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Information on EC 6.2.1.3 - long-chain-fatty-acid-CoA ligase

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.3 long-chain-fatty-acid-CoA ligase
IUBMB Comments
Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
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This record set is specific for:
UNIPROT: Q9VCC6
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
acsl1, fatp4, fatty acid transport protein, acsl3, acsl5, long-chain acyl-coa synthetase, fatty acyl-coa synthetase, acsl6, fatp2, acyl-coa synthetase long-chain, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
fatty acyl-CoA synthetase
-
long fatty acyl-CoA synthetase
-
ACS3
-
-
-
-
Acyl coenzyme A synthetase
-
-
-
-
Acyl-activating enzyme
-
-
-
-
Acyl-CoA ligase
-
-
-
-
Acyl-CoA synthetase
-
-
-
-
Acyl-CoA synthetase 3
-
-
-
-
Acyl-coenzyme A ligase
-
-
-
-
FAA1
-
-
-
-
Fatty acid CoA ligase
-
-
-
-
Fatty acid thiokinase (long chain)
-
-
-
-
Fatty acyl-coenzyme A synthetase
-
-
-
-
Fatty-acyl-CoA ligase
-
-
-
-
LACS
-
-
-
-
LCFA synthetase
-
-
-
-
Long chain fatty acyl CoA ligase
-
-
-
-
Long chain fatty acyl-CoA synthetase
-
-
-
-
Long-chain acyl CoA synthetase
-
-
-
-
Long-chain acyl-CoA synthetase I
-
-
-
-
Long-chain acyl-CoA synthetase II
-
-
-
-
Long-chain acyl-coenzyme A synthetase
-
-
-
-
Long-chain fatty acyl coenzyme A synthetase
-
-
-
-
mACS4
-
-
-
-
Oleoyl-CoA synthetase
-
-
-
-
Palmitoyl coenzyme A synthetase
-
-
-
-
Palmitoyl-CoA ligase
-
-
-
-
Palmityl-coenzyme A synthetase
-
-
-
-
Pristanoyl-CoA synthetase
-
-
-
-
Stearoyl-CoA synthetase
-
-
-
-
Thiokinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
Phosphorylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
long-chain fatty acid:CoA ligase (AMP-forming)
Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-18-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + arachidonate + CoA
AMP + diphosphate + arachidonoyl-CoA
show the reaction diagram
-
-
-
?
ATP + decanoate + CoA
AMP + diphosphate + decanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + laurate + CoA
AMP + diphosphate + lauroyl-CoA
show the reaction diagram
-
-
-
?
ATP + linoleate + CoA
AMP + diphosphate + linoleoyl-CoA
show the reaction diagram
-
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
show the reaction diagram
-
-
-
?
lauric acid
?
show the reaction diagram
-
-
-
?
linoleic acid + ATP + CoA
linoleoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arachidonic acid
concentration above 10 microM
linoleic acid
concentration above 10 microM
oleic acid
concentration above 10 microM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00168
lauric acid
-
0.00188
linoleic acid
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
estimated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9VCC6_DROME
544
0
59939
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
chimeric protein with firefly luciferase, EC 1.13.12.7, 4% of luminescence activity from Photinus pyralis luciferase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-chelate affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oba, Y.; Tanaka, K.; Inouye, S.
Catalytic properties of domain-exchanged chimeric proteins between firefly luciferase and Drosophila fatty acyl-CoA synthetase CG6178
Biosci. Biotechnol. Biochem.
70
2739-2744
2006
Drosophila melanogaster (Q9VCC6), Drosophila melanogaster
Manually annotated by BRENDA team
Inouye, S.
Firefly luciferase: an adenylate-forming enzyme for multicatalytic functions
Cell. Mol. Life Sci.
67
387-404
2010
Agrypnus binodulus, Drosophila melanogaster (Q9VCC6)
Manually annotated by BRENDA team