EC Number   |
Title |
Organism |
|---|
    3.6.1.54 | Crystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosa |
Pseudomonas aeruginosa |
| 3.6.1.54 | Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis |
Haemophilus influenzae |
| 3.6.1.54 | Structure-activity relationship of sulfonyl piperazine LpxH inhibitors analyzed by an LpxE-coupled malachite green assay |
Escherichia coli |
| 3.6.1.54 | Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A |
Neisseria meningitidis |
| 3.6.1.54 | The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release |
Escherichia coli |
| 3.6.1.54 | Toxic accumulation of lps pathway intermediates underlies the requirement of LpxH for growth of acinetobacter Baumannii ATCC 19606 |
Acinetobacter baumannii |
| 3.6.1.54 | Toxic accumulation of lps pathway intermediates underlies the requirement of LpxH for growth of acinetobacter Baumannii ATCC 19606 |
Acinetobacter baumannii ATCC 19606 |
| 3.6.1.54 | Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene |
Escherichia coli |
| 3.6.1.54 | Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene |
Pseudomonas aeruginosa |
| 3.6.1.54 | An alternative route for UDP-diacylglucosamine hydrolysis in bacterial lipid A biosynthesis |
Caulobacter vibrioides |
