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Information on EC 2.3.1.137 - carnitine O-octanoyltransferase and Organism(s) Mus musculus and UniProt Accession Q9DC50
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2.3.1.137 carnitine O-octanoyltransferaseIUBMB 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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Word Map
- 2.3.1.137
- peroxisomal
- acyl-coas
-
beta-oxidation
- malonyl-coa
- acylcarnitine
- palmitoyl-coa
-
ketogenesis
- decanoyl-coa
-
carnitine-dependent
-
crats
-
arrhythmogenesis
- 2-bromopalmitate
-
cpt-ii
-
malonyl-coa-sensitive
- etomoxir
- palmitoylcarnitine
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Carnitine medium-chain acyltransferase
-
-
-
-
carnitine octanoyltransferase
easily solubilized mitochondrial carnitine palmitoyltransferase
-
-
-
-
medium-chain/long-chain carnitine acyltransferase
-
-
-
-
overt mitochondrial carnitine palmitoyltransferase
-
-
-
-
additional information
the enzyme belongs to the carnitine acyltransferase family
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine
acyl-binding hydrophobic pocket structure involving residues G553, C323, and Met335, the acyl-CoA substrate chain length specificity is determined by G553, Met335 is important for catalysis
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
Acyl group transfer
-
-
-
-
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
39369-19-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tetradecanoyl-CoA + L-carnitine
CoA + L-tetradecanoylcarnitine
low activity
-
-
?
hexadecanoyl-CoA + L-carnitine
L-hexadecanoyl-L-carnitine + CoA
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
palmitoyl-CoA + L-carnitine
L-palmitoyl-L-carnitine + CoA
-
-
-
-
r
palmitoyl-L-carnitine + CoA
palmitoyl-CoA + L-carnitine
-
-
-
-
r
octanoyl-CoA + L-carnitine
CoA + L-octanoylcarnitine
preferred substrate
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
-
r
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
gamma-trimethylamino-beta-hydroxybutyrate
-
-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
-
-
-
-
r
additional information
?
-
-
peroxisomal carnitine acyltransferases and acyl-CoA thioesterases are differently expressed to function as complementary enzymes for transport of beta-oxidation metabolites
-
-
?
additional information
?
-
-
peroxisomes contain carnitine acetyltransferase and octanoyltransferase that produce carnitine ester for transport out of the peroxisomes
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + L-carnitine
acyl-L-carnitine + CoA
-
-
-
-
r
L-carnitine + octanoyl-CoA
octanoyl-L-carnitine + CoA
-
-
-
-
r
octanoyl-L-carnitine + CoA
L-carnitine + octanoyl-CoA
-
-
-
-
r
additional information
?
-
-
peroxisomal carnitine acyltransferases and acyl-CoA thioesterases are differently expressed to function as complementary enzymes for transport of beta-oxidation metabolites
-
-
?
additional information
?
-
-
peroxisomes contain carnitine acetyltransferase and octanoyltransferase that produce carnitine ester for transport out of the peroxisomes
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
retains its maximum activity when preincubated at pH 7.0 or 8.5
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
substrate specificity of wild-type and mutant enzymes, overview
additional information
-
substrate specificity of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
low in distal intestine epithelium, distal intestine muscle, brain, heart, lung, spleen, brown and white adipose tissue
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the crat gene contains 2 alternative start codons, translation from the first codon results in a protein of 626 amino acids, with a 21-amino acid leader sequence that targets the CRAT protein to mitochondria
-
in the peroxisomal CRAT mRNA, there is an in-frame stop codon and translation starts at a downstream second start codon, resulting in a protein that contains 605 amino acids
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). OCTC_MOUSE
612
0
70264
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and mutants M335V and C323M enzymes free or in complex with octanoylcarnitine, sitting drop vapour diffusion method, 4°C, reservoir solution contains 0.1 M HEPES, pH 7.4, 62% v/v 2-methyl-2,4-pentanediol, larger crystals by micro- and macroseeding, cross-seeding of recombinant purified selenomethionine-labeled enzyme, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C323M
site-directed mutagenesis, crystal structure comparison with the wild-type enzyme, altered acyl-CoA substrate specificity compared to the wild-type enzyme, highly increased specificity for octanoyl-CoA
G553M
site-directed mutagenesis, highly reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
M335A
site-directed mutagenesis, reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
M335V
site-directed mutagenesis, crystal structure comparison with the wild-type enzyme, highly reduced activity with altered acyl-CoA substrate specificity compared to the wild-type enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
soluble recombinant His-tagged wild-type and selenomethionine-labeled enzyme from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of the His-tagged enzyme in Escherichia coli as soluble protein, expression of enzyme for selenomethionine-labeling in Escherichia coli strain B834(DE3)
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
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
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
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
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
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
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
Jogl, G.; Hsiao, Y.S.; Tong, L.
Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity
J. Biol. Chem.
280
738-744
2005
Mus musculus (Q9DC50), Mus musculus
Gloerich, J.; van Vlies, N.; Jansen, G.A.; Denis, S.; Ruiter, J.P.; van Werkhoven, M.A.; Duran, M.; Vaz, F.M.; Wanders, R.J.; Ferdinandusse, S.
A phytol-enriched diet induces changes in fatty acid metabolism in mice both via PPARalpha-dependent and -independent pathways
J. Lipid Res.
46
716-726
2005
Mus musculus
Westin, M.A.; Hunt, M.C.; Alexson, S.E.
Short- and medium-chain carnitine acyltransferases and acyl-CoA thioesterases in mouse provide complementary systems for transport of beta-oxidation products out of peroxisomes
Cell. Mol. Life Sci.
65
982-990
2008
Mus musculus, Mus musculus 129/Sv
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