Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | formation of acyl-ACP by the enzyme from Chlamydia trachomatis is sensitive to triacsin C, while rosiglitazone G inhibits fatty acid incorporation by Chlamydia-infected cells , while the fatty acid incorporation in HeLa cells is unaffected. The inhibitors acts on acyl-ACP synthase AasC (CT776), not lysophospholipid acyltransferase (CT775) | Chlamydia trachomatis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate | Chlamydia trachomatis | - |
CoA + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate | Chlamydia trachomatis D/UW-3/Cx | - |
CoA + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
additional information | Chlamydia trachomatis | the broad substrate specificity of acyltransferase CT775 provides the organism with the capacity to incorporate straight-chain and bacterial specific branched-chain fatty acids. In vivo incorporation of 1-acyl-GPC in cells infected with Chlamydia trachomatis confirms the active remodeling of exogenous lipids that are translocated into the inclusions | ? | - |
- |
|
additional information | Chlamydia trachomatis D/UW-3/Cx | the broad substrate specificity of acyltransferase CT775 provides the organism with the capacity to incorporate straight-chain and bacterial specific branched-chain fatty acids. In vivo incorporation of 1-acyl-GPC in cells infected with Chlamydia trachomatis confirms the active remodeling of exogenous lipids that are translocated into the inclusions | ? | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chlamydia trachomatis | O84780 | - |
- |
Chlamydia trachomatis D/UW-3/Cx | O84780 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate | - |
Chlamydia trachomatis | CoA + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate | - |
Chlamydia trachomatis D/UW-3/Cx | CoA + 1,2-diacyl-sn-glycerol 3-phosphate | - |
? | |
additional information | the broad substrate specificity of acyltransferase CT775 provides the organism with the capacity to incorporate straight-chain and bacterial specific branched-chain fatty acids. In vivo incorporation of 1-acyl-GPC in cells infected with Chlamydia trachomatis confirms the active remodeling of exogenous lipids that are translocated into the inclusions | Chlamydia trachomatis | ? | - |
- |
|
additional information | broad substrate specificity of acyltransferase CT775. It accepts both acyl-ACP and acyl-CoA as acyl donors and, 1- or 2-acyl isomers of lysophosphoplipids as acyl acceptors, cf. EC 2.3.1.62. CT775 is not exclusively a 2-acyl-GPL acyltransferase, 1-acyl-GPL acyltransferase. The transfer of NBD-C16-CoA to 1-acyl-GPC by hLPCAT1 is strongly reduced in the presence of MeC18-CoA. Although unsaturated C18 fatty acids are very abundant at the sn2 position of human PLs, MeC18-CoA is a stronger competitor than C18:1-CoA, possible preference of the bacterial enzyme for the palmitic chain compared to the stearic chain. MeC18-CoA is a substrate for CT775 | Chlamydia trachomatis | ? | - |
- |
|
additional information | the broad substrate specificity of acyltransferase CT775 provides the organism with the capacity to incorporate straight-chain and bacterial specific branched-chain fatty acids. In vivo incorporation of 1-acyl-GPC in cells infected with Chlamydia trachomatis confirms the active remodeling of exogenous lipids that are translocated into the inclusions | Chlamydia trachomatis D/UW-3/Cx | ? | - |
- |
|
additional information | broad substrate specificity of acyltransferase CT775. It accepts both acyl-ACP and acyl-CoA as acyl donors and, 1- or 2-acyl isomers of lysophosphoplipids as acyl acceptors, cf. EC 2.3.1.62. CT775 is not exclusively a 2-acyl-GPL acyltransferase, 1-acyl-GPL acyltransferase. The transfer of NBD-C16-CoA to 1-acyl-GPC by hLPCAT1 is strongly reduced in the presence of MeC18-CoA. Although unsaturated C18 fatty acids are very abundant at the sn2 position of human PLs, MeC18-CoA is a stronger competitor than C18:1-CoA, possible preference of the bacterial enzyme for the palmitic chain compared to the stearic chain. MeC18-CoA is a substrate for CT775 | Chlamydia trachomatis D/UW-3/Cx | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
CT775 | - |
Chlamydia trachomatis |
CT_775 | - |
Chlamydia trachomatis |
LPAT | - |
Chlamydia trachomatis |
lysophospholipid acyltransferase | - |
Chlamydia trachomatis |
More | cf. EC 2.3.1.62 | Chlamydia trachomatis |
SnGlycerol 3-P acyltransferase | UniProt | Chlamydia trachomatis |
General Information | Comment | Organism |
---|---|---|
metabolism | phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis | Chlamydia trachomatis |
physiological function | the enzyme is involved in the formation of the membrane of the human pathogen Chlamydia trachomatis. The broad substrate specificity of acyltransferase CT775 provides the organism with the capacity to incorporate straight-chain and bacterial specific branched-chain fatty acids. In vivo incorporation of 1-acyl-GPC in cells infected with Chlamydia trachomatis confirms the active remodeling of exogenous lipids that are translocated into the inclusions. Both the bacterial acyltransferase CT775 and human host LPCAT1 can transfer branched acyl-CoA to 1-acyl-GPC to form PC, thereby providing evidence for the presence of a system in which host lipids are modified by the addition of bacterial branched fatty acid within the inclusion | Chlamydia trachomatis |