EC Number   |
General Information |
Reference |
|---|
    6.2.1.20 | 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 |
-, 745328 |
| 6.2.1.20 | malfunction |
fatty acid incorporation by Chlamydia-infected cells and Chlamydia AasC activity is inhibited by triacsin C and rosiglitazoneG |
-, 746468 |
| 6.2.1.20 | 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 |
744979 |
| 6.2.1.20 | 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 |
-, 746039 |
| 6.2.1.20 | 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 |
746399 |
| 6.2.1.20 | metabolism |
phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis |
-, 746468 |
| 6.2.1.20 | 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) |
-, 746468 |
| 6.2.1.20 | 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 |
706328 |
| 6.2.1.20 | 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+ |
746399 |
| 6.2.1.20 | physiological function |
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 |
744979 |
