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Information on EC 2.3.1.137 - carnitine O-octanoyltransferase and Organism(s) Bos taurus and UniProt Accession O19094

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EC Tree
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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Bos taurus
UNIPROT: O19094
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Synonyms
carnitine acyltransferase, carnitine octanoyltransferase, carnitine o-octanoyltransferase, medium-chain/long-chain carnitine acyltransferase, medium-chain carnitine acyltransferase, overt mitochondrial carnitine palmitoyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Carnitine medium-chain acyltransferase
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-
-
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carnitine octanoyltransferase
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CrOT
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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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additional information
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enzyme belongs to the family of carnitine acyltransferases
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
show the reaction diagram
catalytic mechanism, active site structure, substrate recognition mechanism, amino acid residues 343, 564 and 553 determine the acyl-CoA substrate specificity, catalytic residue is His343
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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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
acyl-L-carnitine + CoA
acyl-CoA + L-carnitine
show the reaction diagram
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
-
-
-
?
acetyl-CoA + L-carnitine
CoA + acetyl-carnitine
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
choline + L-carnitine
?
show the reaction diagram
decanoyl-L-carnitine + CoA
decanoyl-CoA + L-carnitine
show the reaction diagram
-
-
-
-
?
dodecanoyl-CoA + L-carnitine
L-dodecanoyl-L-carnitine + CoA
show the reaction diagram
dodecanoyl-L-carnitine + CoA
dodecanoyl-CoA + L-carnitine
show the reaction diagram
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
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
show the reaction diagram
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
show the reaction diagram
L-hexanoylcarnitine + CoA
hexanoyl-CoA + L-carnitine
show the reaction diagram
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
show the reaction diagram
palmitoyl-L-carnitine + CoA
palmitoyl-CoA + L-carnitine
show the reaction diagram
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-
-
-
?
propionyl-CoA + L-carnitine
propionyl-L-carnitine + CoA
show the reaction diagram
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-
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-
r
propionyl-L-carnitine + CoA
propionyl-CoA + L-carnitine
show the reaction diagram
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-
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r
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-L-carnitine + CoA
acyl-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
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
show the reaction diagram
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
show the reaction diagram
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step in the transport of fatty acids across the inner mitochondrial membrane, reaction plays a role in balancing cellular CoA:acyl-CoA ratio
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-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dodecanoyl-CoA
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substrate inhibition
hemiacylcarnitinium
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hemicholinium
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hexadecanoyl-CoA
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substrate inhibition
octanoyl-CoA
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substrate inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000206 - 0.794
decanoyl-CoA
0.0948 - 0.992
L-carnitine
0.6
palmitoyl-CoA
mutant SAA-COT
16
acetyl-CoA
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-
143
choline
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mutant [Asn505]COT
0.00024 - 0.34
decanoyl-CoA
8.4
Decanoyl-L-carnitine
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-
0.036
hexadecanoyl-L-carnitine
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0.0948 - 160
L-carnitine
7.4
palmitoyl-L-carnitine
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
113
hemiacylcarnitinium
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OCTC_BOVIN
612
0
70263
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64400
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SDS-PAGE
70260
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calculated from cDNA sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R518N
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site-directed mutagenesis, mutant shows 1650fold increased Km for L-carnitine, only slightly affected Km for acyl-CoA and kcat compared to the wild-type enzyme
S552A
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site-directed mutagenesis, mutant shows 17fold increased Km for L-carnitine compared to the wild-type enzyme
S554X
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site-directed mutagenesis, mutant shows 10fold decreased kcat compared to the wild-type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, can be kept for several months with only moderate loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
partially
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recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia coli
cDNA cloning by library screening and recombinant expression in Escherichia coli
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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., Oryctolagus cuniculus, Homo sapiens, Platyrrhini, Mus musculus, 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, Rattus norvegicus, Mus musculus NMRI/Bom, Rattus norvegicus Wistar/Moell
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
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
Cronin, C.N.
The conserved serine-threonine-serine motif of the carnitine acyltransferases is involved in carnitine binding and transition-state stabilization: a site-directed mutagenesis study
Biochem. Biophys. Res. Commun.
238
784-789
1997
Bos taurus (O19094)
Manually annotated by BRENDA team
Cronin, C.N.
cDNA cloning, recombinant expression, and site-directed mutagenesis of bovine liver carnitine octanoyltransferase. Arg505 binds the carboxylate group of carnitine
Eur. J. Biochem.
247
1029-1037
1997
Bos taurus
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 (Q9UKG9), Homo sapiens, no activity in Saccharomyces cerevisiae, Rattus norvegicus (P11466)
Manually annotated by BRENDA team
Ramsay, R.R.; Gandour, R.D.
Selective modulation of carnitine long-chain acyltransferase activities: Kinetics, inhibitors, and active sites of COT and CPT-II
Adv. Exp. Med. Biol.
466
103-109
1999
Bos taurus
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
Jogl, G.; Hsiao, Y.S.; Tong, L.
Structure and function of carnitine acyltransferases
Ann. N. Y. Acad. Sci.
1033
17-29
2004
Bos taurus
Manually annotated by BRENDA team