N-acetylglucosamine-1-phosphate uridyltransferase
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3D structures of GlmU
Updated on 29-December-2020
FunctionN-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].) RelevanceGlmU 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 highlightsThe 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]. Surface representation of the uracil binding pocket.
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Updated on 29-December-2020
This page was last modified 15:20, 29 December 2020.