EC Number   |
Application |
Reference |
|---|
    2.7.7.38 | agriculture |
CMP-KDO synthetase inhibitors attract great interest owing to their potential as selective bactericides |
645234 |
| 2.7.7.38 | analysis |
adaptation of a simple colorimetric assay for diphosphate to the enzyme 3-deoxy-D-manno-octulosonate cytidylyltransferase. This assay can be combined with the malachite green assay for phosphate to form an assay system capable of determining phosphate and diphosphate in the same solution. The assay system has the potential for simultaneous screening of the 3-deoxy-D-manno-octulosonate biosynthesis pathway |
721274 |
| 2.7.7.38 | medicine |
- |
645238 |
| 2.7.7.38 | medicine |
essential for the biosynthesis of lipopolysaccharides in gram-negative bacteria, potential target for the discovery of antibacterial agents |
645236, 645239 |
| 2.7.7.38 | medicine |
exclusive pathogen of humans, cause of epidemic bacterial meningitis and sepsis, potential target for develpoment of antibiotic tools |
645237 |
| 2.7.7.38 | medicine |
kanamycin and fosfomycin show no inhibitory effect on the production and release of Vero toxins by Escherichia coli O157, both kanamycin and fosfomycin show the remarkable inhibition of Vero toxin 2 release through synergistic collaboration with CMP:KDO synthase inhibitor (1R,4S,5R)-3-[2-[(S)-1-((S)-1-carboxy-ethylcarbamoyl)-ethylamino]-ethyl]-4,5-dihydroxy-cyclohexanecarboxylic acid |
661340 |
| 2.7.7.38 | medicine |
KDO is not present in animals but is vital for gram-negative bacteria, suggests the possibility of using selective inhibition of its synthesis as antibacterial tool |
645238 |
| 2.7.7.38 | medicine |
the structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae in complex with 3-deoxy-manno-octulosonate will be useful in structure-based inhibitor design |
701461 |
