Application | Comment | Organism |
---|---|---|
drug development | LpxC is a target for the development of antimicrobial agents in the treatment of Gram negative infections | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D197A | site-directed mutagenesis | Escherichia coli |
D197E | site-directed mutagenesis | Escherichia coli |
F192A | site-directed mutagenesis | Escherichia coli |
H19A | site-directed mutagenesis | Escherichia coli |
H19Q | site-directed mutagenesis | Escherichia coli |
H19Y | site-directed mutagenesis | Escherichia coli |
K143A | site-directed mutagenesis | Escherichia coli |
K239A | site-directed mutagenesis | Escherichia coli |
N162A | site-directed mutagenesis | Escherichia coli |
T191A | site-directed mutagenesis | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00019 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | wild-type | Escherichia coli | |
0.0005 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | F192A mutant | Escherichia coli | |
0.0008 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | D197E mutant | Escherichia coli | |
0.0008 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | K239A mutant | Escherichia coli | |
0.0011 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | D197A mutant | Escherichia coli | |
0.0013 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19A mutant | Escherichia coli | |
0.0016 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | T191A mutant | Escherichia coli | |
0.0024 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19Q mutant | Escherichia coli | |
0.011 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19Y mutant | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | metal-dependent deacetylase | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | catalyzes the second step in the biosynthesis of lipid A | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | catalyzes the second step in the biosynthesis of lipid A | Escherichia coli | ? | - |
? | |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | - |
Escherichia coli | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LpxC | - |
Escherichia coli |
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.01 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | K239A mutant | Escherichia coli | |
0.017 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19A mutant | Escherichia coli | |
0.052 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | F192A mutant | Escherichia coli | |
0.053 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | T191A mutant | Escherichia coli | |
0.13 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19Q mutant | Escherichia coli | |
0.25 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19Y mutant | Escherichia coli | |
1.32 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | D197E mutant | Escherichia coli | |
1.5 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | wild-type | Escherichia coli | |
1.5 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | D197A mutant | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
affinity of EcLpxC for the product (myrUDP-GlcNH2) is determined as a function of pH to ascertain whether there are ionizations important for binding affinity. For wild-type LpxC, the KD product value increases at both low and high pH in a log-linear fashion, indicating that two ionizations affect binding affinity | Escherichia coli |
7.5 | - |
assay at | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.31 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19A mutant, 575fold decrease | Escherichia coli | |
12.5 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | K239A mutant, 575fold decrease | Escherichia coli | |
22.73 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19Y mutant, 350fold decrease | Escherichia coli | |
33.13 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | K143A mutant, 700fold decrease | Escherichia coli | |
54.17 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | H19Q mutant, 135fold decrease | Escherichia coli | |
104 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | F192A mutant, 1200fold decrease | Escherichia coli | |
1364 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | D197A mutant, 5fold decrease | Escherichia coli | |
1650 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | D197E mutant, 5fold decrease | Escherichia coli | |
7895 | - |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | wild-type | Escherichia coli |