MOESM6 of Metabolic engineering of Corynebacterium glutamicum for enhanced production of 5-aminovaleric acid

Additional file 6: Table S2. Primers used in this study

Additional file 1: of Low-mass-ion discriminant equation (LOME) for ovarian cancer screening

More detailed information for individual samples. Table S1.Healthy Control Individuals Providing Sera for LMI Profiling. Table S2. Patients with OVC Providing Sera for LMI Profiling. Table S3. Patients with CRC Providing Sera for LMI Profiling. Table S4. Patients with GC Providing Sera for LMI Profiling. Table S5. Patients with BUT Providing Sera for LMI Profiling. Table S6. Patients with BOT Providing Sera for LMI Profiling. Table S7. Patients with PCL Providing Sera for LMI Profiling. Table S8. Patients with BRC Providing Sera for LMI Profiling. Table S9. Patients with BBT Providing Sera for LMI Profiling. Table S10. Patients with UCC Providing Sera for LMI Profiling. Table S11. Patients with EMC Providing Sera for LMI Profiling. (DOCX 145 kb

StructureActivity Relationship of Sulfonyl Piperazine LpxH Inhibitors Analyzed by an LpxE-Coupled Malachite Green Assay

The UDP-2,3-diacylglucosamine pyrophosphatase LpxH in the Raetz pathway of lipid A biosynthesis is an essential enzyme in the vast majority of Gram-negative pathogens and an excellent novel antibiotic target. The 32P-radioautographic thin-layer chromatography assay has been widely used for analysis of LpxH activity, but it is inconvenient for evaluation of a large number of LpxH inhibitors over an extended time period. Here, we report a coupled, nonradioactive LpxH assay that utilizes the recently discovered Aquifex aeolicus lipid A 1-phosphatase LpxE for quantitative removal of the 1-phosphate from lipid X, the product of the LpxH catalysis; the released inorganic phosphate is subsequently quantified by the colorimetric malachite green assay, allowing the monitoring of the LpxH catalysis. Using such a coupled enzymatic assay, we report the biochemical characterization of a series of sulfonyl piperazine LpxH inhibitors. Our analysis establishes a preliminary structure–activity relationship for this class of compounds and reveals a pharmacophore of two aromatic rings, two hydrophobic groups, and one hydrogen-bond acceptor. We expect that our findings will facilitate the development of more effective LpxH inhibitors as potential antibacterial agents