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 | Comment | Organism | Structure |
---|---|---|---|
peptide 920 | a pentadecapeptide | Escherichia coli |
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 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A722 | - |
- |
Escherichia coli | P0A722 | gene lpxA | - |
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 | 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 | - |
? | |
(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 | - |
? | |
(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 | - |
? | |
(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 | - |
? | |
additional information | nucleotide substrate recognition by LpxA, overview | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
trimer | - |
Escherichia coli |
trimer | homotrimer, the active site lies within a positively charged cleft formed at the subunit-subunit interface | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
LpxA | - |
Escherichia coli |
UDP-N-acetylglucosamine acyltransferase | - |
Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00005 | - |
peptide 920 | peptide 920 disrupts LpxA interactions with the R-3-hydroxymyristoyl-ACP substrate | Escherichia coli |