Information on EC 6.2.1.20 - long-chain-fatty-acid-[acyl-carrier-protein] ligase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
6.2.1.20
-
RECOMMENDED NAME
GeneOntology No.
long-chain-fatty-acid-[acyl-carrier-protein] ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + a long-chain fatty acid + an [acyl-carrier protein] = AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
-
-
-
-
Acylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
alkane biosynthesis I
-
-
Fatty acid degradation
-
-
heptadecane biosynthesis
-
-
lipoate biosynthesis
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-
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
-
77322-37-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
ecotype Columbia
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-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
PCC 7942
UniProt
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + an acid + [acyl-carrier protein]
?
show the reaction diagram
-
enzyme functions in the incorporation of fatty acids into phospholipid
-
-
-
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
show the reaction diagram
ATP + cis-vaccenic acid + [acyl-carrier protein]
AMP + diphosphate + cis-vaccenoyl-[acyl-carrier protein]
show the reaction diagram
-
-
-
-
-
ATP + decanoic acid + [acyl-carrier protein]
AMP + diphosphate + decanoyl-[acyl-carrier protein]
show the reaction diagram
ATP + hexanoic acid + [acyl-carrier protein]
AMP + diphosphate + hexanoyl-[acyl-carrier protein]
show the reaction diagram
ATP + lauric acid + [acyl-carrier protein]
AMP + diphosphate + lauroyl-[acyl-carrier protein]
show the reaction diagram
ATP + linoleic acid + [acyl-carrier protein]
AMP + diphosphate + linoleoyl-[acyl-carrier protein]
show the reaction diagram
ATP + myristic acid + [acyl-carrier protein]
AMP + diphosphate + myristoyl-[acyl-carrier protein]
show the reaction diagram
ATP + octanoate + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
show the reaction diagram
ATP + octanoic acid + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
show the reaction diagram
ATP + oleic acid + [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
show the reaction diagram
ATP + palmitic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
show the reaction diagram
ATP + palmitoleic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoleoyl-[acyl-carrier protein]
show the reaction diagram
ATP + stearic acid + [acyl-carrier protein]
AMP + diphosphate + stearoyl-[acyl-carrier protein]
show the reaction diagram
ATP + tetradecanoate + [acyl-carrier protein]
AMP + diphosphate + tetradecanoyl-[acyl-carrier protein]
show the reaction diagram
dATP + a fatty acid + [acyl-carrier protein]
dAMP + diphosphate + fatty acid-[acyl-carrier protein]
show the reaction diagram
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25% of the activity relative to ATP
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-
-
additional information
?
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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
ATP + an acid + [acyl-carrier protein]
?
show the reaction diagram
-
enzyme functions in the incorporation of fatty acids into phospholipid
-
-
-
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
requires high concentrations of both Ca2+ and Mg2+
lithium ion
-
0.4 M, required
Salt
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requirement for high concentrations of salt, with the exception of Mg2+, the requirement for ion is nonspecific. Chaotrophic salts are effective at lower concentrations than less chaotrophic salts
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Detergents
-
-
Monovalent salts
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-
-
NEM
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acyl-carrier protein or ATP protects
Triton X-100
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-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
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stimulates
Triton X-100
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stimulates
additional information
-
no evidence for a phospholipid requirement
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 7.9
acyl-carrier protein
0.3 - 2.5
ATP
0.1
Decanoic acid
-
-
0.0035
E. coli acyl-carrier protein
-
-
0.025
lauric acid
-
-
0.023
linoleic acid
-
pH 8.0, 30°C
0.015
myristic acid
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palmitic acid
0.166
Octanoic acid
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-
0.01 - 0.03
oleic acid
0.0053 - 0.043
palmitic acid
0.02
palmitoleic acid
0.005 - 0.015
saturated fatty acids
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C12:0 to C16:0
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0.004
spinach acyl-carrier protein
-
-
0.013 - 0.03
stearic acid
0.03 - 0.16
unsaturated fatty acids
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fatty acids with shorter chain length than 12
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additional information
additional information
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Km values given for several mutant acyl-carrier proteins
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
oleic acid
Synechococcus elongatus
Q31PS1
pH 8.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000478
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at 37°C for 30 min with 10 mM MgSO4, 10 mM ATP, 0.1 mM [9,10-3H]myristic acid in 100 mM Tris-HCl, pH 7.8, and 5 mM dithiothreitol
0.022
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transfected Escherichia coli BL21(DE3) with lactose as inducer and palmitic acid as substrate
0.028
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-
0.071
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transfected Escherichia coli C41(DE3) with IPTG as inducer and palmitic acid as substrate
1.32
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purified enzyme from Escherichia coli C41(DE3) with palmitic acid as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
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-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
x * 27000, SDS-PAGE
35000
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SDS-PAGE and native PAGE
60400
SDS-PAGE, hexahistidine-tagged
62000
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x * 62000, SDS-PAGE
80000
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gel filtration under reducing conditions
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 35000, molecular weight of native protein and subunits by native and SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
half-life: 2 min, in presence of ATP the half-life increases to above 32 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP protects against heat inactivation at 55°C
-
Mg2+ is not required for ATP to protect the enzyme from heat denaturation
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not inactivated by repeated freeze/thaw cycles
-
salts destabilize the enzyme, which results in increased heat lability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.002% Triton X-100, 10% glycerol, 50% loss of activity within 1 month
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-20°C, stable for months in the presence of glycerol
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-80°C, 20 mM Tris-HCl (pH 7.5), 10% glycerol, 1 mM EDTA, 0.1 mM dithiothreitol and 0.002% Triton X-100, several months, no detectable loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a single enzyme protein catalyzes two activities: 2-acylglycerophosphoethanolamine acyltransferase activity and acyl-[acyl-carrier protein] synthetase activity
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Ni-NTA column chromatography
partial purification by DEAE-Sepharose chromatography and Sephacryl S-300 gel filtration
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recombinant proteins using His-tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) and C41(DE3)
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expressed in Escherichia coli strain BL21(DELTADE3)
overexpression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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