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Information on EC 6.2.1.20 - long-chain-fatty-acid-[acyl-carrier-protein] ligase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8W471

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EC Tree
IUBMB Comments
The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein. Not identical with EC 6.2.1.3 long-chain-fatty-acid---CoA ligase.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q8W471
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acyl-coa ligase, acyl-acp synthetase, acyl carrier protein synthase, acyl-acyl carrier protein synthetase, acp synthase, pfacp, slr1609, aae15, at4g14070, acyl-acp synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl-ACP synthetase
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Acyl-acyl carrier protein synthetase
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Acyl-ACP synthetase
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-
-
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Acyl-acyl carrier protein synthetase
-
-
-
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Acyl-[acyl carrier protein] synthetase
-
-
-
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Acyl-[acyl-carrier-protein]synthetase
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-
-
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Stearoyl-ACP synthetase
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-
-
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Synthetase, acyl-[acyl carrier protein]
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
long-chain-fatty-acid:[acyl-carrier protein] ligase (AMP-forming)
The enzyme ligates long chain fatty acids (with aliphatic chain of 13-22 carbons) to an acyl-carrier protein. Not identical with EC 6.2.1.3 long-chain-fatty-acid---CoA ligase.
CAS REGISTRY NUMBER
COMMENTARY hide
61701-20-0
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77322-37-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
ATP + decanoate + an [acyl-carrier protein]
AMP + diphosphate + long-chain decanoyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
ATP + hexadecanoate + an [acyl-carrier protein]
AMP + diphosphate + hexadecanoyl-[acyl-carrier protein]
show the reaction diagram
low activity
-
-
?
ATP + laurate + an [acyl-carrier protein]
AMP + diphosphate + lauroyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
ATP + myristate + an [acyl-carrier protein]
AMP + diphosphate + myristoyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
ATP + octanoate + an [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
show the reaction diagram
low activity
-
-
?
additional information
?
-
recombinant enzyme AAE15 has acyl-ACP synthetase activity in vitro with specificity for medium chain fatty acids, substrate specificity, overview. Low activity with fatty acids 18:0, 18:1, 18:2, and 18:3
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-
?
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 + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000667
purified recombinant enzyme, pH 8.0, 37°C, with substrate decanoate
0.0001027
purified recombinant enzyme, pH 8.0, 37°C, with substrate laurate
0.0001572
purified recombinant enzyme, pH 8.0, 37°C, with substrate myristate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme has a predicted plastidial targeting peptide
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AAE15_ARATH
727
0
81466
Swiss-Prot
Chloroplast (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 79000, recombinant truncated enzyme lacking the predicted plastidial targeting signal sequence, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
generation of a N-terminally truncated enzyme mutant with deleted predicted plastidial targeting signal sequence by removing the sequence encoding a predicted plastidial targeting peptide increases the expression level significantly
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme, full-length or lacking the predicted plastidial targeting signal sequence, from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography, gel filtration, and dialysis. Removing the sequence encoding a predicted plastidial targeting peptide increases the expression level significantly, like DELTAaas, DELTAaas:AAE15 secretes large amounts of fatty acids into the culture medium. Expression of AAE15 in the DELTAaas strain does not affect fatty acid profiles and does not have a significant complementation effect
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AAE15 or At4g14070, recombinant expression of N-terminally His6-tagged enzyme, full-length or lacking the predicted plastidial targeting signal sequence, in Spodoptera frugiperda Sf9 cells via baculovirus transfection method, recombinant expression of Arabidopsis thaliana AAE15 in an AAS deletion mutant of Synechocystis sp. PCC 6803 resulting in changes in intracellular and extracellular free fatty acids pools in the cyanobacterial DELTAaas strain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koo, A.J.; Fulda, M.; Browse, J.; Ohlrogge, J.B.
Identification of a plastid acyl-acyl carrier protein synthetase in Arabidopsis and its role in the activation and elongation of exogenous fatty acids
Plant J.
44
620-632
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Kaczmarzyk, D.; Hudson, E.P.; Fulda, M.
Arabidopsis acyl-acyl carrier protein synthetase AAE15 with medium chain fatty acid specificity is functional in cyanobacteria
AMB Express
6
doi: 10.1186/s13568-016-0178-z
2016
Arabidopsis thaliana (Q8W471)
Manually annotated by BRENDA team