Literature summary for 2.3.1.51 extracted from

Soupene, E.; Kuypers, F.A.
Phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis (2017), Sci. Rep., 7, 15767 .

Search for more literature for 2.3.1.51

Inhibitors

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

Localization	Comment	Organism	GeneOntology No.	Textmining

Natural Substrates/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Chlamydia trachomatis	O84780	-	-
Chlamydia trachomatis D/UW-3/Cx	O84780	-	-

Substrates and Products (Substrate)

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

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

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

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Release 2023.1 (January 2023)