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0.008
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant K403A
0.016
-
cosubstrate acetoacetyl-CoA, pH 7.5, 30°C
0.016
-
pH 7.5, 30°C, cosubstrate: acetoacetyl-CoA
0.044
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant N456A
0.061
-
pH and temperature not specified in the publication, recombinant His-tagged wild-type GlmU
0.066
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant E458A
0.069
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant R463A
0.073
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S474A
0.107
-
pH 7.5, 37°C, recombinant enzyme
0.107
-
pH not specified in the publication, temperature not specified in the publication
0.13
-
pH and temperature not specified in the publication, recombinant His-tagged GlmU mutant S416A
0.241
-
mutant enzyme C380A, at pH 8.0 and 37°C
0.278
-
mutant enzyme C405A, at pH 8.0 and 37°C
0.283
-
pH 7.6, 30°C, recombinant mutant N397A
0.29
-
cosubstrate acetyl-CoA, pH 7.5, 30°C
0.3
-
pH 7.6, 30°C, recombinant mutant H374A
0.3
-
pH 8.2, 37°C, recombinant His6-tagged enzyme
0.304
-
mutant enzyme V385C/C405S, at pH 8.0 and 37°C
0.333
-
wild type enzyme, at pH 8.0 and 37°C
0.353
-
pH 7.6, 30°C, recombinant wild-type
0.359
-
mutant enzyme C405S, at pH 8.0 and 37°C
0.37
-
pH 7.6, 30°C, recombinant mutant S416A
0.47
-
mutant enzyme C380A/C405S, at pH 8.0 and 37°C
0.56
-
pH 7.5, 80°C, deletion mutant D005 of ST0452 protein
0.56
-
pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein
0.59
-
pH 7.5, 80°C, wild-type enzyme
0.59
-
pH 7.5, 80°C, wild-type ST0452 protein
0.98
-
cosubstrate propionyl-CoA, pH 7.5, 30°C
0.98
-
pH 7.5, 30°C, cosubstrate: n-propionyl-CoA
1.69
-
pH 7.5, 80°C, deletion mutant D011 of ST0452 protein
1.69
-
pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein
0.04
-
with cellobiose as acceptor, at pH 7.0 and 37°C
0.05
-
with laminatriose as acceptor, at pH 7.0 and 37°C
0.69
-
cosubstrate dTTP, pH 7.5, temperature not specified in the publication
0.7
-
cosubstrate UTP, pH 7.5, temperature not specified in the publication
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-
Molecular weight and some physicochemical and catalytic properties of sugar phosphate phosphohydrolase from Escherichia coli and Neisseria meningitidis
1975
Lee, Y.P.; Lee, A.T.; Choy, F.Y.M.; Sowokinos, J.R.
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Cloning and expression of glucose-1-phosphate thymidylyltransferase gene (schS6) from Streptomyces sp. SCC-2136
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Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase
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Crystallization and initial crystallographic analysis of phosphoglucosamine mutase from Bacillus anthracis
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Acta Crystallogr. Sect. F
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Contribution of phosphoglucosamine mutase to the resistance of Streptococcus gordonii DL1 to polymorphonuclear leukocyte killing
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Kinetic properties of Mycobacterium tuberculosis bifunctional GlmU
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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
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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
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Design and synthesis of novel cell wall inhibitors of Mycobacterium tuberculosis GlmM and GlmU
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Structure-based virtual screening of novel inhibitors of the uridyltransferase activity of Xanthomonas oryzae pv. oryzae GlmU
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Identification of amino acids involved in catalytic process of M. tuberculosis GlmU acetyltransferase
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In vitro validation of acetyltransferase activity of GlmU as an antibacterial target in Haemophilus influenzae
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Substrate bound crystal structures reveal features unique to Mycobacterium tuberculosis N-acetyl-glucosamine-1-phosphate uridyltransferase and a catalytic mechanism for acetyltransfer
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Kinetic modelling of GlmU reactions - prioritization of reaction for therapeutic application
2012
Singh, V.K.; Das, K.; Seshadri, K.
PLoS ONE
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Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7
2010
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J. Bacteriol.
192
3287-3293
Effect of phosphoglucosamine mutase on biofilm formation and antimicrobial susceptibilities in M. smegmatis glmM gene knockdown strain
2013
Kang, J.; Xu, L.; Yang, S.; Yu, W.; Liu, S.; Xin, Y.; Ma, Y.
PLoS ONE
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Characterization of the amino acid residues mediating the unique amino-sugar-1-phosphate acetyltransferase activity of the archaeal ST0452 protein
2015
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Extremophiles
19
417-427
Identification and characterization of a thermostable bifunctional enzyme with phosphomannose isomerase and sugar-1-phosphate nucleotidylyltransferase activities from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3
2015
Akutsu, J.; Zhang, Z.; Morita, R.; Kawarabayasi, Y.
Extremophiles
19
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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)
2015
Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
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Purification and biochemical characterisation of GlmU from Yersinia pestis
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Identification and optimization of Escherichia coli GlmU inhibitors: An in silico approach with validation thereof
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Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
2016
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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
2016
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Depletion of M. tuberculosis GlmU from infected murine lungs effects the clearance of the pathogen
2015
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High-throughput screen identifies small molecule inhibitors targeting acetyltransferase activity of Mycobacterium tuberculosis GlmU
2015
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Kinetic evaluation of glucose 1-phosphate analogues with a thymidylyltransferase using a continuous coupled enzyme assay
2015
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13
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Molecular characterization of legionellosis drug target candidate enzyme phosphoglucosamine mutase from Legionella pneumophila (strain Paris) an in silico approach
2014
Hasan, A.; Mazumder, H.H.; Khan, A.; Hossain, M.U.; Chowdhury, H.K.
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12
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Crystal structure of Aquifex aeolicus gene product Aq1627 a putative phosphoglucosamine mutase reveals a unique C-terminal end-to-end disulfide linkage
2017
Sridharan, U.; Kuramitsu, S.; Yokoyama, S.; Kumarevel, T.; Ponnuraj, K.
Mol. Biosyst.
13
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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)
2016
Sharma, R.; Rani, C.; Mehra, R.; Nargotra, A.; Chib, R.; Rajput, V.; Kumar, S.; Singh, S.; Sharma, P.; Khan, I.
Appl. Microbiol. Biotechnol.
100
3071-3085
The Mechanism of acetyl transfer catalyzed by Mycobacterium tuberculosis GlmU
2018
Craggs, P.D.; Mouilleron, S.; Rejzek, M.; de Chiara, C.; Young, R.J.; Field, R.A.; Argyrou, A.; de Carvalho, L.P.S.
Biochemistry
57
3387-3401
Preparative and kinetic analysis of beta-1,4- and beta-1,3-glucan phosphorylases informs access to human milk oligosaccharide fragments and analogues thereof
2020
Singh, R.P.; Pergolizzi, G.; Nepogodiev, S.A.; de Andrade, P.; Kuhaudomlarp, S.; Field, R.A.
ChemBioChem
21
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Action of dicumarol on glucosamine-1-phosphate acetyltransferase of GlmU and Mycobacterium tuberculosis
2019
Han, X.; Chen, C.; Yan, Q.; Jia, L.; Taj, A.; Ma, Y.
Front. Microbiol.
10
1799
Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) inhibitory activity of terreic acid isolated from Aspergillus terreus
2016
Sharma, R.; Lambu, M.R.; Jamwal, U.; Rani, C.; Chib, R.; Wazir, P.; Mukherjee, D.; Chaubey, A.; Khan, I.A.
J. Biomol. Screen.
21
342-353
-
Exploring the broad nucleotide triphosphate and sugar-1-phosphate specificity of thymidylyltransferase Cps23FL from Streptococcus pneumonia serotype 23F
2020
Li, S.; Wang, H.; Jin, G.; Chen, Z.; Gu, G.
RSC Adv.
10
30110-30114
-
Mutational analysis to identify the residues essential for the acetyltransferase activity of GlmU in Bacillus subtilis
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