Literature summary for 2.3.1.191 extracted from

Bainbridge, B.W.; Karimi-Naser, L.; Reife, R.; Blethen, F.; Ernst, R.K.; Darveau, R.P.
Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis (2008), J. Bacteriol., 190, 4549-4558.

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Cloned(Commentary)

Cloned (Comment)	Organism
lpxA (lpxAPg) and lpxDPg are cloned and expressed in Escherichia coli strains in which the homologous gene is mutated. Lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity	Escherichia coli
lpxA (lpxAPg) and lpxDPg are cloned and expressed in Escherichia coli strains in which the homologous gene is mutated. Lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity	Porphyromonas gingivalis

Cloned (Comment)

Organism

lpxA (lpxAPg) and lpxDPg are cloned and expressed in Escherichia coli strains in which the homologous gene is mutated. Lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity

Escherichia coli

Porphyromonas gingivalis

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Porphyromonas gingivalis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	both LpxA and LpxD, from Escherichia coli are also able to incorporate odd-chain fatty acids into lipid A when grown in the presence of 1% propionic acid. When grown on 1% propionic acid lipid A also contains the odd-chain fatty acids tridecanoic acid (C13), pentadecanoic acid (C15), hydroxy tridecanoic acid (C13OH), and hydroxy pentadecanoic acid (C15OH). Escherichia coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available	Escherichia coli	?	-	?
additional information	lipid A from strains expressing either of the Porphyromonas gingivalis transferases contains 16-carbon hydroxy fatty acids in addition to the normal Escherichia coli 14-carbon hydroxy fatty acids, demonstrating that these acyltransferases display a relaxed acyl chain length specificity. Both LpxA and LpxD, from either Escherichia coli or Porphyromonas gingivalis are also able to incorporate odd-chain fatty acids into lipid A when grown in the presence of 1% propionic acid. The relaxed specificity of the Porphyromonas gingivalis lipid A acyltransferases and the substrate availability account for the lipid A structural clusters that differ by 14 mass units observed in Porphyromonas gingivalis lipopolysaccharide preparations	Porphyromonas gingivalis	?	-	?

Synonyms

Synonyms	Comment	Organism
acyltransferase LpxD	-	Escherichia coli
acyltransferase LpxD	-	Porphyromonas gingivalis