Reference on EC 2.3.1.157 - glucosamine-1-phosphate N-acetyltransferase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mengin-Lecreulx, D.; van Heijenoort, J.
Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis
J. Bacteriol.
176
5788-5795
1994
Bacillus subtilis, Escherichia coli, Escherichia coli JM83
Pompeo, F.; Van Heijenoort, J.; Mengin-Lecreulx, D.
Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes
J. Bacteriol.
180
4799-4803
1998
Bacillus subtilis, Escherichia coli, Neisseria gonorrhoeae, Escherichia coli JM83
Olsen, L.R.; Tian, Y.; Roderick, S.L.
Purification, crystallization and preliminary x-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase
Acta Crystallogr. Sect. D
57
296-297
2001
Escherichia coli
Pompeo, F.; Bourne, Y.; Van Heijenoort, J.; Fassy, F.; Mengin-Lecreulx, D.
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth
J. Biol. Chem.
276
3833-3839
2001
Escherichia coli, Escherichia coli JM83
Sulzenbacher, G.; Gal, L.; Peneff, C.; Fassy, F.; Bourne, Y.
Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture
J. Biol. Chem.
276
11844-11851
2001
Streptococcus pneumoniae (Q97R46), Streptococcus pneumoniae
Olsen, L.R.; Roderick, S.L.
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
Biochemistry
40
1913-1921
2001
Escherichia coli (P0ACC7)
Kostrewa, D.; D'Arcy, A.; Takacs, B.; Kamber, M.
Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution
J. Mol. Biol.
305
279-289
2001
Streptococcus pneumoniae (Q97R46), Streptococcus pneumoniae
Olsen, L.R.; Vetting, M.W.; Roderick, S.L.
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products
Protein Sci.
16
1230-1235
2007
Escherichia coli
Zhang, W.; Jones, V.C.; Scherman, M.S.; Mahapatra, S.; Crick, D.; Bhamidi, S.; Xin, Y.; McNeil, M.R.; Ma, Y.
Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase
Int. J. Biochem. Cell Biol.
40
2560-2571
2008
Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMN3), Mycobacterium tuberculosis H37Rv
Zhang, Z.; Bulloch, E.M.; Bunker, R.D.; Baker, E.N.; Squire, C.J.
Structure and function of GlmU from Mycobacterium tuberculosis
Acta Crystallogr. Sect. D
65
275-283
2009
Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis H37Rv (P9WMN3)
Verma, S.K.; Jaiswal, M.; Kumar, N.; Parikh, A.; Nandicoori, V.K.; Prakash, B.
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 (P9WMN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMN3)
Parikh, A.; Verma, S.K.; Khan, S.; Prakash, B.; Nandicoori, V.K.
PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity
J. Mol. Biol.
386
451-464
2009
Mycobacterium tuberculosis
Mochalkin, I.; Lightle, S.; Narasimhan, L.; Bornemeier, D.; Melnick, M.; Vanderroest, S.; McDowell, L.
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
Zhou, Y.; Xin, Y.; Sha, S.; Ma, Y.
Kinetic properties of Mycobacterium tuberculosis bifunctional GlmU
Arch. Microbiol.
193
751-757
2011
Mycobacterium tuberculosis
Green, O.M.; McKenzie, A.R.; Shapiro, A.B.; Otterbein, L.; Ni, H.; Patten, A.; Stokes, S.; Albert, R.; Kawatkar, S.; Breed, J.
Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1: Hit to lead evaluation of a novel arylsulfonamide series
Bioorg. Med. Chem. Lett.
22
1510-1519
2012
Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Staphylococcus aureus
Stokes, S.S.; Albert, R.; Buurman, E.T.; Andrews, B.; Shapiro, A.B.; Green, O.M.; McKenzie, A.R.; Otterbein, L.R.
Inhibitors of the acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridylyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 2: Optimization of physical properties leading to antibacterial aryl sulfonamides
Bioorg. Med. Chem. Lett.
22
7019-7023
2012
Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae
Rodriguez-Diaz, J.; Rubio-del-Campo, A.; Yebra, M.J.
Metabolic engineering of Lactobacillus casei for production of UDP-N-acetylglucosamine
Biotechnol. Bioeng.
109
1704-1712
2012
Lacticaseibacillus casei
Li, Y.; Zhou, Y.; Ma, Y.; Li, X.
Design and synthesis of novel cell wall inhibitors of Mycobacterium tuberculosis GlmM and GlmU
Carbohydr. Res.
346
1714-1720
2011
Mycobacterium tuberculosis
Min, J.; Lin, D.; Zhang, Q.; Zhang, J.; Yu, Z.
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
Zhou, Y.; Yu, W.; Zheng, Q.; Xin, Y.; Ma, Y.
Identification of amino acids involved in catalytic process of M. tuberculosis GlmU acetyltransferase
Glycoconj. J.
29
297-303
2012
Mycobacterium tuberculosis
Buurman, E.T.; Andrews, B.; Gao, N.; Hu, J.; Keating, T.A.; Lahiri, S.; Otterbein, L.R.; Patten, A.D.; Stokes, S.S.; Shapiro, A.B.
In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae
J. Biol. Chem.
286
40734-40742
2011
Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Staphylococcus aureus, Streptococcus pneumoniae NCTC 7466, Escherichia coli ATCC 27325, Haemophilus influenzae ATCC 51907, Staphylococcus aureus RN4220
Jagtap, P.K.; Soni, V.; Vithani, N.; Jhingan, G.D.; Bais, V.S.; Nandicoori, V.K.; Prakash, B.
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, Mycobacterium tuberculosis (P9WMN3)
Singh, V.K.; Das, K.; Seshadri, K.
Kinetic modelling of GlmU reactions - prioritization of reaction for therapeutic application
PLoS ONE
7
e43969
2012
Mycobacterium tuberculosis
Zhang, Z.; Akutsu, J.; Kawarabayasi, Y.
Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7
J. Bacteriol.
192
3287-3293
2010
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q975F9)
Zhang, Z.; Shimizu, Y.; Kawarabayasi, Y.
Characterization of the amino acid residues mediating the unique amino-sugar-1-phosphate acetyltransferase activity of the archaeal ST0452 protein
Extremophiles
19
417-427
2015
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7 (Q975F9), Sulfurisphaera tokodaii DSM 16993 / JCM 10545 / NBRC 100140 / 7 (Q975F9)
Vithani, N.; Bais, V.; Prakash, B.
GlmU (N-acetylglucosamine-1-phosphate uridyltransferase) bound to three magnesium ions and ATP at the active site
Acta Crystallogr. Sect. F
70
703-708
2014
Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis ATCC 25618 (P9WMN3)
Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU)
Appl. Microbiol. Biotechnol.
100
3071-3085
2015
Escherichia coli, Escherichia coli (P0ACC7), Haemophilus influenzae (P43889), Escherichia coli ATCC 25922, Escherichia coli ATCC 25922 (P0ACC7), Haemophilus influenzae ATCC 51907 (P43889)
Patin, D.; Bayliss, M.; Mengin-Lecreulx, D.; Oyston, P.; Blanot, D.
Purification and biochemical characterisation of GlmU from Yersinia pestis
Arch. Microbiol.
197
371-378
2015
Yersinia pestis, Yersinia pseudotuberculosis, Yersinia pseudotuberculosis YPIII, Yersinia pestis YPIII
Mehra, R.; Sharma, R.; Khan, I.; Nargotra, A.
Identification and optimization of Escherichia coli GlmU inhibitors: An in silico approach with validation thereof
Eur. J. Med. Chem.
92
78-90
2014
Escherichia coli, Escherichia coli (P0ACC7), Escherichia coli ATCC 25922 (P0ACC7)
Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
J. Biomol. Screen.
21
342-353
2016
Escherichia coli, Escherichia coli (P0ACC7), Escherichia coli ATCC 25922, Escherichia coli ATCC 25922 (P0ACC7)
Dziadek, B.; Brzostek, A.; Grzybowski, M.; Fol, M.; Krupa, A.; Kryczka, J.; Plocinski, P.; Kurdowska, A.; Dziadek, J.
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
PLoS ONE
11
e0148030
2016
Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WMN3), Mycobacterium tuberculosis ATCC 25618 (P9WMN3)
Soni, V.; Upadhayay, S.; Suryadevara, P.; Samla, G.; Singh, A.; Yogeeswari, P.; Sriram, D.; Nandicoori, V.K.
Depletion of M. tuberculosis GlmU from infected murine lungs effects the clearance of the pathogen
PLoS Pathog.
11
e1005235
2015
Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis ATCC 25618 (P9WMN3), Mycobacterium tuberculosis H37Rv (P9WMN3)
Rani, C.; Mehra, R.; Sharma, R.; Chib, R.; Wazir, P.; Nargotra, A.; Khan, I.A.
High-throughput screen identifies small molecule inhibitors targeting acetyltransferase activity of Mycobacterium tuberculosis GlmU
Tuberculosis
95
664-677
2015
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WMN3), Mycobacterium tuberculosis H37Rv (P9WMN3)
Honda, Y.; Nakano, S.; Ito, S.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
Improvement of ST0452 N-acetylglucosamine-1-phosphate uridyltransferase activity by the cooperative effect of two single mutations identified through structure-based protein engineering
Appl. Environ. Microbiol.
84
e002213-18
2018
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Honda, Y.; Zang, Q.; Shimizu, Y.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
Increasing the thermostable sugar-1-phosphate nucleotidylyltransferase activities of the archaeal ST0452 protein through site saturation mutagenesis of the 97th amino acid position
Appl. Environ. Microbiol.
83
e02291-16
2017
Sulfurisphaera tokodaii (Q975F9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (Q975F9)
Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU)
Appl. Microbiol. Biotechnol.
100
3071-3085
2016
Escherichia coli, Haemophilus influenzae, Escherichia coli ATCC 25922
Craggs, P.D.; Mouilleron, S.; Rejzek, M.; de Chiara, C.; Young, R.J.; Field, R.A.; Argyrou, A.; de Carvalho, L.P.S.
The Mechanism of acetyl transfer catalyzed by Mycobacterium tuberculosis GlmU
Biochemistry
57
3387-3401
2018
Mycobacterium tuberculosis (A5U161), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25177 (A5U161)
Han, X.; Chen, C.; Yan, Q.; Jia, L.; Taj, A.; Ma, Y.
Action of dicumarol on glucosamine-1-phosphate acetyltransferase of GlmU and Mycobacterium tuberculosis
Front. Microbiol.
10
1799
2019
Mycobacterium tuberculosis (A5U161), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25177 (A5U161)
Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
J. Biomol. Screen.
21
342-353
2016
Haemophilus influenzae, Escherichia coli (P0ACC7), Escherichia coli, Escherichia coli ATCC 25922 (P0ACC7)
Wang, M.; Huang, M.; Gu, H.; Li, S.; Ma, Y.; Wang, J.
Mutational analysis to identify the residues essential for the acetyltransferase activity of GlmU in Bacillus subtilis
RSC Adv.
7
13858-13867
2017
Escherichia coli (P0ACC7), Bacillus subtilis (P14192), Bacillus subtilis 168 (P14192)
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