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Information on EC 2.3.1.137 - carnitine O-octanoyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9UKG9

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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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This record set is specific for:
Homo sapiens
UNIPROT: Q9UKG9
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The taxonomic range for the selected organisms is: Homo sapiens
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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easily solubilized mitochondrial carnitine palmitoyltransferase
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medium-chain/long-chain carnitine acyltransferase
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overt mitochondrial carnitine palmitoyltransferase
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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
4,8-dimethylnonanoyl-CoA + L-carnitine
4,8-dimethylnonanoyl-L-carnitine + CoA
show the reaction diagram
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r
4,8-dimethylnonanoyl-L-carnitine + CoA
4,8-dimethylnonanoyl-CoA + L-carnitine
show the reaction diagram
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r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
show the reaction diagram
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r
decanoyl-CoA + L-carnitine
L-decanoyl-L-carnitine + CoA
show the reaction diagram
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r
heptanoyl-CoA + L-carnitine
L-heptanoyl-L-carnitine + CoA
show the reaction diagram
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r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
show the reaction diagram
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r
acyl-L-carnitine + CoA
acyl-CoA + L-carnitine
show the reaction diagram
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r
dodecanoyl-CoA + L-carnitine
L-dodecanoyl-L-carnitine + CoA
show the reaction diagram
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r
dodecanoyl-L-carnitine + CoA
dodecanoyl-CoA + L-carnitine
show the reaction diagram
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r
hexadecanoyl-L-carnitine + CoA
hexadecanoyl-CoA + L-carnitine
show the reaction diagram
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r
hexanoyl-CoA + L-carnitine
CoA + L-hexanoylcarnitine
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
L-hexanoylcarnitine + CoA
hexanoyl-CoA + L-carnitine
show the reaction diagram
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r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
show the reaction diagram
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r
additional information
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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
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r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
show the reaction diagram
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r
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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?
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
show the reaction diagram
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r
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
skin fibroblast
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
overexpression and knock-down of the enzyme gene in a model of hepatic cells. Increase in enzymic activity induces a decrease in medium chain fatty acid and very long chaichain fatty acid levels in the cell. These changes are accompanied by an increase in the level of mRNA encoding enzymes of the peroxisomal beta oxidation, while there is no change in mitochondrial function. A decrease in carnitine ocatanoyltransferase activity has the opposite effect. Results suggest that carnitine ocatanoyltransferase activity, by controlling the peroxisomal amount of medium chain acyls, may control the peroxisomal oxidative pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OCTC_HUMAN
612
0
70178
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
recombinant enzyme, expressed in Saccharomyces cerevisiae
70000
calculated from cDNA sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 66000, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA PCR amplified, cloned in yeast expression vector pEL26 and expressed in Saccharomyces cerevisiae
expression in HepG2 cell
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
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
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
Le Borgne, F.; Ben Mohamed, A.; Logerot, M.; Garnier, E.; Demarquoy, J.
Changes in carnitine octanoyltransferase activity induce alteration in fatty acid metabolism
Biochem. Biophys. Res. Commun.
409
699-704
2011
Homo sapiens (Q9UKG9)
Manually annotated by BRENDA team