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Literature summary extracted from

  • Williams, A.H.; Immormino, R.M.; Gewirth, D.T.; Raetz, C.R.
    Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide (2006), Proc. Natl. Acad. Sci. USA, 103, 10877-10882.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.3.1.129 drug development the enzyme is a target for design of inhibitors with antibiotic potency Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.129 purified enzyme LpxA in a complex with inhibitor peptide 920, 20 mg/ml protein in solution with a 25fold molar excess of peptide 920 of 12.5 mM, crystal growth at 18°C, hanging drop vapor diffusion method, mixing of 0.002 ml protein solution with 0.002 ml of 0.8–1.8 M phosphate buffer, pH 6.3–6.9, and 30-35% DMSO, about 2 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using crystal structure PDB ID code 1LXA, determined at 2.6 A resolution Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.129 peptide 920 pentadecapeptide NH2-SSGWMLDPIAGKWSR-COOH, the enzyme binds peptide 920 with three peptides, each of which adopts a beta-hairpin conformation, bound per LpxA trimer, the peptides are located at the interfaces of adjacent subunits in the vicinity of the three active sites, each peptide interacts with residues from both adjacent subunits, noncovalent interaction and binding structure, overview Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.129 0.005
-
 (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] pH 8.0, 30°C 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 LpxA is essential for the growth of Escherichia coli, and is important in lipid A biosynthesis, overview [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 gene lpxA
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.129 (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine LpxA is essential for the growth of Escherichia coli, and is important in lipid A biosynthesis, 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 i.e. (R)-3-hydroxymyristoyl-[acyl-carrier protein], the enzyme catalyzes the first step of lipid A biosynthesis, the transfer of the (R)-3-hydroxyacyl chain from (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] to the glucosamine 3-OH group of UDP-GlcNAc Escherichia coli [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.129 trimer homotrimer, LpxA contains an unusual, left-handed parallel beta-helix fold, crystal structure analysis 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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.129 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.129 8
-
 assay at Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.129 additional information
-
 additional information inhibition kinetics Escherichia coli
2.3.1.129 0.00005
-
 peptide 920 pH 8.0, 30°C Escherichia coli