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Information on EC 2.3.1.137 - carnitine O-octanoyltransferase and Organism(s) Rattus norvegicus and UniProt Accession P11466

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IUBMB Comments
Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC 2.3.1.21 (carnitine O-palmitoyltransferase).
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Select one or more organisms in this record:
This record set is specific for:
Rattus norvegicus
UNIPROT: P11466
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
carnitine acyltransferase, Carnitine medium-chain acyltransferase, carnitine octanoyltransferase, COT, CRAT, CrOT, easily solubilized mitochondrial carnitine palmitoyltransferase, medium-chain carnitine acyltransferase, medium-chain/long-chain carnitine acyltransferase, More, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Carnitine medium-chain acyltransferase
-
-
-
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carnitine octanoyltransferase
248
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easily solubilized mitochondrial carnitine palmitoyltransferase
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-
-
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medium-chain/long-chain carnitine acyltransferase
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-
-
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overt mitochondrial carnitine palmitoyltransferase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
show the reaction diagram
acyl-CoA substrate specificity is determined by Gly553, active site structure and substrate positioning modeling
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
-
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SYSTEMATIC NAME
IUBMB Comments
octanoyl-CoA:L-carnitine O-octanoyltransferase
Acts on a range of acyl-CoAs, with optimal activity with C6 or C8 acyl groups. cf. EC 2.3.1.7 (carnitine O-acetyltransferase) and EC 2.3.1.21 (carnitine O-palmitoyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
39369-19-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
show the reaction diagram
3-hydroxy-3-methylglutaryl-CoA + L-carnitine
3-hydroxy-3-methylglutaryl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
3-methylglutaryl-CoA + L-carnitine
3-methylglutaryl-L-carnitine + CoA
show the reaction diagram
-
little capacity to use this substrate
-
-
r
3-methylglutaryl-L-carnitine + CoA
3-methylglutaryl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
acetoacetyl-CoA + L-carnitine
acetoacetyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
acetoacetyl-L-carnitine + CoA
acetoacetyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-carnitine
acetyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
acetyl-CoA + L-carnitine
CoA + L-acetylcarnitine
show the reaction diagram
-
low activity
-
-
?
acetyl-L-carnitine + CoA
acetyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
show the reaction diagram
acyl-L-carnitine + CoA
acyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
beta-hydroxy-beta-methylglutaryl-L-carnitine + CoA
beta-hydroxy-beta-methylglutaryl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
butanoyl-CoA + L-carnitine
CoA + L-butanoylcarnitine
show the reaction diagram
-
-
-
-
?
butyryl-CoA + L-carnitine
butyryl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
butyryl-L-carnitine + CoA
butyryl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
decanoyl-CoA + L-carnitine
CoA + L-decanoylcarnitine
show the reaction diagram
-
best substrate
-
-
?
decanoyl-CoA + L-carnitine
L-decanoyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
decanoyl-L-carnitine + CoA
decanoyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
dodecanoyl-CoA + L-carnitine
CoA + L-dodecanoylcarnitine
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + L-carnitine
L-dodecanoyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
dodecanoyl-L-carnitine + CoA
dodecanoyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
heptanoyl-CoA + L-carnitine
L-heptanoyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
heptanoyl-L-carnitine + CoA
heptanoyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
hexadecanoyl-CoA + L-carnitine
CoA + L-hexadecanoylcarnitine
show the reaction diagram
-
low activity
-
-
?
hexadecanoyl-CoA + L-carnitine
L-hexadecanoyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
hexadecanoyl-L-carnitine + CoA
hexadecanoyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
show the reaction diagram
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
L-hexanoylcarnitine + CoA
hexanoyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
malonyl-CoA + L-carnitine
malonyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
malonyl-L-carnitine + CoA
malonyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
myristoyl-CoA + L-carnitine
myristoyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
myristoyl-L-carnitine + CoA
myristoyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
-
-
-
-
?
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
show the reaction diagram
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-
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r
palmitoyl-CoA + L-carnitine
L-palmitoyl-L-carnitine + CoA
show the reaction diagram
-
-
-
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r
palmitoyl-L-carnitine + CoA
palmitoyl-CoA + L-carnitine
show the reaction diagram
-
-
-
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r
pivaloyl-CoA + L-carnitine
L-pivaloyl-L-carnitine + CoA
show the reaction diagram
-
little capacity to use this substrate
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-
r
pivaloyl-L-carnitine + CoA
pivaloyl-CoA + L-carnitine
show the reaction diagram
-
-
-
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r
propionyl-CoA + L-carnitine
propionyl-L-carnitine + CoA
show the reaction diagram
-
-
-
-
r
propionyl-L-carnitine + CoA
propionyl-CoA + L-carnitine
show the reaction diagram
-
-
-
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r
tetradecanoyl-CoA + L-carnitine
CoA + L-tetradecanoylcarnitine
show the reaction diagram
-
-
-
-
?
valproyl-CoA + L-carnitine
L-valproyl-L-carnitine + CoA
show the reaction diagram
-
little capacity to use this substrate
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r
valproyl-L-carnitine + CoA
valproyl-CoA + L-carnitine
show the reaction diagram
-
-
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r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
show the reaction diagram
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
show the reaction diagram
acyl-L-carnitine + CoA
acyl-CoA + L-carnitine
show the reaction diagram
-
-
-
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r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
show the reaction diagram
-
-
-
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r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
-
-
-
-
?
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
show the reaction diagram
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-
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r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-bromopalmitoyl-CoA
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Aminocarnitine
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D-carnitine
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dodecanoyl-CoA
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substrate inhibition
etomoxir
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hypoglycaemia-inducing drug, double mutant H131A/H340A is insensitive to etomoxir
etomoxiryl-CoA
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hexadecanoyl-CoA
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substrate inhibition
malonyl-CoA
octanoyl-CoA
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substrate inhibition
palmitoyl-CoA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002 - 0.006
decanoyl-CoA
0.106 - 160
L-carnitine
0.002 - 0.0167
acyl-CoA
0.00024 - 0.013
decanoyl-CoA
0.102 - 146
L-carnitine
0.015
octanoyl-CoA
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-
0.00046 - 0.0006
palmitoyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0035 - 0.106
malonyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
acyl-CoA substrate specificity of wild-type and G553M mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
OCTC_RAT
612
0
70302
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000 - 55000
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SDS-PAGE
53000
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Western blot, polyclonal antibody reaction
59000
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gel filtration
69000
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x * 69000, recombinant enzyme, SDS-PAGE
70000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 69000, recombinant enzyme, SDS-PAGE
additional information
-
active site structure and substrate positioning modeling for wild-type and G553M mutant enzymes
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G553M
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site-directed mutagenesis, the mutant enzyme shows altered substrate specificity: highly reduced activity with medium- and long-chain acyl-CoAs and increased activity with acetyl-CoA and butanoyl-CoA compared to the wild-type enzyme
additional information
-
the carnitine acetyl-transferase, specific for acetyl-CoA/short-chain acyl-CoAs, can be modified to an enzyme with elevated carnitine octanoyltransferase activity by mutation of Met564 to Gly, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
quite unstable, labile in Triton X-100 and octylglucoside, stable in 8 mM CHAPS, 200 mM guanidium chloride and 0.5% Tween 20
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stable for at least 1 week in 100 mM phosphate buffer with 0.4 M KCl, pH 5.5-7.5
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, stable to freezing at for at least 5 months
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
cDNA clone from a rat liver library, 2 forms of COT in peroxisomes results of the trans-splicing mechanism in pre-mRNAs
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expression of wild-type and G553M mutant enzymes in an enzyme-deficient Saccharomyces cerevisiae strain
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pYES2 plasmid containing the wild-type and the double mutant H131A/H340A of COT expressed in Saccharomyces cerevisiae
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Solberg, H.E.
Different carnitine acyltransferases in calf liver
Biochim. Biophys. Acta
280
422-433
1972
Bos taurus, Canis lupus familiaris, Columba sp., Homo sapiens, Mus musculus, Oryctolagus cuniculus, Platyrrhini, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Solberg, H.E.
Acyl group specificity of mitochondrial pools of carnitine acyltransferases
Biochim. Biophys. Acta
360
101-112
1974
Bos taurus, Mus musculus, Mus musculus NMRI/Bom, Rattus norvegicus, Rattus norvegicus Wistar/Moell
Manually annotated by BRENDA team
Markwell, M.A.K.; Tolbert, N.E.; Bieber, L.L.
Comparison of the carnitine acyltransferase activities from rat liver peroxisomes and microsomes
Arch. Biochem. Biophys.
176
479-488
1976
Columba sp., Rattus norvegicus, Sus scrofa
-
Manually annotated by BRENDA team
Saggerson, E.D.; Carpenter, C.A.
Malonyl CoA inhibition of carnitine acyltransferase activities: effects of thiol-group reagents
FEBS Lett.
137
124-128
1982
Rattus norvegicus
Manually annotated by BRENDA team
Farrell, S.O.; Bieber, L.L.
Carnitine octanoyltransferase of mouse liver peroxisomes: properties and effect of hypolipidemic drugs
Arch. Biochem. Biophys.
222
123-132
1983
Bos taurus, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Farrell, S.O.; Fiol, C.J.; Reddy, J.K.; Bieber, L.L.
Properties of purified carnitine acyltransferases of mouse liver peroxisomes
J. Biol. Chem.
259
13089-13095
1984
Bos taurus, Canis lupus familiaris, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Bird, M.I.; Munday, L.A.; Saggerson, E.D.; Clark, J.B.
Carnitine acyltransferase activities in rat brain mitochondria. Bimodal distribution, kinetic constants, regulation by malonyl-CoA and developmental pattern
Biochem. J.
226
323-330
1985
Mus musculus, Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Healy, M.J.; Kerner, J.; Bieber, L.L.
Enzymes of carnitine acylation. Is overt carnitine palmitoyltransferase of liver peroxisomal carnitine octanoyltransferase?
Biochem. J.
249
231-237
1988
Bos taurus, Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Lilly, K.; Bugaisky, G.E.; Umeda, P.K.; Bieber, L.L.
The medium-chain carnitine acyltransferase activity associated with rat liver microsomes is malonyl-CoA sensitive
Arch. Biochem. Biophys.
280
167-174
1990
Homo sapiens, Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Nic A'Bhaird, N.; Ramsay, R.R.
Malonyl-CoA inhibition of peroxisomal carnitine octanoyltransferase
Biochem. J.
286
637-640
1992
Rattus norvegicus
Manually annotated by BRENDA team
Chung, C.D.; Bieber, L.L.
Properties of the medium chain/long chain carnitine acyltransferase purified from rat liver microsomes
J. Biol. Chem.
268
4519-4524
1993
Rattus norvegicus
Manually annotated by BRENDA team
Pagot, Y.; Belin, J.M.
Involvement of carnitine acyltransferases in peroxisomal fatty acid metabolism by the yeast Pichia guilliermondii
Appl. Environ. Microbiol.
62
3864-3867
1996
Meyerozyma guilliermondii, Rattus norvegicus
Manually annotated by BRENDA team
Caudevilla, C.; Serra, D.; Miliar, A.; Codony, C.; Asins, G.; Bach, M.; Hegardt, F.G.
Processing of carnitine octanoyltransferase pre-mRNAs by cis and trans-splicing
Adv. Exp. Med. Biol.
466
95-102
1999
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ferdinandusse, S.; Mulders, J.; IJlst, L.; Denis, S.; Dacremont, G.; Waterham, H.R.; Wanders, R.J.A.
Molecular cloning and expression of human carnitine octanoyltransferase: Evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids
Biochem. Biophys. Res. Commun.
263
213-218
1999
Bos taurus, Bos taurus (O19094), Homo sapiens, Homo sapiens (Q9UKG9), no activity in Saccharomyces cerevisiae, Rattus norvegicus (P11466)
Manually annotated by BRENDA team
Morillas, M.; Clotet, J.; Rubi, B.; Serra, D.; Arino, J.; Hegardt, F.G.; Asins, G.
Inhibition by etomoxir of rat liver carnitine octanoyltransferase is produced through the co-ordinate interaction with two histidine residues
Biochem. J.
351
495-502
2000
Bos taurus, no activity in Saccharomyces cerevisiae, Rattus norvegicus (P11466)
-
Manually annotated by BRENDA team
Hegardt, F.G.; Bach, M.; Asins, G.; Caudevilla, C.; Morillas, M.; Codony, C.; Serra, D.
Post-transcriptional regulation of rat carnitine octanoyltransferase
Biochem. Soc. Trans.
29
316-320
2001
Rattus norvegicus
Manually annotated by BRENDA team
Morillas, M.; Gomez-Puertas, P.; Roca, R.; Serra, D.; Asins, G.; Valencia, A.; Hegardt, F.G.
Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT). Mutation of CPT 1 histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity
J. Biol. Chem.
276
45001-45008
2001
Rattus norvegicus
Manually annotated by BRENDA team
Morillas, M.; Gomez-Puertas, P.; Rubi, B.; Clotet, J.; Arino, J.; Valencia, A.; Hegardt, F.G.; Serra, D.; Asins, G.
Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I. Mutational analysis of a malonyl-CoA affinity domain
J. Biol. Chem.
277
11473-11480
2002
Rattus norvegicus (P11466)
Manually annotated by BRENDA team
Morillas, M.; Gomez-Puertas, P.; Bentebibel, A.; Selles, E.; Casals, N.; Valencia, A.; Hegardt, F.G.; Asins, G.; Serra, D.
Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition
J. Biol. Chem.
278
9058-9063
2003
Rattus norvegicus
Manually annotated by BRENDA team
Cordente, A.G.; Lopez-Vinas, E.; Vazquez, M.I.; Swiegers, J.H.; Pretorius, I.S.; Gomez-Puertas, P.; Hegardt, F.G.; Asins, G.; Serra, D.
Redesign of carnitine acetyltransferase specificity by protein engineering
J. Biol. Chem.
279
33899-33908
2004
Rattus norvegicus
Manually annotated by BRENDA team
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