dTDP-4-amino-4,6-dideoxygalactose transaminase (WecE) (WecE)

WecE, also known as dTDP-4-amino-4,6-dideoxygalactose transaminase, is a bacterial enzyme that plays a vital role in the biosynthesis of the Enterobacterial Common Antigen (ECA) [5, 21]. ECA is a conserved carbohydrate antigen found on the outer membrane of all members of the Enterobacterales order, including pathogens such as Escherichia coli, Salmonella, and Yersinia [3, 5]. WecE is a pyridoxal phosphate (PLP)-dependent aminotransferase that catalyzes the conversion of a keto-sugar precursor into an amino-sugar intermediate, which is subsequently incorporated into the ECA trisaccharide repeat unit [21, 27]. This enzyme is considered a promising target for the development of novel antibacterial agents because ECA is essential for bacterial fitness, outer membrane integrity, and resistance to host-derived stressors like bile salts [25, 31]. Inhibition of WecE leads to the accumulation of toxic lipid-linked intermediates and the depletion of the undecaprenyl phosphate lipid carrier, which disrupts cell wall homeostasis and reduces bacterial virulence [25, 33]. Although no drugs targeting WecE are currently approved for clinical use, its role in maintaining bacterial pathogenicity makes it a significant focus for antimicrobial research [31, 35]. Additionally, WecE has been explored in biotechnology for the green synthesis of amino-sugar derivatives like valienamine, a glucosidase inhibitor [32, 34].

Other names

wecEUDP-4-amino-4,6-dideoxy-D-glucose aminotransferaseTDP-4-keto-6-deoxy-D-glucose transaminaseSugar aminotransferase WecEdTDP-4-amino-4,6-dideoxy-D-galactose:2-oxoglutarate aminotransferase

Inhibition of Enterobacterial Common Antigen (ECA) biosynthesis