Activating Compound | Comment | Organism | Structure |
---|---|---|---|
bovine serum albumin | addition of bovine serum albumin slightly increases activity | Escherichia coli |
Application | Comment | Organism |
---|---|---|
medicine | LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(4R)-2-(3,4-dimethoxy-5-propylphenyl)-N-hydroxy-4,5-dihydro-1,3-oxazole-4-carboxamide | i.e L-161,240 | Escherichia coli | |
(4R)-N-hydroxy-2-(4-methoxyphenyl)-4,5-dihydro-1,3-oxazole-4-carboxamide | i.e. L-159,692 | Escherichia coli | |
EDTA | 5 mM, complete loss of activity | Escherichia coli | |
Zn2+ | 0.1 mM, about 65% loss of activity | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.367 | - |
UDP-(2-acetamino)-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose | pH 6.0, 30°C | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | 0.1 mM, significantly enhances activity | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | Escherichia coli | LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UD-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-(2-acetamino)-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose + H2O | a homogenous fluorescence-based assay is developed that uses UDP3-O-(N-hexyl-propionamide)-N-acetylglucosamine as a surrogate substrate. This surrogate can be prepared from commercially available UDP-GlcNAc by enzymatic conversion to UDP-MurNAc, which is then chemically coupled to n-hexylamine. Following the LpxC reaction, the free amine of the deacetylation product can be derivatized by fluorescamine, thus generating a fluorescent signal | Escherichia coli | UDP-2-amino-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose + acetate | - |
? | |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | - |
Escherichia coli | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
? | |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UD-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery | Escherichia coli | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
? | |
UDP-3-O-(N-hexyl-propionamide)-N-acetylglucosamine + H2O | - |
Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LpxC enzyme | - |
Escherichia coli |
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.36 | - |
UDP-3-O-(N-hexyl-propionamide)-N-acetylglucosamine | pH 6.0, 30°C | Escherichia coli |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
26 | - |
pH 6.0, 30°C, substrate: UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | Escherichia coli | (4R)-2-(3,4-dimethoxy-5-propylphenyl)-N-hydroxy-4,5-dihydro-1,3-oxazole-4-carboxamide | |
75 | - |
pH 6.0, 30°C, substrate: UDP3-O-(N-hexyl-propionamide)-N-acetylglucosamine | Escherichia coli | (4R)-2-(3,4-dimethoxy-5-propylphenyl)-N-hydroxy-4,5-dihydro-1,3-oxazole-4-carboxamide | |
2500 | - |
pH 6.0, 30°C, substrate: UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine | Escherichia coli | (4R)-N-hydroxy-2-(4-methoxyphenyl)-4,5-dihydro-1,3-oxazole-4-carboxamide | |
2600 | - |
pH 6.0, 30°C, substrate: UDP3-O-(N-hexyl-propionamide)-N-acetylglucosamine | Escherichia coli | (4R)-N-hydroxy-2-(4-methoxyphenyl)-4,5-dihydro-1,3-oxazole-4-carboxamide |
General Information | Comment | Organism |
---|---|---|
physiological function | LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.98 | - |
UDP-(2-acetamino)-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose | pH 6.0, 30°C | Escherichia coli |