Application | Comment | Organism |
---|---|---|
drug development | development of small molecule, dual-binding LpxA/LpxD inhibitors as novel antimicrobials | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
recombinant expresssion | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
LpxA | - |
Escherichia coli |
UDP-N-acetylglucosamine acyltransferase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
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 Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.019 | - |
pH 7.5, 30°C | Escherichia coli | RJPXD33 |
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 |