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5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
-
-
r
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
A0A1S0QXP6
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
the carbamate carboxylate is directly transferred to generate 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, without equilibration with HCO3- and CO2 in solution
-
-
?
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
?
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(2-bromo-5-ethoxy-4-methoxyphenyl)methanol
A0A1S0QXP6
-
(2-ethoxyphenyl)(morpholino)methanethione
A0A1S0QXP6
-
(5-(2-chlorophenyl)isoxazol-3-yl)methanamine
A0A1S0QXP6
-
2-methyl-N-(5-methylthiazol-2-yl)furan-3-carboxamide
A0A1S0QXP6
-
3,4-dihydroxybenzoic acid
A0A1S0QXP6
a scaffold hit from library screening
3-(4-methoxyphenyl)-1H-pyrazol-5-amine
A0A1S0QXP6
-
3-chloro-N-(5-(2,5-dichlorophenyl)-1,3,4-oxadiazol-2-yl)benzamide
19% inhibition at 0.010 mM
3-phenyl-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazol-6-amine
A0A1S0QXP6
-
4,5-dichlorobenzene-1,2-diol
A0A1S0QXP6
-
4-benzoyl-N-(5-(2,4-dimethylphenyl)-1,3,4-oxadiazol-2-yl)benzamide
13% inhibition at 0.010 mM
4-Nitro-5-aminoimidazole ribonucleotide
NAIR
5-ethyl-N-(1,3,4-thiadiazol-2-yl)thiophene-2-carboxamide
A0A1S0QXP6
49% inhibition at 0.025 mM
5-fluoro-1H-indole-2-carboxylic acid
A0A1S0QXP6
a scaffold hit from library screening
6-methoxyquinolin-3-amine
A0A1S0QXP6
-
indoline-1-carbothioamide
A0A1S0QXP6
-
isoquinolin-1-amine
A0A1S0QXP6
a scaffold hit from library screening
N-(3-fluorophenyl)-5-methylisoxazole-3-carboxamide
A0A1S0QXP6
-
N-(p-tolyl)-1,2,3,4-thiatriazol-5-amine
A0A1S0QXP6
36% inhibition at 0.1 mM
pyridin-4-yl(p-tolyl)methanamine
A0A1S0QXP6
-
additional information
high-throughput screening of compounds binding to Bacillus anthracis PurE. A a low ionic strength buffer condition is used to accentuate the thermal shift stabilization induced by compound binding to Bacillus anthracis PurE. Computational ligand docking to the active site. Determination of inhibitory compounds for inhibition of BaPurE activity and for cytotoxicity against Bacillus anthracis (DELTAANR strain), Escherichia coli (BW25113 strain, wild-type and DELTATolC), Francisella tularensis, Staphylococcus aureus (both methicillin susceptible and methicillin-resistant strains) and Yersinia pestis. Minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) values, overview
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0.0007 - 0.2
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
0.0007
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89G, 37°C, pH 8.0
0.0014
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89N, 37°C, pH 8.0
0.006
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89D, 37°C, pH 8.0
0.008
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, 37°C, pH 8.0
0.008
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89V, 37°C, pH 8.0
0.009
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89F, 37°C, pH 8.0
0.0226
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, pH 7.5, 23°C
0.03
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59Q, 37°C, pH 8.0
0.2
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59D, 37°C, pH 8.0
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0.0004 - 15.6
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
0.0021 - 15.5
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
0.0004
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H45W, pH 7.5, 23°C
0.0006
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59Q, 37°C, pH 8.0
0.0012
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H45Q, pH 7.5, 23°C
0.063
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89N, 37°C, pH 8.0
0.4
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89D, 37°C, pH 8.0
0.49
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59D, 37°C, pH 8.0
0.97
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89G, 37°C, pH 8.0
1.97
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89F, 37°C, pH 8.0
2.1
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89V, 37°C, pH 8.0
12.2
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, 37°C, pH 8.0
15.6
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, pH 7.5, 23°C
0.0021
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
mutant H45Q, pH 7.5, 23°C
15.5
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
wild-type, pH 7.5, 23°C
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hanging-drop method, crystals grow best at 295 K with the optimized mother-liquor conditions of 21-23% PEG 4K, 0.19 M ammonium acetate and 90 mM citrate, pH 5.25-5.5. Crystals belong to space group I422, with unit-cell parameters a = 99.25, c = 164.81 A
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multiple REDOR NMR studies of a 151000 Da complex of uniformly 15N-labeled enzyme and the active site ligand [6-13C]-citrate show a single ionization equilibrium associated with the key histidine H59. H59 exists in approximately equimolar amounts of an Ndelta-unprotonated pyridine-like form and an Ndelta-protonated pyrrole-like form. Proton transfer mechanism involves H59 Ndelta
mutant H59N soaked in 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, protonation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate C4 may occur in absence of H59
hanging-drop vapor-diffusion method, crystals grown in the presence of 4-carboxaminoimidazole ribonucleotide belong to space group P2(1)2(1)2(1), with unit cell parameters a = 86.92, b = 94.55 and c = 149.96 A. The 1.5 A crystal structure reveals an octameric structure with 422 symmetry
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wild-type cocrystallized with 4-nitroaminoimidazole ribonucleotide and mutants H45N and H45Q soaked with 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
purified recombinant detagged enzyme, crystallization at room temperature, 10 mg/ml protein is mixed with a reservoir solution consisting of 0.1 M sodium acetate trihydrate, pH 4.5, and 2 M ammonium sulfate, 24 h, X-ray diffraction structure determination and analysis at 1.45 Aresolution, molecular replacement using the structure of Bacillus anthracis PurE, PDB ID 1xmp, as template
nanodroplet vapor diffusion method, 1.77 A resolution, unit cell parameters: a = b = 103.25 A, c = 65.45 A, alpha = beta = 90°
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Meyer, E.; Leonard, N.J.; Bhat, B.; Stubbe, J.; Smith, J.M.
Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway
Biochemistry
31
5022-5032
1992
Escherichia coli
brenda
Meyer, E.; Kappock, T.J.; Osuji, C.; Stubbe, J.
Evidence for the Direct Transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase
Biochemistry
38
3012-3018
1999
Escherichia coli
brenda
Settembre, E.C.; Chittuluru, J.R.; Mill, C.P.; Kappock, T.J.; Ealick, S.E.
Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE)
Acta Crystallogr. Sect. D
60
1753-1760
2004
Acetobacter aceti
brenda
Mueller, E.J.; Meyer, E.; Rudolph, J.; Davisson, V.J.; Stubbe, J.
N5-carboxyaminoimidazole ribonucleotide: evidence for a new intermediate and two new enzymatic activities in the de novo purine biosynthetic pathway of Escherichia coli
Biochemistry
33
2269-2278
1994
Escherichia coli
brenda
Chung, S.O.; Lee, J.H.; Lee, S.Y.; Lee, D.S.
Genomic organization of purK and purE in Brevibacterium ammoniagenes ATCC 6872: purE locus provides a clue for genomic evolution
FEMS Microbiol. Lett.
137
265-268
1996
Corynebacterium ammoniagenes
brenda
Sorensen, I.S.; Dandanell, G.
Identification and sequence analysis of Sulfolobus solfataricus purE and purK genes
FEMS Microbiol. Lett.
154
173-180
1997
Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617
brenda
Watanabe, W.; Sampei, G.; Aiba, A.; Mizobuchi, K.
Identification and sequence analysis of Escherichia coli purE and purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de novo purine biosynthesis
J. Bacteriol.
171
198-204
1989
Escherichia coli, Escherichia coli NK6051
brenda
Schwarzenbacher, R.; Jaroszewski, L.; von Delft, F.; et al.
Crystal structure of a phosphoribosylaminoimidazole mutase PurE from Thermotoga maritima at 1.77 A resolution
Proteins
55
474-478
2004
Thermotoga maritima
brenda
Mathews, I.I.; Kappock, T.J.; Stubbe, J.; Ealick, S.E.
Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway
Structure
7
1395-1406
1999
Escherichia coli
brenda
Constantine, C.Z.; Starks, C.M.; Mill, C.P.; Ransome, A.E.; Karpowicz, S.J.; Francois, J.A.; Goodman, R.A.; Kappock, T.J.
Biochemical and structural studies of N5-carboxyaminoimidazole ribonucleotide mutase from the acidophilic bacterium Acetobacter aceti
Biochemistry
45
8193-8208
2006
Acetobacter aceti (Q2QJL2), Acetobacter aceti
brenda
Hoskins, A.A.; Morar, M.; Kappock, T.J.; Mathews, I.I.; Zaugg, J.B.; Barder, T.E.; Peng, P.; Okamoto, A.; Ealick, S.E.; Stubbe, J.
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis
Biochemistry
46
2842-2855
2007
Escherichia coli (P0AG18), Escherichia coli
brenda
Schaefer, J.; Jiang, H.; Ransome, A.E.; Kappock, T.J.
Multiple active site histidine protonation states in Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase detected by REDOR NMR
Biochemistry
46
9507-9512
2007
Acetobacter aceti (Q2QJL3), Acetobacter aceti
brenda
Brugarolas, P.; Duguid, E.M.; Zhang, W.; Poor, C.B.; He, C.
Structural and biochemical characterization of N5-carboxyaminoimidazole ribonucleotide synthetase and N5-carboxyaminoimidazole ribonucleotide mutase from Staphylococcus aureus
Acta Crystallogr. Sect. D
67
707-715
2011
Staphylococcus aureus (A0A0H3K7Y1)
brenda
Kim, A.; Wolf, N.; Zhu, T.; Johnson, M.; Deng, J.; Cook, J.; Fung, L.
Identification of Bacillus anthracis PurE inhibitors with antimicrobial activity
Bioorg. Med. Chem.
23
1492-1499
2015
Bacillus anthracis (A0A150QXP6)
brenda
Lei, H.; Jones, C.; Zhu, T.; Patel, K.; Wolf, N.M.; Fung, L.W.; Lee, H.; Johnson, M.E.
Identification of B. anthracis N(5)-carboxyaminoimidazole ribonucleotide mutase (PurE) active site binding compounds via fragment library screening
Bioorg. Med. Chem.
24
596-605
2016
Bacillus anthracis (A0A1S0QXP6), Bacillus anthracis
brenda