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Literature summary for 2.3.1.129 extracted from

  • Joo, S.H.; Chung, H.S.
    Crystal structure and activity of Francisella novicida UDP-N-acetylglucosamine acyltransferase (2016), Biochem. Biophys. Res. Commun., 478, 1223-1229 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.129

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Francisella tularensis subsp. novicida

Crystallization (Commentary)

Crystallization (Comment) Organism
structure to 2.06 A resolution. The supposed ruler residues for hydrocarbon length, L171 in one monomer and H168 in the adjacent monomer in a functional trimer of LpxA, are located just 3.8 A apart that renders not enough space for binding of 3-OH-laurate or longer acyl chains Francisella tularensis subsp. novicida

Organism

Organism UniProt Comment Textmining
Francisella tularensis subsp. novicida
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0021
-
 pH 7.4, 30°C Francisella tularensis subsp. novicida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
R,S-3-hydroxypalmitoyl-ACP + UDP-N-acetyl-alpha-D-glucosamine
-
 Francisella tularensis subsp. novicida ACP + UDP-3-O-(3-hydroxypalmitoyl)-N-acetyl-alpha-D-glucosamine
-
 ?

Synonyms

Synonyms Comment Organism
LpxA
-
 Francisella tularensis subsp. novicida

General Information

General Information Comment Organism
physiological function Francisella novicida LpxA functionally complements an Escherichia coli LpxA knockout mutant and efficiently transfers 3-OH-myristoylate as well as 3-OH-palmitate in Echerichia coli. The acyl chain length of lipid A is determined by several factors including acyl chain selectivity of LpxA and downstream enzymes, as well as the composition of the acyl-ACP pool in vivo Francisella tularensis subsp. novicida