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Literature summary extracted from

  • Ulaganathan, V.; Buetow, L.; Hunter, W.N.
    Nucleotide substrate recognition by UDP-N-acetylglucosamine acyltransferase (LpxA) in the first step of lipid A biosynthesis (2007), J. Mol. Biol., 369, 305-312.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.129 by the sitting-drop, vapour-diffusion method using 0.00l ml of protein solution Escherichia coli
2.3.1.129 LpxA in complex with UDP-GlcNAc, modelling Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.129 peptide 920 a pentadecapeptide Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.129 (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine Escherichia coli the enzyme is responsible for the first step of lipid A biosynthesis, lipid A is an integral component of the lipopolysaccharide that forms the selective and protective outer monolayer of Gram-negative bacteria, and is essential for bacterial growth and viability [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.129 Escherichia coli P0A722
-
-
2.3.1.129 Escherichia coli P0A722 gene lpxA
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.129 a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine = an [acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine reaction mechanism, acylation occurs via nucleophilic attack of deprotonated UDP-GlcNAc on the acyl donor in a general base-catalyzed mechanism involving a catalytic dyad of His125 and Asp126, His125, the general base, interacts with the 3'-hydroxyl group of UDP-GlcNAc to generate the nucleophile, the Asp126 side-chain accepts a hydrogen bond from His125 and helps orient the general base to participate in catalysis Escherichia coli
a
2.3.1.129 a (3R)-3-hydroxyacyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine = an [acyl-carrier protein] + a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine reaction mechanism, acylation occurs via nucleophilic attack of deprotonated UDP-GlcNAc on the acyl donor in a general base-catalyzed mechanism involving a catalytic dyad of His125 and Asp126, His125, the general base, interacts with the 3'-hydroxyl group of UDP-GlcNAc to generate the nucleophile, the Asp126 side-chain accepts a hydrogen bond from His125 and helps orientate the general base to participate in catalysis Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.129 (R)-3-hydroxymyristoyl-[acyl carrier protein] + UDP-N-acetylglucosamine first step in lipid A biosynthesis Escherichia coli [acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
-
 ?
2.3.1.129 (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine the enzyme is responsible for the first step of lipid A biosynthesis, lipid A is an integral component of the lipopolysaccharide that forms the selective and protective outer monolayer of Gram-negative bacteria, and is essential for bacterial growth and viability Escherichia coli [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
-
 ?
2.3.1.129 (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine substrate binding site structure with prominent hydrophilic interactions between highly conserved clusters of residues Asn198, Glu200, Arg204 and Arg205 with UDP, and Asp74, His125, His144 and Gln161 with the GlcNAc moiety, these interactions serve to bind and orient the substrate for catalysis, overview Escherichia coli [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
-
 ?
2.3.1.129 (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine substrate binding site structure with prominent hydrophilic interactions between highly conserved clusters of residues Asn198, Glu200, Arg204 and Arg205 with UDP, and Asp74, His125, His144 and Gln161 with the GlcNAc moiety, these interactions serve to bind and orientate the substrate for catalysis, overview Escherichia coli [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
-
 ?
2.3.1.129 additional information nucleotide substrate recognition by LpxA, overview Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.129 trimer
-
 Escherichia coli
2.3.1.129 trimer homotrimer, the active site lies within a positively charged cleft formed at the subunit-subunit interface Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.3.1.129 LpxA
-
 Escherichia coli
2.3.1.129 UDP-N-acetylglucosamine acyltransferase
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.129 0.00005
-
 peptide 920 peptide 920 disrupts LpxA interactions with the R-3-hydroxymyristoyl-ACP substrate Escherichia coli