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ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
ATP + a long-chain fatty acid + LipD
AMP + diphosphate + a long-chain acyl-LipD
ATP + an acid + [acyl-carrier protein]
?
-
enzyme functions in the incorporation of fatty acids into phospholipid
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
ATP + cis-vaccenic acid + [acyl-carrier protein]
AMP + diphosphate + cis-vaccenoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + decanoate + an [acyl-carrier protein]
AMP + diphosphate + long-chain decanoyl-[acyl-carrier protein]
-
-
-
?
ATP + decanoic acid + [acyl-carrier protein]
AMP + diphosphate + decanoyl-[acyl-carrier protein]
ATP + hexadecanoate + an [acyl-carrier protein]
AMP + diphosphate + hexadecanoyl-[acyl-carrier protein]
low activity
-
-
?
ATP + hexanoic acid + [acyl-carrier protein]
AMP + diphosphate + hexanoyl-[acyl-carrier protein]
ATP + laurate + an [acyl-carrier protein]
AMP + diphosphate + lauroyl-[acyl-carrier protein]
-
-
-
?
ATP + lauric acid + [acyl-carrier protein]
AMP + diphosphate + lauroyl-[acyl-carrier protein]
ATP + linoleic acid + [acyl-carrier protein]
AMP + diphosphate + linoleoyl-[acyl-carrier protein]
ATP + myristate + an [acyl-carrier protein]
AMP + diphosphate + myristoyl-[acyl-carrier protein]
-
-
-
?
ATP + myristic acid + [acyl-carrier protein]
AMP + diphosphate + myristoyl-[acyl-carrier protein]
ATP + octanoate + an [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
low activity
-
-
?
ATP + octanoate + [AcpP1]
AMP + diphosphate + octanoyl-[AcpP1]
recombinant holo-AcpP1 from Pseudomonas aeruginosa
-
-
?
ATP + octanoate + [AcpP2]
AMP + diphosphate + octanoyl-[AcpP2]
recombinant holo-AcpP2 from Pseudomonas aeruginosa
-
-
?
ATP + octanoate + [AcpP3]
AMP + diphosphate + octanoyl-[AcpP3]
recombinant holo-AcpP3 from Pseudomonas aeruginosa
-
-
?
ATP + octanoate + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
ATP + octanoic acid + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
ATP + oleate + an [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
ATP + oleic acid + [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
ATP + palmitate + an [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
ATP + palmitic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
ATP + palmitoleic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoleoyl-[acyl-carrier protein]
ATP + saturated fatty acids + an [acyl-carrier protein]
?
-
-
-
-
?
ATP + stearic acid + [acyl-carrier protein]
AMP + diphosphate + stearoyl-[acyl-carrier protein]
ATP + tetradecanoate + [acyl-carrier protein]
AMP + diphosphate + tetradecanoyl-[acyl-carrier protein]
ATP + unsaturated fatty acids + an [acyl-carrier protein]
?
-
-
-
-
?
dATP + a fatty acid + [acyl-carrier protein]
dAMP + diphosphate + fatty acid-[acyl-carrier protein]
-
25% of the activity relative to ATP
-
-
?
additional information
?
-
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
the enzyme uses host cell fatty acids as substrates
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
the enzyme uses host cell fatty acids as substrates
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
the enzyme uses host cell fatty acids as substrates
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + LipD
AMP + diphosphate + a long-chain acyl-LipD
-
-
-
?
ATP + a long-chain fatty acid + LipD
AMP + diphosphate + a long-chain acyl-LipD
LipD structure analysis and comparisons, overview
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
E. coli enzyme is able to acylate acyl-carrier protein from spinach, soybean, avocado, corn, and several other plants
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
the best substrates are saturated fatty acids, C12:0 to C16:0
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
synthesis of activated acyl-carrier protein that is essential as a carrier of acyl-intermediates, donor for activated acyl groups for the synthesis of lipids and lipid derivatives, functions as 2-acylglycerophosphoethanolamine acyltransferase
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
fatty acids with chain lengths between 8 and 18 carbons serve as substrates
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
-
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
synthesis of activated acyl-carrier protein that is essential as a carrier of acyl-intermediates and donor for activated acyl groups for the synthesis of lipids and lipid derivatives
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
synthesis of activated acyl-carrier protein that is essential as a carrier of acyl-intermediates and donor for activated acyl groups for the synthesis of lipids and lipid derivatives
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
mutations E41D, E41K, A45G, A45C, A45W and V43I in acyl-carrier protein have only minor effects on activity
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
mutations in acyl-carrier protein F50A, I54L and I54V increases Km-values, minor effects with mutations at positions V12G, Y71A and A59G
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
-
-
?
ATP + decanoic acid + [acyl-carrier protein]
AMP + diphosphate + decanoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + decanoic acid + [acyl-carrier protein]
AMP + diphosphate + decanoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + decanoic acid + [acyl-carrier protein]
AMP + diphosphate + decanoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + hexanoic acid + [acyl-carrier protein]
AMP + diphosphate + hexanoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + hexanoic acid + [acyl-carrier protein]
AMP + diphosphate + hexanoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + lauric acid + [acyl-carrier protein]
AMP + diphosphate + lauroyl-[acyl-carrier protein]
-
-
-
-
?
ATP + lauric acid + [acyl-carrier protein]
AMP + diphosphate + lauroyl-[acyl-carrier protein]
-
-
-
-
?
ATP + lauric acid + [acyl-carrier protein]
AMP + diphosphate + lauroyl-[acyl-carrier protein]
-
-
-
-
?
ATP + linoleic acid + [acyl-carrier protein]
AMP + diphosphate + linoleoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + linoleic acid + [acyl-carrier protein]
AMP + diphosphate + linoleoyl-[acyl-carrier protein]
-
most effective subtrate
-
-
?
ATP + myristic acid + [acyl-carrier protein]
AMP + diphosphate + myristoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + myristic acid + [acyl-carrier protein]
AMP + diphosphate + myristoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + myristic acid + [acyl-carrier protein]
AMP + diphosphate + myristoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + octanoate + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
acyl-carrier protein from Eschrichia coli is a good substrate, whilst octanoylation of the Lactococcus lactis acyl-carrier protein is very weak and that of the bovine mitochondrial acyl-carrier protein only barely detectable
-
-
?
ATP + octanoate + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
acyl-carrier protein from Eschrichia coli is a good substrate, whilst octanoylation of the Lactococcus lactis acyl-carrier protein is very weak and that of the bovine mitochondrial acyl-carrier protein only barely detectable
-
-
?
ATP + octanoic acid + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + octanoic acid + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + octanoic acid + [acyl-carrier protein]
AMP + diphosphate + octanoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + oleate + an [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
-
-
?
ATP + oleate + an [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + oleate + an [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
-
-
?
ATP + oleic acid + [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + oleic acid + [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + oleic acid + [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + oleic acid + [acyl-carrier protein]
AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
-
-
?
ATP + palmitate + an [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
preferred acyl substrate
-
-
?
ATP + palmitate + an [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
preferred acyl substrate
-
-
?
ATP + palmitate + an [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
preferred acyl substrate
-
-
?
ATP + palmitic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + palmitic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
-
-
?
ATP + palmitic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + palmitic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
-
-
?
ATP + palmitic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + palmitoleic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoleoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + palmitoleic acid + [acyl-carrier protein]
AMP + diphosphate + palmitoleoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + stearic acid + [acyl-carrier protein]
AMP + diphosphate + stearoyl-[acyl-carrier protein]
-
stearic acid is a better substrate than palmitic acid or oleic acid
-
-
?
ATP + stearic acid + [acyl-carrier protein]
AMP + diphosphate + stearoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + stearic acid + [acyl-carrier protein]
AMP + diphosphate + stearoyl-[acyl-carrier protein]
-
-
-
-
?
ATP + tetradecanoate + [acyl-carrier protein]
AMP + diphosphate + tetradecanoyl-[acyl-carrier protein]
-
-
-
?
ATP + tetradecanoate + [acyl-carrier protein]
AMP + diphosphate + tetradecanoyl-[acyl-carrier protein]
-
-
-
?
additional information
?
-
different surface charges of acyl-carrier protein derivatives LipD and FAS-ACP from Actinoplanes friuliensis allow the acyl-CoA ligase to interact preferentially with the LipD instead of binding to the FAS-ACP, overview
-
-
?
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
-
-
?
additional information
?
-
-
exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo
-
-
?
additional information
?
-
exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo
-
-
?
additional information
?
-
-
exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo
-
-
?
additional information
?
-
exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo
-
-
?
additional information
?
-
-
enzyme may function to reintroduce free fatty acids into the biosynthetic pathway
-
-
?
additional information
?
-
-
possibly functions in the activation of free fatty acids into a form that can be transferred into phospholipid
-
-
?
additional information
?
-
-
physiological role of 2-acylglycerophosphoethanolamine acyltransferase/acyl-acyl carrier protein synthetase in fatty acid uptake and lysophospholipid uptake, and in maintaining membrane phospholipid composition
-
-
?
additional information
?
-
-
the cell-free extract of Pseudomonas aeruginosa can acylate only the holo-form of the acyl carrier protein AcpP1 for the synthesis of fatty acids, while it is inactive with acyl carrier proteins AcpP2 and AcpP3
-
-
?
additional information
?
-
-
no activity with GTP, CTP or UTP
-
-
?
additional information
?
-
rather broad substrate specificity, accepting fatty acids with chain length between C12 and C18
-
-
?
additional information
?
-
-
rather broad substrate specificity, accepting fatty acids with chain length between C12 and C18
-
-
?
additional information
?
-
the enzyme from Vibrio harveyi can acylate holo-forms of the acyl carrier proteins, AcpP1, AcpP2, and AcpP3, from Pseudomonas aeruginosa
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
ATP + a long-chain fatty acid + LipD
AMP + diphosphate + a long-chain acyl-LipD
-
-
-
?
ATP + an acid + [acyl-carrier protein]
?
-
enzyme functions in the incorporation of fatty acids into phospholipid
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
additional information
?
-
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
the enzyme uses host cell fatty acids as substrates
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
the enzyme uses host cell fatty acids as substrates
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
the enzyme uses host cell fatty acids as substrates
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
-
?
ATP + a long-chain fatty acid + an [acyl-carrier protein]
AMP + diphosphate + a long-chain acyl-[acyl-carrier protein]
-
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
synthesis of activated acyl-carrier protein that is essential as a carrier of acyl-intermediates, donor for activated acyl groups for the synthesis of lipids and lipid derivatives, functions as 2-acylglycerophosphoethanolamine acyltransferase
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
synthesis of activated acyl-carrier protein that is essential as a carrier of acyl-intermediates and donor for activated acyl groups for the synthesis of lipids and lipid derivatives
-
-
?
ATP + an acid + [acyl-carrier protein]
AMP + diphosphate + acyl-[acyl-carrier protein]
-
synthesis of activated acyl-carrier protein that is essential as a carrier of acyl-intermediates and donor for activated acyl groups for the synthesis of lipids and lipid derivatives
-
-
?
additional information
?
-
-
exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo
-
-
?
additional information
?
-
exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo
-
-
?
additional information
?
-
-
exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo
-
-
?
additional information
?
-
exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo
-
-
?
additional information
?
-
-
enzyme may function to reintroduce free fatty acids into the biosynthetic pathway
-
-
?
additional information
?
-
-
possibly functions in the activation of free fatty acids into a form that can be transferred into phospholipid
-
-
?
additional information
?
-
-
physiological role of 2-acylglycerophosphoethanolamine acyltransferase/acyl-acyl carrier protein synthetase in fatty acid uptake and lysophospholipid uptake, and in maintaining membrane phospholipid composition
-
-
?
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evolution
Chlamydia trachomatis encodes for a homologue (CT776, aasC) to the C-terminal acyl-ACP synthetase domain of the bifunctional Escherichia coli Aas. The Escherichia coli aas gene encodes a bifunctional protein with 2-acyl-GPE acyltransferase activity localized in the N-terminal domain and an acyl-ACP synthetase activity in the C-terminal domain. Chlamydia trachomatis encodes adjacent genes that are homologous to the two aas domains. The CT775 gene product is related to the N-terminal Escherichia coli Aas acyltransferase domain (residues 11-149) and contains the acyltransferase catalytic HX4D motif. The CT776 gene product is related to the C-terminal acyl-ACP synthetase domain (residues 256-709) and contains the domain, which corresponds to the binding site for the acyl-adenylate intermediate
evolution
-
Chlamydia trachomatis encodes for a homologue (CT776, aasC) to the C-terminal acyl-ACP synthetase domain of the bifunctional Escherichia coli Aas. The Escherichia coli aas gene encodes a bifunctional protein with 2-acyl-GPE acyltransferase activity localized in the N-terminal domain and an acyl-ACP synthetase activity in the C-terminal domain. Chlamydia trachomatis encodes adjacent genes that are homologous to the two aas domains. The CT775 gene product is related to the N-terminal Escherichia coli Aas acyltransferase domain (residues 11-149) and contains the acyltransferase catalytic HX4D motif. The CT776 gene product is related to the C-terminal acyl-ACP synthetase domain (residues 256-709) and contains the domain, which corresponds to the binding site for the acyl-adenylate intermediate
-
evolution
-
Chlamydia trachomatis encodes for a homologue (CT776, aasC) to the C-terminal acyl-ACP synthetase domain of the bifunctional Escherichia coli Aas. The Escherichia coli aas gene encodes a bifunctional protein with 2-acyl-GPE acyltransferase activity localized in the N-terminal domain and an acyl-ACP synthetase activity in the C-terminal domain. Chlamydia trachomatis encodes adjacent genes that are homologous to the two aas domains. The CT775 gene product is related to the N-terminal Escherichia coli Aas acyltransferase domain (residues 11-149) and contains the acyltransferase catalytic HX4D motif. The CT776 gene product is related to the C-terminal acyl-ACP synthetase domain (residues 256-709) and contains the domain, which corresponds to the binding site for the acyl-adenylate intermediate
-
malfunction
fatty acid incorporation by Chlamydia-infected cells and Chlamydia AasC activity is inhibited by triacsin C and rosiglitazoneG
malfunction
-
Pseudomonas aeruginosa acpP1 deletion is lethal, while disruption of acpP2 or acpP3 in the Pseudomonas aeruginosa genome allowa mutant strains to grow like the wild-type strain. AcpP1 functions in fatty acid biosynthesis with the enzyme acyl-ACP synthetase, acpP2 and acpP3 do not play roles in the fatty acid synthetic pathway. Replacement of acpP1 with Escherichia coli acpP reduces the ability of Pseudomonas aeruginosa to produce some exo-products and abolished swarming motility
malfunction
-
unlike wild-type cells, the aas-deficient cells of a mutant Synechococcus elongatus strain PCC 7942 cannot increase their growth rate as the light intensity is increased from 50 to 400 mmol photons m/s, and the high-light-grown mutant cells accumulate free fatty acids and the lysolipids derived from all the four major classes of membrane lipids, revealing high-light-induced lipid deacylation. The high-light-grown mutant cells show much lower photosystem PSII activity and Chl contents as compared with the wild-type cells or low-light-grown mutant cells. The loss of Aas accelerates photodamage of PSII but does not affect the repair process of PSII, indicating that PSII is destabilized in the mutant. Effects of high light and Aas deficiency on oligomerization state of photosystems. Phenotype, detailed overview
malfunction
-
fatty acid incorporation by Chlamydia-infected cells and Chlamydia AasC activity is inhibited by triacsin C and rosiglitazoneG
-
malfunction
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unlike wild-type cells, the aas-deficient cells of a mutant Synechococcus elongatus strain PCC 7942 cannot increase their growth rate as the light intensity is increased from 50 to 400 mmol photons m/s, and the high-light-grown mutant cells accumulate free fatty acids and the lysolipids derived from all the four major classes of membrane lipids, revealing high-light-induced lipid deacylation. The high-light-grown mutant cells show much lower photosystem PSII activity and Chl contents as compared with the wild-type cells or low-light-grown mutant cells. The loss of Aas accelerates photodamage of PSII but does not affect the repair process of PSII, indicating that PSII is destabilized in the mutant. Effects of high light and Aas deficiency on oligomerization state of photosystems. Phenotype, detailed overview
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metabolism
friulimicin is a cyclic lipodecapeptide antibiotic that is produced by Actinoplanes friuliensis. Similar to the related lipopeptide drug daptomycin, the peptide skeleton of friulimicin is synthesized by a large multienzyme nonribosomal peptide synthetase (NRPS) system. The LipD protein plays a major role in the acylation reaction of friulimicin. The attachment of the fatty acid group promotes its antibiotic activity. Phylogenetic analysis reveals that LipD is most closely related to other freestanding acyl carrier proteins (ACPs), for which the genes are located near to NRPS gene clusters
metabolism
phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis
metabolism
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phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis
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physiological function
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knockout mutant strains show two phenotypes characterized by the inability to utilize exogenous fatty acids and by the secretion of endogenous fatty acids into the culture medium. The detected free fatty acids are released from membrane lipids. The data suggest a considerable turnover of lipid molecules and a role for Aas activity in recycling the released fatty acids
physiological function
knockout mutant strains show two phenotypes characterized by the inability to utilize exogenous fatty acids and by the secretion of endogenous fatty acids into the culture medium. The detected free fatty acids are released from membrane lipids. The data suggest a considerable turnover of lipid molecules and a role for Aas activity in recycling the released fatty acids
physiological function
in infected cells, incorporation of exogenous long-chain fatty acids into membrane glycerophospholipids proceeds by their esterification to acyl-CoA by human long-chain acyl-CoA synthetase (hACSL) enzymes and to acyl-ACP by the bacterial acyl carrier protein (ACP) synthase AasC (CT776)
physiological function
LipA seems to be involved in the initiation of the acylation reaction during the synthesis of lipopeptide antibiotics through the nonribosomal peptide synthetase (NRPS) system. The activation of the fatty acid is carried out by a two-step catalysis reaction in the presence of ATP and Mg2+
physiological function
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only the acpP1 gene can restore growth in the Escherichia coli acpP mutant strain CY1877, while genes acpP2 and acpP3 are ineffective, neither AcpP2 nor AcpP3 can act as a substrate for synthesis of N-acylhomoserine lactones molecules in vivo. Gene acpP1 is essential for Pseudomonas aeruginosa growth
physiological function
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remodeling of membrane lipids is activated by high-intensity light and that the recycling of free fatty acids is essential for acclimation to highlight conditions involving the enzyme. Aas is essential for acclimation of the cyanobacterium to high-light conditions
physiological function
the CT776 gene encodes an acyl-ACP synthetase (AasC) with a substrate preference for palmitic compared with oleic acid in vitro. Exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo. Possible existence of an AasC-dependent pathway in Chlamydia trachomatis that selectively scavenges host saturated fatty acids to be used for the de novo synthesis of its membrane constituents
physiological function
-
in infected cells, incorporation of exogenous long-chain fatty acids into membrane glycerophospholipids proceeds by their esterification to acyl-CoA by human long-chain acyl-CoA synthetase (hACSL) enzymes and to acyl-ACP by the bacterial acyl carrier protein (ACP) synthase AasC (CT776)
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physiological function
-
the CT776 gene encodes an acyl-ACP synthetase (AasC) with a substrate preference for palmitic compared with oleic acid in vitro. Exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo. Possible existence of an AasC-dependent pathway in Chlamydia trachomatis that selectively scavenges host saturated fatty acids to be used for the de novo synthesis of its membrane constituents
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physiological function
-
remodeling of membrane lipids is activated by high-intensity light and that the recycling of free fatty acids is essential for acclimation to highlight conditions involving the enzyme. Aas is essential for acclimation of the cyanobacterium to high-light conditions
-
physiological function
-
the CT776 gene encodes an acyl-ACP synthetase (AasC) with a substrate preference for palmitic compared with oleic acid in vitro. Exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo. Possible existence of an AasC-dependent pathway in Chlamydia trachomatis that selectively scavenges host saturated fatty acids to be used for the de novo synthesis of its membrane constituents
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