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Information on EC 6.2.1.3 - long-chain-fatty-acid-CoA ligase and Organism(s) Photinus pyralis and UniProt Accession P08659

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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:
Photinus pyralis
UNIPROT: P08659
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Word Map
The taxonomic range for the selected organisms is: Photinus pyralis
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
fatty acyl-CoA synthetase
-
luciferase-like protein
-
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
-
-
-
-
additional information
the enzyme is a part of a larger AMP-forming superfamily
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
decanoic acid + ATP + CoA
decanoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
lauric acid + ATP + CoA
lauroyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
myristic acid + ATP + CoA
myristoyl-CoA + AMP + diphosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
luciferin + O2 + ATP
oxidized luciferin + CO2 + H2O + AMP + diphosphate + hv
show the reaction diagram
-
the enzyme in peroxisomes may keep the catalytic functions in bioluminescence and fatty acid metabolism
-
-
?
additional information
?
-
firefly luciferase has two catalytic functions, it can act as a monooxygenase, luciferase, EC 1.13.12.7, but can also synthesize a long-chain fatty acyl-CoA from various long-chain fatty acids in the presence of ATP, CoA and Mg2+
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00741
lauric acid
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.278
lauric acid
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
North American firefly
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LUCI_PHOPY
550
0
60745
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oba, Y.; Sato, M.; Ojika, M.; Inouye, S.
Enzymatic and genetic characterization of firefly luciferase and Drosophila CG6178 as a fatty acyl-CoA synthetase
Biosci. Biotechnol. Biochem.
69
819-828
2005
Luciola cruciata, Photinus pyralis
Manually annotated by BRENDA team
Oba, Y.; Ojika, M.; Inouye, S.
Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase
FEBS Lett.
540
251-254
2003
Luciola cruciata, Photinus pyralis
Manually annotated by BRENDA team
Day, J.C.; Goodall, T.I.; Bailey, M.J.
The evolution of the adenylate-forming protein family in beetles: Multiple luciferase gene paralogues in fireflies and glow-worms
Mol. Phylogenet. Evol.
50
93-101
2008
Photinus pyralis (P08659), Tribolium castaneum
Manually annotated by BRENDA team