Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a promising target for antibacterial drug development, structure-guided drug discovery of broad spectrum Gram-negative antibiotics | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
purified enzyme mutant C125S in complex with product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine, hanging-drop vapor diffusion, mixing of 12 mg/ml protein in 20 mM HEPES, pH 7.0, 50 mM NaCl, and 0.5 mM zinc sulfate, with reservori solution containing 0.4 M NaH2PO4, 0.8 M K2HPO4, 0.2 M CAPS, pH 10.5, 50mM Li2SO4, 20°C, 3 days, X-ray diffraction structure determination and analysis at 2.59 A resolution, modeling | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
C125S | site-directed mutagenesis, crystal structure analysis | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(2R)-N-hydroxy-2-[(naphthalene-2-sulfonyl)methyl]-3-(naphthalen-2-yl)propanamide | - |
Escherichia coli | |
1,5-anhydro-2-deoxy-2-[(2Z)-2-hydroxy-2-(hydroxyimino)ethyl]-3-O-tetradecanoyl-L-mannitol | - |
Escherichia coli | |
additional information | structure-guided drug discovery of broad spectrum Gram-negative antibiotics, overview | Escherichia coli | |
N-[(2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl]-4-(4-phenylbuta-1,3-diyn-1-yl)benzamide | - |
Escherichia coli | |
N-[(2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl]-4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)benzamide | - |
Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | metal-dependent enzyme | Escherichia coli | |
Zn2+ | catalytic Zn2+ | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O | Escherichia coli | - |
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene lpxC | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | analysis of recognition of substrates and products by the enzyme, phosphate binding is stabilized by the catalytic Zn2+ and an extensive network of hydrogen bonds to key active site residues and myr-UDP-GlcN, overview | Escherichia coli | ? | - |
? | |
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O | - |
Escherichia coli | UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate | - |
r | |
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O | via tetrahedral transition state | Escherichia coli | UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
LpxC | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | LpxC enzyme catalyzes the committed step of lipopolysaccharide biosynthesis | Escherichia coli |
physiological function | LpxC is a metal-dependent deacetylase essential for lipopolysaccharide biosynthesis | Escherichia coli |