**Acknowledgements**

biosynthesis in some bacteria and has been recognized as an antibacterial drug target. A succinylphosphonate ester, 4‐(methoxyoxidophosphoryl)‐4‐oxobutanoate (**8**) was reported to be a competitive inhibitor of MenD (Ki values ∼700 nM) [35]. An analog of the cofactor, thiamine diphosphate, oxythiamine **9** was reported to exhibit MenD enzyme and *S. aureus*

MenE (*o*‐succinylbenzoate‐CoA synthetase) is an essential adenylate‐forming enzyme that is also a promising target for development of novel antibiotics in the menaquinone biosynthesis. Adenosylsulfonamide, adenosylsulfamate, and adenosylsulfamide analogs **10**, **11**, and **12** were developed as inhibitors of MenE enzymes based on the structure of *o*‐succinylbenzoate‐CoA. The vinyl sulfonamide **10** was found to be the most potent MenE inhibitor (IC50 ∼ 5.7 μM against *M. tuberculosis* MenE) [37]. The vinyl sulfonamide **10** is a competitive inhibitor of *M. tuberculosis* MenE with respect to Adenosine triphosphate (ATP) (Ki = 5.4 ± 0.1 nM) (**Figure 8**).

Bacterial Adenosine triphosphate (ATP) synthase, F1F0‐ATPase, is a viable target for treatment of *M. tuberculosis* infections. Diarylquinolone, an inhibitor of *M. tuberculosis* Adenosine triphosphate (ATP) synthase exhibited a remarkable activity against *Mycobacterium* spp. Electron transport systems associated with Adenosine triphosphate (ATP) synthases are

growth inhibitory activities (**Figure 7**) [36].

290 Vitamin K2 - Vital for Health and Wellbeing

**Figure 7.** MenD inhibitors.

**7.4. MenE inhibitors**

**Figure 8.** MenE inhibitors.

**8. Conclusion**

I thank CORNET award (University of Tennessee Health Science Center) for generous financial support.
