@article{open3098,
          volume = {175},
           month = {February},
          author = {Ramesh Nimma and Ajay Kumar and Zahid Gani and Anuj Gahlawat and Rahul Dilawari and Kumar Rajesh  Rohilla and Hemangi Kumbhar and Prabha Garg and Sidharth Chopra and Manoj Raje and Chaaya Iyengar Raje},
            note = {The copyright of this article belongs to Elsevier Science},
           title = {Characterization of the enzymatic and multifunctional properties of Acinetobacter baumannii erythrose-4-phosphate dehydrogenase (E4PDH)
},
       publisher = {Elsevier Science},
         journal = {Microbial pathogenesis},
            year = {2023},
        keywords = {Acinetobacter baumannii (A. baumannii); Erythrose-4-phosphate dehydrogenase (E4PDH); Iron; Protein multifunctionality; Vitamin B6.},
             url = {http://crdd.osdd.net/open/3098/},
        abstract = {Infections due to Acinetobacter baumannii (A. baumannii) are rapidly increasing worldwide and consequently therapeutic options for treatment are limited. The emergence of multi drug resistant (MDR) strains has rendered available antibiotics ineffective, necessitating the urgent discovery of new drugs and drug targets. The vitamin B6 biosynthetic pathway has been considered as a potential antibacterial drug target but it is as yet uncharacterized for A. baumannii. In the current work, we have carried out in silico and biochemical characterization of Erythrose-4-phosphate dehydrogenase (E4PDH) (EC 1.2.1.72). This enzyme catalyzes the first step in the deoxyxylulose-5-phosphate (DXP) dependent Vitamin B6 biosynthetic pathway i.e. the conversion of d-erythrose-4-phosphate (E4P) to 4-Phosphoerythronate. E4PDH also possesses an additional activity whereby it can catalyze the conversion of Glyceraldehyde-3-phosphate (G3P) to 1,3 bisphosphoglycerate (1,3BPG). Our studies have revealed that this enzyme exhibits an alternate moonlighting function as a cell surface receptor for the human iron transport proteins transferrin (Tf) and lactoferrin (Lf). The present work reports the internalization of Tf and consequent iron acquisition as an alternate strategy for iron acquisition. Given its essential role in two crucial pathways i.e. metabolism and iron acquisition, A. baumannii E4PDH may play a vital role in bacterial pathogenesis.

}
}