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Literature summary for 2.3.1.129 extracted from

  • Jenkins, R.J.; Dotson, G.D.
    Dual targeting antibacterial peptide inhibitor of early lipid a biosynthesis (2012), ACS Chem. Biol., 7, 1170-1177.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.129

Application

Application Comment Organism
drug development development of small molecule, dual-binding LpxA/LpxD inhibitors as novel antimicrobials Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expresssion Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
FITC-P920 i.e. FITC-(beta)SSGWMLDPIAGKWSRNH2, fluoresecent-labeled peptide Escherichia coli
additional information measurement of binding of fluorescein-labeled peptide to acyltransferase by measuring the changes in fluorescence polarization, KD values, overview. No inhibition of LpxA by SENNFMLPLLPL-NH2, i.e. peptide RJPXD34 Escherichia coli
P920 i.e. SSGWMLDPIAGKWSR Escherichia coli
RJPXD31 i.e. QHFMVPDINDMQ-NH2 Escherichia coli
RJPXD33 i.e. TNLYMLPKWDIP-NH2, a peptide identified from a phage-bound random peptide library screen uing Escherichia oli strain XL-1 Blue, binds to UDP-3-O-(R-3-hydroxyacyl)GlcN N-acyltransferase, LpxD, and UDP-N-acetylglucosamine acyltransferase, LpxA. RJPXD33 binds to LpxA in a competitive fashion with P920 Escherichia coli

Organism

Organism UniProt Comment Textmining
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
7.5
-
 activity assay at Escherichia coli
8
-
 binding assay at Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.019
-
 pH 7.5, 30°C Escherichia coli RJPXD33

General Information

General Information Comment Organism
metabolism acyltransferases LpxA and LpxD catalyze functionally similar acylations of their respective UDP-glucosamine-based substrates using R-3-hydroxymyristoyl-ACP as the acyl donor in the Kdo2-lipid A biosynthesis in Escherichia coli Escherichia coli