Information on EC 6.2.1.19 - long-chain-fatty-acid-protein ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.2.1.19
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RECOMMENDED NAME
GeneOntology No.
long-chain-fatty-acid-protein ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + a long-chain fatty acid + [protein]-L-cysteine = AMP + diphosphate + a [protein]-S-(long-chain-acyl)-L-cysteine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacterial bioluminescence
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SYSTEMATIC NAME
IUBMB Comments
long-chain-fatty-acid:protein ligase (AMP-forming)
Together with a hydrolase component (EC 3.1.2.2/EC 3.1.2.14) and a reductase component (EC 1.2.1.50), this enzyme forms a multienzyme fatty acid reductase complex that produces the long-chain aldehyde substrate of the bacterial luciferase enzyme (EC 1.14.14.3). The enzyme activates free long-chain fatty acids, generated by the action of the transferase component, forming a fatty acyl-AMP intermediate, followed by the transfer of the acyl group to an internal L-cysteine residue. It then transfers the acyl group to EC 1.2.1.50, long-chain acyl-protein thioester reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
82657-98-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + myristic acid + protein
AMP + diphosphate + myristoyl-protein thiolester
show the reaction diagram
additional information
?
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the enzyme complex is involved in the reduction of fatty acids to aldehydes in luminescent bacteria
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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the enzyme complex is involved in the reduction of fatty acids to aldehydes in luminescent bacteria
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required for formation of acyl-AMP
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43130
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calculation from nucleotide sequence
45000
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1 * 45000, SDS-PAGE
52000
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calculation from amino acid composition
66000
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gel filtration
additional information
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450000, MW of the fatty acid reductase complex, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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two polypeptides of MW 34000 and MW 50000 being involved in the acyl-protein synthetase activity are identified. Acylation of the 50000 MW polypeptide alone occurs at a low rate. The rate and level of acylation are greatly stimulated by the addition of either the 34000 MW polypeptide or by the 58000 MW acyl-CoA reductase
monomer
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1 * 45000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE