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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
2.3.1.157
701468
Structure and function of GlmU from Mycobacterium tuberculosis
Acta Crystallogr. Sect. D
65
275-283
2009
Mycobacterium tuberculosis H37Rv
19237750
2.3.1.157
706622
Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site
Protein Sci.
17
577-582
2008
Mycobacterium tuberculosis
18218712
2.3.1.157
701520
Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group
Acta Crystallogr. Sect. F
65
435-439
2009
Mycobacterium tuberculosis
19407371
2.3.1.157
701520
Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group
Acta Crystallogr. Sect. F
65
435-439
2009
Mycobacterium tuberculosis H37Rv
19407371
2.3.1.157
677026
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products
Protein Sci.
16
1230-1235
2007
Escherichia coli
17473010
2.3.1.157
643075
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
Biochemistry
40
1913-1921
2001
Escherichia coli
11329257
2.3.1.157
719411
Structure-based virtual screening of novel inhibitors of the uridyltransferase activity of Xanthomonas oryzae pv. oryzae GlmU
Eur. J. Med. Chem.
53
150-158
2012
Xanthomonas oryzae
22521370
2.3.1.157
720042
Substrate bound crystal structures reveal features unique to Mycobacterium tuberculosis N-acetyl-glucosamine-1-phosphate uridyltransferase and a catalytic mechanism for acetyltransfer
J. Biol. Chem.
287
39524-39537
2012
Mycobacterium tuberculosis
22969087
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