2.3.1.191	(3R)-3-hydroxyarachidonoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine	the external layer of the Gram-negative bacterial outer membrane is primarily composed of a protective, selectively permeable lipopolysaccharide. The biosynthesis of lipopolysaccharide relies on UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD), which transfers 3-hydroxy-arachidonic acid from acyl carrier protein to the 2' amine of UDP-3-O-myristoyl glucosamine. CtLpxD is expected to utilize R-3-hydroxyarachidonoyl-[acyl-carrier protein] and UDP-3-O-(myristoyl)-R-D-glucosamine, based on the predominant molecular species of Chlamydia trachomatis lipid A. This proposal is not validated by in vitro assays	Chlamydia trachomatis	UDP-2-N-((3R)-3-hydroxyarachidonoyl)-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]	-	?	402282	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine	a comparison of the lipid A structures shows that in Escherichia coli and Neisseria meningitidis, LpxD can be expected to have the same specificity, both adding 3-hydroxymyristoyl chains	Neisseria meningitidis	UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]	-	?	402283	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine	since only (R)-3-hydroxymyristate is found at the 2,3,2’, and 3’ positions of Escherichia coli lipid A, it is reassuring that both Escherichia coli acyltransferases display extraordinary specificity for (R)-3-hydroxymyristoyl-[acyl-carrier protein]	Escherichia coli	UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]	-	?	402283	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine	myristoyl-[acyl-carrier protein] does not serve as an acyl donor for the overproduced UDP-3-O-((R)-3-hydroxymyristoyl)-GlcN N-acyltransferase	Escherichia coli	UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]	-	?	402283	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine	third step of lipid A biosynthesis	Escherichia coli	UDP-2,3-bis(3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]	-	?	402285	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine	compulsory ordered mechanism in which (3R)-3-hydroxymyristoyl-[acyl-carrier protein] binds prior to UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine. The product, UDP-2,3-diacylglucosamine, dissociates prior to acyl-carrier protein	Escherichia coli	UDP-2,3-bis(3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]	-	?	402285	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine	-	Escherichia coli	UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]	-	ir	419221	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine	-	Francisella tularensis subsp. novicida	UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]	-	ir	419221	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine	-	Arabidopsis thaliana	UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]	-	ir	419221	
2.3.1.191	(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine	the LpxD1 enzyme adds a 3-OH C18 acyl group at 37 °C (host), whereas the LpxD2 enzyme adds a 3-OH C16 acyl group at 18 °C (environment)	Francisella tularensis subsp. novicida	UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]	-	ir	419221