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Literature summary for 2.3.1.129 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
Search for more literature for 2.3.1.129

Application

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.005
-
 (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] pH 8.0, 30°C 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 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

Organism UniProt Comment Textmining
Escherichia coli P0A722 gene lpxA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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
-
 ?
(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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Ki Value [mM]

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