Literature summary for 2.3.1.191 extracted from

Li, Y.; Powell, D.A.; Shaffer, S.A.; Rasko, D.A.; Pelletier, M.R.; Leszyk, J.D.; Scott, A.J.; Masoudi, A.; Goodlett, D.R.; Wang, X.; Raetz, C.R.; Ernst, R.K.
LPS remodeling is an evolved survival strategy for bacteria (2012), Proc. Natl. Acad. Sci. USA, 109, 8716-8721.

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Cloned(Commentary)

Cloned (Comment)	Organism
genes lpxD1 and lpxD2, DNA and amino acid sequence determination and analysis, phyylogenetic analysis, the lpxD1gene lies within an essential four-gene operon, lpxD1/fabZ/lpxA/lpxB, while the second gene lpxD2 as a single gene is predicted to be regulated by its own promoter	Francisella tularensis subsp. novicida

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of lpxD1-null and lpxD2-null mutant strains, that show altered antibiotic susceptibility patterns, membrane permeability, but no innate immune responses	Francisella tularensis subsp. novicida

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(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
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine	Francisella tularensis subsp. novicida U112	-	UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]	-	ir

Organism

Organism	UniProt	Comment	Textmining
Francisella tularensis subsp. novicida	-	genes lpxD1 and lpxD2	-
Francisella tularensis subsp. novicida U112	-	genes lpxD1 and lpxD2	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
cell culture	growth temperatures of 18°C to 37°C	Francisella tularensis subsp. novicida	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(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
(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
(3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine	-	Francisella tularensis subsp. novicida U112	UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]	-	ir
(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 U112	UDP-2,3-bis[O-(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + a holo-[acyl-carrier protein]	-	ir

Synonyms

Synonyms	Comment	Organism
LpxD	-	Francisella tularensis subsp. novicida
LpxD1	-	Francisella tularensis subsp. novicida
Lpxd2	-	Francisella tularensis subsp. novicida

General Information

General Information	Comment	Organism
malfunction	the lpxD1-null mutant is attenuated in C57BL/6 mice and subsequently exhibits protection against a lethal wild-type challenge. The lpxD1-null and lpxD2-null mutant strains show altered antibiotic susceptibility patterns, membrane permeability, but no innate immune responses. The DELTAlpxD1 mutant is more susceptible to antibiotics with diverse mechanisms of action such as chloramphenicol, carbenicillin, ciprofloxacin, erythromycin, rifampin, and vancomycin, whereas the DELTAlpxD2 mutant is only susceptible to carbenicillin and erythromycin	Francisella tularensis subsp. novicida
metabolism	Francisella modifies its lipid A structure in response to temperature adaptation by altering the length of the amidelinked acyl chains: 3-OH-C16 at environmental temperature and 3-OH-C18 at mammalian temperature	Francisella tularensis subsp. novicida
physiological function	functional LpxD is essential for bacterial viability, transcriptional control of the lpxD genes, encoding the lipid A-modifying N-acyltransferase enzymes LpxD1/2,and posttranslational control of the LpxD1 and LpxD2 enzymatic activities are involved in the mechanism for temperature-regulated membrane remodeling by LPS/lipid A-level modifications resulting in alterations of membrane fluidity, as well as integrity, that may represent a general paradigm for bacterial membrane adaptation and virulence-state adaptation	Francisella tularensis subsp. novicida

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Release 2023.1 (January 2023)