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Information on EC 6.2.1.3 - long-chain-fatty-acid-CoA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38137

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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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Saccharomyces cerevisiae
UNIPROT: P38137
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected 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
Acyl-CoA synthetase
-
fatty acid thiokinase
-
fatty acid:CoA ligase, AMP-forming
-
ACS3
-
-
-
-
Acyl coenzyme A synthetase
-
-
-
-
Acyl-activating enzyme
-
-
-
-
Acyl-CoA ligase
-
-
-
-
Acyl-CoA synthetase
Acyl-CoA synthetase 3
-
-
-
-
Acyl-coenzyme A ligase
-
-
-
-
FAA1
-
-
-
-
Faa1p
Faa3p
-
in the membrane
Faa4p
-
in membrane and cytosol
Fatty acid CoA ligase
-
-
-
-
fatty acid CoA ligase: AMP forming
-
-
fatty acid thiokinase
-
Fatty acid thiokinase (long chain)
-
-
-
-
fatty acid:CoA ligase, AMP-forming
-
Fatty acyl-coenzyme A synthetase
-
-
-
-
Fatty-acyl-CoA ligase
-
-
-
-
LACS
-
-
-
-
LCFA synthetase
-
-
-
-
long chain acyl-CoA 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 + lignocerate + CoA
AMP + diphosphate + lignoceroyl-CoA
show the reaction diagram
-
-
-
?
ATP + long-chain carboxylic acid + CoA
?
show the reaction diagram
-
at 36°C the enzyme is required for the utilization of exogenous myristate by the N-myristoyltransferase. This requirement is not apparent at 24°C or 30°C, suggesting that another acylCoA synthetase activity with differing chain length and/or temperature optima exists
-
-
?
ATP + myristate + CoA
AMP + diphosphate + myristoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + oleate + CoA
AMP + diphosphate + oleoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + palmitate + CoA
AMP + diphosphate + palmitoyl-CoA
show the reaction diagram
-
-
-
?
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
ATP + long-chain carboxylic acid + CoA
?
show the reaction diagram
-
at 36°C the enzyme is required for the utilization of exogenous myristate by the N-myristoyltransferase. This requirement is not apparent at 24°C or 30°C, suggesting that another acylCoA synthetase activity with differing chain length and/or temperature optima exists
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required, 10 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0516
ATP
-
in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 30°C
0.0183
CoA
-
in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 30°C
0.0711
oleate
-
in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.121
-
in the presence of 10 mM MnCl2, at pH 8.0
0.145
-
in the presence of 10 mM MgCl2, at pH 8.0
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.58
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
-
gel filtration
72500
-
2 * 72500, gel filtration
77870
calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
2 * 72500, gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography and Sephacryl S-200 HR gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Duronio, R.J.; Knoll, L.J.; Gordon, J.I.
Isolation of a Saccharomyces cerevisiae long chain fatty acyl:CoA synthetase gene (FAA1) and assessment of its role in protein N-myristoylation
J. Cell Biol.
117
515-529
1992
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Li, H.; Melton, E.M.; Quackenbush, S.; DiRusso, C.C.; Black, P.N.
Mechanistic studies of the long chain acyl-CoA synthetase Faa1p from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1771
1246-1253
2007
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Black, P.N.; DiRusso, C.C.
Yeast acyl-CoA synthetases at the crossroads of fatty acid metabolism and regulation
Biochim. Biophys. Acta
1771
286-298
2007
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38137), Saccharomyces cerevisiae (P38225), Saccharomyces cerevisiae (P39518), Rattus norvegicus (O35547), Rattus norvegicus (O88813)
Manually annotated by BRENDA team