
additional information
additional information
-
0.0051
butyryl-CoA
-
-
0.0009
decanoyl-CoA
-
-
0.0018
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
0.056
L-carnitine
-
30°C, 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
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
V368I mutant protein, COS-7 cell lysate
0.135
L-carnitine
-
30°C, recombinant wildtype isozyme CPT1A
0.14
L-carnitine
M647V mutant protein, COS-7 cell lysate
0.147
L-carnitine
-
3 wk old pig, liver
0.147 - 0.28
L-carnitine
-
liver CPT 1
0.17
L-carnitine
-
peroxisomal soluble enzyme
0.179
L-carnitine
-
1 wk old pig, liver
0.185
L-carnitine
-
with C16-CoA
0.197
L-carnitine
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
wild-type L-CPT 1
0.218
L-carnitine
-
adult pig, liver
0.228
L-carnitine
-
1 wk old pig, skeletal muscle
0.228 - 0.46
L-carnitine
-
skeletal muscle CPT 1
0.24
L-carnitine
-
isoform CPT1c, at pH 7.4 and 30°C
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
0.28
L-carnitine
-
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
P504L mutant protein, COS-7 cell lysate
0.35
L-carnitine
V605L mutant protein, COS-7 cell lysate
0.36
L-carnitine
F352C mutant protein, COS-7 cell lysate
0.37
L-carnitine
F352C/V368I mutant protein, COS-7 cell lysate
0.37
L-carnitine
wild-type protein and P504L/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.38
L-carnitine
P504L/V605L mutant protein, COS-7 cell lysate
0.381
L-carnitine
-
newborn pig, skeletal muscle
0.424 - 0.534
L-carnitine
-
pH 7.2, 30°C, skeletal muscle CPT 1
0.431 - 0.527
L-carnitine
-
pH 7.2, 30°C, liver CPT 1
0.46
L-carnitine
-
5 wk old pig, skeletal muscle
0.4893
L-carnitine
-
enzyme from 3 month old animal, at 25°C, pH not specified in the publication
0.5
L-carnitine
-
isoform L-CPT I, with 2[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylic acid
0.52
L-carnitine
F352C/V368I/V605L mutant protein, COS-7 cell lysate
0.53
L-carnitine
wild-type protein and F352C/V368I/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.56
L-carnitine
wild-type M-CPT 1
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
0.6697
L-carnitine
-
enzyme at hatching, at 25°C, pH not specified in the publication
0.679
L-carnitine
wild-type enzyme
0.683
L-carnitine
-
wild-type protein, mitochondrial preparation
0.69
L-carnitine
enzyme from spleen, at pH 8.0 and 37°C
0.706
L-carnitine
-
mutant enzyme E3A/V19A/L23A/S24A
0.7695
L-carnitine
-
D17E mutant protein, mitochondrial preparation
0.785
L-carnitine
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, 37°C, recombinant wild-type enzyme
0.913
L-carnitine
-
wild-type enzyme
0.92
L-carnitine
-
pH 8.0, 37°C, recombinant revertant A305C
0.93
L-carnitine
enzyme from muscle, at pH 8.0 and 37°C
0.95
L-carnitine
-
recombinant CPT II
0.968
L-carnitine
-
mutant enzyme H5A
0.98
L-carnitine
enzyme from heart, at pH 8.0 and 37°C
1.152
L-carnitine
-
enzyme from 6 month old animal, at 25°C, pH not specified in the publication
1.16
L-carnitine
enzyme from liver, at pH 8.0 and 37°C
1.201
L-carnitine
-
enzyme from 1 month old animal, at 25°C, pH not specified in the publication
1.34
L-carnitine
enzyme from intestine, at pH 8.0 and 37°C
1.38
L-carnitine
25°C, pH not specified in the publication
1.588
L-carnitine
mutant enzyme L764R
2.8
L-carnitine
-
inner mitochondrial membrane
4.44
L-carnitine
-
isoform CPT1b, at pH 7.4 and 30°C
11.1
L-carnitine
-
isoform CPT1a, at pH 7.4 and 30°C
58.53
L-carnitine
-
microsomes of PC-12 cells overexpressing CPT1c
127
L-carnitine
-
microsomes, PC-12 cell, CPT1a
0.123
L-palmitoylcarnitine
-
-
0.14
L-palmitoylcarnitine
-
-
0.011
lauroyl-CoA
-
-
0.0012
myristoyl-CoA
-
-
0.0085
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
wild-type
0.0049
palmitoyl-CoA
-
recombinant wild-type CPT I
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
-
30°C, recombinant CPT1A mutant R243T
0.0071
palmitoyl-CoA
pH 7.4, 37°C
0.0074
palmitoyl-CoA
mutant M593S
0.0078
palmitoyl-CoA
-
mutant enzyme E3A/V19A/L23A/S24A
0.011
palmitoyl-CoA
-
CPT I
0.0127
palmitoyl-CoA
enzyme from intestine, at pH 8.0 and 37°C
0.0137
palmitoyl-CoA
enzyme from heart, at pH 8.0 and 37°C
0.014
palmitoyl-CoA
enzyme from muscle, at pH 8.0 and 37°C
0.0151
palmitoyl-CoA
mutant A478G
0.0159
palmitoyl-CoA
enzyme from liver, at pH 8.0 and 37°C
0.0167
palmitoyl-CoA
enzyme from spleen, at pH 8.0 and 37°C
0.017
palmitoyl-CoA
-
CPT I after gamma-linoleic acid treatment
0.0243
palmitoyl-CoA
mutant C608A
0.028
palmitoyl-CoA
-
purified recombinant L-CPT I, reconstituted in liposomes
0.03
palmitoyl-CoA
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
wild-type L-CPT1
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
0.0622
palmitoyl-CoA
mutant enzyme E590A
0.066
palmitoyl-CoA
-
pH 8.0, 37°C, recombinant revertant A305C
0.0676
palmitoyl-CoA
wild-type M-CPT1
0.0679
palmitoyl-CoA
-
wild-type enzyme
0.073
palmitoyl-CoA
-
pH 8.0, 37°C, recombinant wild-type enzyme
0.0744
palmitoyl-CoA
mutant enzyme E590Q
0.079
palmitoyl-CoA
-
mitochondria isolated from newborn pig, pH 7.2, 30°C
0.0823
palmitoyl-CoA
-
mutant enzyme E3A
0.083
palmitoyl-CoA
pH 7.0, recombinant enzyme
0.142
palmitoyl-CoA
-
mitochondria isolated from 24-h-old, fed pig, pH 7.2, 30°C
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, 30°C
0.4
palmitoyl-CoA
-
30°C, recombinant wildtype isozyme CPT1A
0.461
palmitoyl-CoA
-
mitochondria isolated from adult pig, pH 7.2, 30°C
4.9
palmitoyl-CoA
-
microsomes, PC-12 cell, CPT1a
25.35
palmitoyl-CoA
-
microsomes of PC-12 cells overexpressing CPT1c
0.0017
stearoyl-CoA
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
Km values of deletion and chimeric L-CPT I mutants
-
additional information
additional information
-
Km values of deletion and chimeric L-CPT I mutants
-
additional information
additional information
-
influence of detergent on Km value
-
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
-
effects of malonyl-CoA on kinetics
-
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
-
overview: Km values of recombinant chimeric proteins of L-CPT I and M-CPT I
-
additional information
additional information
-
Km values for carnitine with different acyl-CoA substrates
-
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
-
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 cats, overview
-
additional information
additional information
-
Michaelis-Menten kinetics at different developmental stages of pigs, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000015 - 0.0041
etomoxiryl-CoA
0.00003 - 0.319
malonyl-CoA
0.00004
C75-CoA
Rattus norvegicus
-
IC50: 0.00004 mM in muscle
0.00024
C75-CoA
Rattus norvegicus
-
IC50: 0.00024 mM recombinant isozyme L-CPT I
0.00025
C75-CoA
Homo sapiens
-
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
Rattus norvegicus
-
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
Homo sapiens
-
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
Rattus norvegicus
-
potent competitive inhibition, IC50: 0.0007 mM in liver
0.000015
etomoxiryl-CoA
Rattus norvegicus
-
IC50: 0.000015 mM in muscle
0.00025
etomoxiryl-CoA
Rattus norvegicus
-
IC50: 0.00025 mM in liver
0.00121 - 0.00287
etomoxiryl-CoA
Homo sapiens
-
IC50: 0.00121 mM in INS(832/13) cells, IC50: 0.00287 in L6E9 myotubes
0.0031
etomoxiryl-CoA
Rattus norvegicus
-
IC50: 0.0031 mM recombinant isozyme M-CPT I
0.0041
etomoxiryl-CoA
Rattus norvegicus
-
IC50: 0.0041 mM recombinant isozyme L-CPT I
0.00003
malonyl-CoA
Homo sapiens
-
-
0.00007
malonyl-CoA
Homo sapiens
-
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
Oncorhynchus mykiss
-
mitochondrial isolate from liver, high polyunsaturated fat diet
0.000079
malonyl-CoA
Oncorhynchus mykiss
-
CPT I, liver
0.000096
malonyl-CoA
Homo sapiens
-
wild-type protein, 1 mM carnitine, mitochondrial preparation
0.00011
malonyl-CoA
Oncorhynchus mykiss
-
mitochondrial isolate from liver, high saturated fat diet
0.000117
malonyl-CoA
Homo sapiens
-
wild-type protein, 0.683 mM carnitine, mitochondrial preparation
0.00012
malonyl-CoA
Oncorhynchus mykiss
-
mitochondrial isolate from liver, control diet
0.00019
malonyl-CoA
Homo sapiens
-
chimeric protein: residues 1-50 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.00019
malonyl-CoA
Sus scrofa
-
mitochondria isolated from newborn pig, pH 7.2, 30°C
0.00021
malonyl-CoA
Sus scrofa
-
mitochondria isolated from adult pig, pH 7.2, 30°C
0.000246
malonyl-CoA
Homo sapiens
-
D17E mutant protein, 0.770 mM carnitine, mitochondrial preparation
0.00026
malonyl-CoA
Sus scrofa
-
mitochondria isolated from 24-h-old, fed pig, pH 7.2, 30°C
0.000279
malonyl-CoA
Homo sapiens
-
D17E mutant protein, 1 mM carnitine, mitochondrial preparation
0.000284
malonyl-CoA
Sus scrofa
-
E17D mutant protein, 0.606 mM carnitine, mitochondrial preparation
0.000297
malonyl-CoA
Sus scrofa
-
E17D mutant protein, 1 mM carnitine, mitochondrial preparation
0.000325
malonyl-CoA
Homo sapiens
-
chimeric protein: residues 1-128 of pig enzyme recombined with human enzyme, mitochondrial preparation
0.00035
malonyl-CoA
Oncorhynchus mykiss
-
mitochondrial isolate from red muscle, high polyunsaturated fat diet
0.000359
malonyl-CoA
Sus scrofa
-
chimeric protein: residues 1-128 of human enzyme recombined with pig enzyme, mitochondrial preparation
0.00037
malonyl-CoA
Oncorhynchus mykiss
-
CPT I, white muscle
0.0004
malonyl-CoA
Oncorhynchus mykiss
-
CPT I, heart
0.000457
malonyl-CoA
Sus scrofa
-
chimeric protein: residues 1-50 of human enzyme recombined with pig enzyme, mitochondrial preparation
0.0005
malonyl-CoA
Homo sapiens
-
IC50: 0.0005 mM for the recombinant wild-type enzyme
0.00052
malonyl-CoA
Homo sapiens
-
IC50: 0.00052 mM for the recombinant revertant A305C, IC50 values of recombinant mutant isozymes M-CPT I overview
0.00053
malonyl-CoA
Sus scrofa
-
mitochondria isolated from 24-h-old, fasted pig, pH 7.2, 30°C
0.00055
malonyl-CoA
Oncorhynchus mykiss
-
CPT I, red muscle
0.00055
malonyl-CoA
Sus scrofa
-
wild-type protein, 0.198 mM carnitine, mitochondrial preparation
0.00074
malonyl-CoA
Drosophila melanogaster
-
at 0.035 mM palmitoyl-CoA
0.00076
malonyl-CoA
Drosophila melanogaster
-
at 0.035 mM palmitoyl-CoA
0.000804
malonyl-CoA
Sus scrofa
-
wild-type protein, 1 mM carnitine, mitochondrial preparation
0.000906
malonyl-CoA
Sus scrofa
IC50: 906 nM
0.00101
malonyl-CoA
Drosophila melanogaster
-
at 0.07 mM palmitoyl-CoA
0.00119
malonyl-CoA
Oncorhynchus mykiss
-
mitochondrial isolate from red muscle, control diet
0.00183
malonyl-CoA
Oncorhynchus mykiss
-
mitochondrial isolate from red muscle, high saturated fat diet
0.00232
malonyl-CoA
Drosophila melanogaster
-
at 0.07 mM palmitoyl-CoA
0.00339
malonyl-CoA
Rattus norvegicus
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
Homo sapiens
-
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
Rattus norvegicus
IC50 0.0087 mM for mutant enzyme N464D
0.01
malonyl-CoA
Ovis aries
IC50 for wild-type M-CPT-1 is 0.010 mM
0.0123
malonyl-CoA
Rattus norvegicus
IC50: 0.0123 for wild-type enzyme
0.015
malonyl-CoA
Rattus norvegicus
IC50 0.015 mM for mutant enzyme T314S
0.0252
malonyl-CoA
Macrobrachium borellii
-
10 min pre-incubation with malonyl-CoA
0.0275
malonyl-CoA
Rattus norvegicus
IC50 0.0275 mM for mutant enzyme C608A
0.0298
malonyl-CoA
Ovis aries
IC50 for wild-type L-CPT-1 is 0.0298 mM
0.03556
malonyl-CoA
Sus scrofa
-
protein with deletion of residue 1-18, mitochondrial preparation
0.03919
malonyl-CoA
Sus scrofa
-
protein with deletion of residue 1-28, mitochondrial preparation
0.0395
malonyl-CoA
Rattus norvegicus
IC50 0.0395 mM for mutant enzyme A478G
0.0768
malonyl-CoA
Rattus norvegicus
-
mitochondrial isolate
0.1058
malonyl-CoA
Macrobrachium borellii
-
without pre-incubation with malonyl-CoA
0.1103
malonyl-CoA
Rattus norvegicus
-
mitochondrial isolate, after incubation with protein kinase A
0.155
malonyl-CoA
Rattus norvegicus
IC50 0.155 mM for mutant enzyme M593A
0.319
malonyl-CoA
Rattus norvegicus
IC50 0.319 mM for mutant enzyme M593 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00018
mutant enzyme F352C/V368I, at 30°C, pH not specified in the publication
0.00027
mutant enzyme V368I, at 30°C, pH not specified in the publication
0.00028
wild type enzyme, at 30°C, pH not specified in the publication
0.00035
-
transfected HEK-293T cell
0.0006
hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.00062
F352C/V368I/V605L mutant protein, COS-7 cell lysate
0.00063
wild-type protein and F352C/V368I/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.00071
P504L/V605L mutant protein, COS-7 cell lysate
0.00073
F352C mutant protein, COS-7 cell lysate
0.00076
P504L mutant protein, COS-7 cell lysate
0.00078
V605L mutant protein, COS-7 cell lysate
0.0008
hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.00081
M647V mutant protein, COS-7 cell lysate
0.00085
V368I mutant protein, COS-7 cell lysate
0.00087
wild-type protein, COS-7 cell lysate
0.0014
-
CPT I after gamma-linoleic acid treatment
0.0017
hepatocytes transduced with adenovirus encoding CPT-1a exposed to exogenous palmitate, measurement of CPT-1 activity at the end of the incubation period
0.0019
hepatocytes transduced with adenovirus encoding CPT-1a exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.00194
-
transfectecd PC-12 cell
0.002
-
CPT II, red muscle
0.00227
-
mitochondrial fraction, wild-type protein expressed in COS-7 cell
0.00279
-
wild-type protein, mitochondrial preparation
0.0028
-
recombinant revertant A305C
0.0033
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding CPT-2, incubation with palmitate
0.0041
hepatic CPT-1 activity, rats fed standard diet, transduced with adenovirus encoding CPT-1a, incubation with palmitate
0.00416
-
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
0.0047
-
CPT I, heart, plus 50 microM malonyl-CoA
0.0051
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
0.0062
-
cell line 3T3-L1, CPT II, 6 days after differentiation
0.0063
hepatocytes transduced with adenovirus encoding CPT-2 exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.0069
-
mitochondrial fraction of recombinant Pichia pastoris expressing CPT II
0.0078
-
recombinant wild-type L-CPT I
0.0083
-
CPT II, white muscle
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
0.0128
-
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
0.0263
-
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
13.2
-
purified peroxisomal enzyme
33
mutant S113L, pH 7.4, 30°C
39
wild-type, pH 7.4, 30°C
4.65
-
purified mitochondrial enzyme
0.00072
F352C/V368I mutant protein, COS-7 cell lysate
0.00072
wild-type protein and P504L/V605L mutant protein, COS-7 cell lysate (doubly transfected)
0.001
-
-
0.001
hepatocytes transduced with adenovirus encoding beta-galctosidase exposed to exogenous palmitate, measurement of CPT-2 activity at the end of the incubation period
0.0013
-
cell line 3T3-L1, CPT I, 6 days after differentiation
0.0013
-
native L-CPT I in liver mitochondria
0.0021
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
0.0029
-
recombinant wild-type enzyme
0.0029
hepatic CPT-1 activity, rats fed high-fat diet, transduced with adenovirus encoding beta-galctosidase, incubation with palmitate
0.0029
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
0.0036
-
CPT I
0.0036
-
rat primary hepatocytes infected with adenovirus vectors expressing Ad-PGC-1beta
0.0054
-
CPT I, liver, plus 50 microM malonyl-CoA
0.0054
-
CPT I, white muscle, plus 50 microM malonyl-CoA
additional information
-
-
additional information
-
plasma and free carnitine levels and enzyme activity at different developmental stages, overview
additional information
-
-
additional information
-
-
additional information
-
CPT I and II activities in muscle biopsis
additional information
-
activity of mutant enzymes
additional information
-
quantitative expression analysis
additional information
-
quantitative expression analysis
additional information
-
-
additional information
-
-
additional information
-
activities of deletion and chimeric L-CPT I mutants
additional information
-
activity of tissue-specific isozymes L-CPT1 and M-CPT1, overview
additional information
-
activities of deletion and chimeric L-CPT I mutants
additional information
-
activity at early developmental stages in skeletal muscle
additional information
-
plasma and free carnitine levels at different developmental stages of pigs, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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/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/V368I/V605L
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
L764V
as active as the wild-type enzyme
M593S
-
site-directed mutagenesis, the mutant is insensitive to malonyl-CoA
M647V
naturally occuring mutation
P479L
-
naturally occuring mutation, reduced enzyme activity
P504L
naturally occuring mutation
P504L/V605L
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
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
V605L
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
A587S/S588A/M592L/R594L
-
inert isoform CPT1c
C608A
2.2fold increase in IC50 for malonyl-CoA, 2.5fold increase in KM-value for carnitine, 5fold increase in Km-value for palmitoyl-CoA as compared to wild-type enzyme
D454G
-
site-directed mutagenesis, loss of activity
E590A
IC50 for malonyl CoA is 16fold lower than the wild-type value, partial decrease in catalytic activity,1.5fold increase in Km-value for carnitine, 2.9fold decrease in KM-value doe palmitoyl-CoA
E590D
inactive mutant enzyme
E590K
IC50 for malonyl CoA is 13.5fold lower than the wild-type value, partial decrease in catalytic activity
E590Q
IC50 for malonyl CoA is 8.7fold lower than the wild-type value, partial decrease in catalytic activity, 1.3fold increase in Km-value for carnitine, 2fold decrease in KM-value doe palmitoyl-CoA
H473A
-
site-directed mutagenesis, active site mutant, no remaining activity
L484P
-
site-directed mutagenesis, loss of activity
M593A
12.6fold increase in IC50 for malonyl-CoA, 2.3fold increase in KM-value for carnitine, 1.2fold increase in Km-value for palmitoyl-CoA as compared to wild-type enzyme
M593E
18fold increase in IC50 for malonyl-CoA, 1.2fold increase in KM-value for carnitine, 1.3fold decrease in Km-value for palmitoyl-CoA as compared to wild-type enzyme
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
E17D
-
human protein: Asp in this position
C305A
-
site-directed mutagenesis, inactive mutant
C305A
-
5% of wild-type activity in mitochondrial fraction, 30% of wild-type expression in COS-7 cell
E3A
-
57fold increase in IC50 for malonyl-CoA, 1.5fold decrease in KM-value for carnitine, 1.2fold increase in Km-value for palmitoyl-CoA
E3A
-
used as reference mutation, similar activity as the wild-type enzyme, shows high resistance against malonyl-CoA
F352C
-
naturally occuring mutation
F352C
naturally occuring mutation
F352C/V368I
double mutant with naturally occuring mutations
F352C/V368I
the mutant shows thermal instability, reduced residual enzyme activities and a short half-life compared to the wild type enzyme
L764R
16.3% of the wild-type activity
L764R
-
used as reference mutation, negligible activity
S113L
-
natural missense mutation of CPT II, enzyme deficiency leads to myopathic syndroms, metabolic characterization, e.g. insulin resistance, increased content of muscle lipidsreduced lipolysis
S113L
mutant displays an abnormal thermal destabilization at 40°C and 45°C consistent with an increased flexibility at 40°C. Preincubation with L-carnitine and acyl-L-carnitines containing more than 10 carbons in the acyl side-chain stabilizes the mutant
V368I
naturally occuring mutation
V368I
the mutant shows thermal instability, reduced residual enzyme activities and a short half-life compared to the wild type enzyme
M593S
26fold increase in IC50 for malonyl-CoA, KM-value for carnitine is nearly identical to wild-type value, 1.5fold increase in Km-value for palmitoyl-CoA as compared to wild-type enzyme
M593S
-
malonyl-CoA-insensitive mutant
W391A
-
site-directed mutagenesis, loss of activity
W391A
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
mutation alters secondary structure, leading to decreased binding affinity for long chain fatty acid-CoA, and almost completely abolishes enzymic activity
additional information
-
overexpression of CPT I in skeletal muscle in vivo increases fatty acid oxidation, i.e. palmitate oxidation by 28%, and reduces triacylglycerol esterification, overview
additional information
-
screening for mutations in isozymes CPT1 and CPT2 encoding genes, determination of relation between mutations and metabolic disorders, age, onset and prognosis, overview
additional information
-
pig-human chimeras
additional information
-
disruption of the cpt1c gene results in lower body weight and decreased food intake, construction of CPT1c knockout mice, which exhibit decreased rates of fatty acid oxidation, which may contribute to their increased susceptibility to diet-induced obesity, overview
additional information
Q7YQR7
chimaera in which the distinctive N-terminal segmant of ovine m-BPT 1 is replaced with that from rat M-CPT 1. The ovine N-terminal segment influences the kinetics of the enzyme for both its substrates, such that the Km for palmitoyl-CoA is decreased and that for carnitine is increased for the chimera, relative to the parental enzyme M-CPT 1 from Ovis aries
additional information
chimaera in which the distinctive N-terminal segmant of ovine m-BPT 1 is replaced with that from rat M-CPT 1. The ovine N-terminal segment influences the kinetics of the enzyme for both its substrates, such that the Km for palmitoyl-CoA is decreased and that for carnitine is increased for the chimera, relative to the parental enzyme M-CPT 1 from Ovis aries
additional information
-
chimaera in which the distinctive N-terminal segmant of ovine m-BPT 1 is replaced with that from rat M-CPT 1. The ovine N-terminal segment influences the kinetics of the enzyme for both its substrates, such that the Km for palmitoyl-CoA is decreased and that for carnitine is increased for the chimera, relative to the parental enzyme M-CPT 1 from Ovis aries
additional information
-
CPT I mutant with deletion of Arg395 show no activity
additional information
recombinant expression of the cytoplasmic C-terminal region of liver CPTI. The C-terminal 89 residues are sufficient for high affinity binding of long chain fatty acid-CoA and direct interaction with several cytoplasmic long chain fatty acid-CoA binding proteins, leading to enhanced enzymic activity
additional information
-
deletion of residues 1-18, and deletion of residues 1-28, human-pig chimeras
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.