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 , GlcNAc interacting pocket and a lipophilic pocket ^[3]. .