N-acetylglucosamine-1-phosphate uridyltransferase

Function

N-acetylglucosamine-1-phosphate uridyltransferase (GlmU} or bifunctional protein GlmU is a bifunctional acetyltransferase/uridyltransferase that catalyzes the formation of UDP-GlcNAc from glucosamine-1-phosphate (G1P)(^[1].)

Relevance

GlmU is essensial enzyme participating in the biosynthetic pathway for production of peptidoglycans which constitute the mycobacterial cell wall. Hence the inhibition of GlmU is a potential anti-tuberculosis drug target^[2].

Structural highlights

The UDP-GlcNAc binds to GlmU in the enzyme's N-terminal domain and the majority of the key active site residues are highly conserved across the bacterial GlmU family. The 3D structure of the complex shows an exposed uracil binding pocket, GlcNAc interacting pocket and a lipophilic pocket ^[3].