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Literature summary for 2.3.1.129 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)

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

Inhibitors

Inhibitors Comment Organism Structure
peptide 920 a pentadecapeptide Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(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
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Organism

Organism UniProt Comment Textmining
Escherichia coli P0A722
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Escherichia coli P0A722 gene lpxA
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Reaction

Reaction Comment Organism Reaction ID
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 (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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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
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(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
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?
(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
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(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
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additional information nucleotide substrate recognition by LpxA, overview Escherichia coli ?
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Subunits

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

Synonyms

Synonyms Comment Organism
LpxA
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Escherichia coli
UDP-N-acetylglucosamine acyltransferase
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Escherichia coli

Ki Value [mM]

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