N-acetylglucosamine-1-phosphate uridyltransferase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='2v0j' size='340' side='right' caption='GlmU complex with its reaction product UDP-GlcNAC, PEG, Mg++, So4, tetraethylene glycol and triethylene glycol (PDB code [[2v0j]])' scene=''> |
== Function == | == 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)(<ref>PMID:19237750</ref>.) | '''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)(<ref>PMID:19237750</ref>.) | ||
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| - | == Disease == | ||
== Relevance == | == Relevance == | ||
| - | GlmU is | + | 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<ref>PMID:3=18573680</ref>. |
== Structural highlights == | == Structural highlights == | ||
Revision as of 07:48, 13 April 2020
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3D structures of GlmU
Updated on 13-April-2020
References
- ↑ Zhang Z, Bulloch EM, Bunker RD, Baker EN, Squire CJ. Structure and function of GlmU from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr. 2009 Mar;65(Pt 3):275-83. Epub 2009, Feb 20. PMID:19237750 doi:10.1107/S0907444909001036
- ↑ PMID:3=18573680
