2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18573680&form=6&db=m	Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase.	causal interaction,ongoing research,therapeutic application,unassigned	3,2,4,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18765909&form=6&db=m	Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosis.	ongoing research,therapeutic application,unassigned	3,1,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19121323&form=6&db=m	PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity.	ongoing research,therapeutic application,unassigned	2,1,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19407371&form=6&db=m	Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.	ongoing research,unassigned	2,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22669463&form=6&db=m	Identification of amino acids involved in catalytic process of M. tuberculosis GlmU acetyltransferase.	ongoing research,therapeutic application,unassigned	2,1,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24158720&form=6&db=m	Inhibition studies on Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).	ongoing research,therapeutic application,unassigned	2,2,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26078037&form=6&db=m	Structure-based design of diverse inhibitors of Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase: combined molecular docking, dynamic simulation, and biological activity.	therapeutic application,unassigned	1,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26690048&form=6&db=m	UDP-GlcNAc pathway: Potential target for inhibitor discovery against M. tuberculosis.	ongoing research,unassigned	1,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26829648&form=6&db=m	Mycobacterium tuberculosis AtsG (Rv0296c), GlmU (Rv1018c) and SahH (Rv3248c) Proteins Function as the Human IL-8-Binding Effectors and Contribute to Pathogen Entry into Human Neutrophils.	diagnostic usage,unassigned	3,0	
2.3.1.157	Tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31380295&form=6&db=m	The Inhibitory Effect of GlmU Acetyltransferase Inhibitor TPSA on Mycobacterium tuberculosis May Be Affected Due to Its Methylation by Methyltransferase Rv0560c.	causal interaction,unassigned	1,0