Literature summary for 2.3.1.191 extracted from

Bartling, C.M.; Raetz, C.R.
Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis (2009), Biochemistry, 48, 8672-8683.

Search for more literature for 2.3.1.191

Cloned(Commentary)

Cloned (Comment)	Organism
LpxD protein modified with an N-terminal His6 tag followed by a one glycine residue linker and the P2A substitution, is constructed and transformed into Escherichia coli Rosetta (DE3)/pLysS	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop/vapor diffusion method. The crystal structure of N-terminally His6-tagged EcLpxD is determined by molecular replacement at 2.6 A resolution, using Chlamydia trachomatis (PDB code: 2IUA) as the model. Comparison of LpxD from Escherichia coli and Chlamydia trachomatis. Attempts to crystallize EcLpxD with UDP-GlcNAc, UDP-3-O-(R-3-hydroxymyristoyl)-R-D-GlcNAc or its product UDP-2,3-diacylglucosamine are unsuccessful	Escherichia coli

Crystallization (Comment)

Organism

hanging drop/vapor diffusion method. The crystal structure of N-terminally His6-tagged EcLpxD is determined by molecular replacement at 2.6 A resolution, using Chlamydia trachomatis (PDB code: 2IUA) as the model. Comparison of LpxD from Escherichia coli and Chlamydia trachomatis. Attempts to crystallize EcLpxD with UDP-GlcNAc, UDP-3-O-(R-3-hydroxymyristoyl)-R-D-GlcNAc or its product UDP-2,3-diacylglucosamine are unsuccessful

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
M290A	wild-type EcLpxD prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 3, whereas the M290A mutant has the opposite selectivity. Both wild-type and M290A EcLpxD rescue the conditional lethality of Escherichia coli RL25, a temperature-sensitive strain harboring point mutations in lpxD. Complementation with wild-type EcLpxD restores normal lipid A containing only N-linked hydroxymyristate to RL25 at 42°C, as judged by mass spectrometry, whereas the M290A mutant generates multiple lipid A species containing one or two longer hydroxy fatty acids in place of the usual (3R)-3-hydroxymyristate at positions 2 and 20	Escherichia coli
M292A	wild-type EcLpxD prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 3, mutant enzyme M292A prefers (R,S)-3-hydroxymyristoyl-ACP over (R,S)-3-hydroxypalmitoyl-ACP by a factor of 2.5	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P21645	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(R,S)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine	wild-type LpxD prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] by a factor of 3, whereas the M290A mutant has the opposite selectivity	Escherichia coli	UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]	-	?
(R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine	wild-type LpxD prefers (R,S)-3-hydroxymyristoyl-[acyl-carrier protein] over (R,S)-3-hydroxypalmitoyl-[acyl-carrier protein] by a factor of 3, whereas the M290A mutant has the opposite selectivity	Escherichia coli	UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]	-	?

Synonyms

Synonyms	Comment	Organism
EcLpxD	-	Escherichia coli
LpxD	-	Escherichia coli