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3
-
wild-type, pH 7.2, 25°C
0.03
-
recombinant enzyme, pH 7.5, 25°C
0.0005
-
same enzyme preparation as following, substitution with 50 microM Zn2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.00123
-
recombinant enzyme produced in Escherichia coli, native Zn2+ and Fe2+ not substituted, 100 mM Tris-acetate, pH 7.5, 40°C
0.00156
-
same enzyme preparation as following, substitution with 5 microM Cu2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.002
-
same enzyme preparation as following, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.00227
-
independently prepared enzyme, substitution with 50 microM Cd2+, pH 5.0, 40°C
0.0025
-
wild-type, pH 7.5, temperature not specified in the publication
0.00318
-
independently prepared enzyme, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.0044
-
pH 7.4, 25°C, wild-type enzyme
0.0057
-
wild type, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.00593
-
pH 6.5, 25°C, Cd2+-enzyme
0.00773
-
pH 6.5, 25°C
0.0079
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.0093
-
pH 7.4, 37°C, wild-type enzyme
0.012
-
N23C mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.012
-
P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.012
-
pH and temperature not specified in the publication
0.012
-
wild-type, pH 7.5, temperature not specified in the publication
0.013
-
N23C/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.014
-
pH 7.4, 25°C, mutant enzyme P145S
0.01926
-
same enzyme preparation as before, substitution with 5 microM Cu2+, pH 5.0, 40°C
0.02
-
pH 7.5, 37°C, wild-type enzyme
0.021
-
wild-type, pH 7.2, 37°C
0.022
-
wild-type, pH 7.5, temperature not specified in the publication
0.024
-
mutant P245A, pH 7.2, 37°C
0.0385
-
pH 6.5, 25°C, Zn2+-enzyme
0.043
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
0.06
-
D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.06
-
N23C mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.067
-
pH 7.5, 60°C, wild-type Mn2+-enzyme
0.07
-
60°C, pH 7.0, 0.48 mM Cd2+
0.07
-
pH 7.5, 37°C, Mn2+ mutant enzyme N26C
0.074
-
D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.075
-
pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated
0.081
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.097
-
N23C/C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.107
-
N23C/C247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.109
-
N23C/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.11
-
pH 7.5, 37°C, Cd2+ mutant enzyme N26C
0.14
-
N23C/C247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.14
-
pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated
0.19
-
N23C/C246S/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.2
-
28°C, parent strain PR122
0.213
-
C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.22
-
37°C, parent strain PR122
0.23
-
37°C, mutant strain PR32
0.24
-
N23C/C247E mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.28
-
pH 7.4, 37°C, mutant enzyme P145S
0.285
-
pH and temperature not specified in the publication, mutant F114R
0.33
-
N23C/C247E/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.45
-
42°C, mutant strain PR32
0.498
-
N23C/C246S/D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.503
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.54
-
N23C/C246S/D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.594
-
pH and temperature not specified in the publication, mutant F139A
0.816
-
pH and temperature not specified in the publication, R117K
0.83
-
42°C, parent strain PR122
0.873
-
pH and temperature not specified in the publication, mutant F114A
1.04
-
N23C/C246S mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1.1
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
2.63
-
mutant D243E, pH 7.2, 37°C
2.742
-
pH and temperature not specified in the publication, mutant F114R/R117Q
3.21
-
pH and temperature not specified in the publication, R117Q
3.6
-
pH and temperature not specified in the publication, F114R/R117Q/F139G
3.7
-
pH and temperature not specified in the publication, mutant F114R/R117A
0.38
-
at 37°C, pH not specified in the publication
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Crystal structures of substrate and inhibitor complexes of ribose 5-phosphate isomerase A from Vibrio vulnificus YJ016
2009
Kim, T.G.; Kwon, T.H.; Min, K.; Dong, M.S.; Park, Y.I.; Ban, C.
Mol. Cells
27
99-103
Electronic structure of the metal center in the Cd(2+), Zn(2+), and Cu(2+) substituted forms of KDO8P synthase: implications for catalysis
2009
Kona, F.; Tao, P.; Martin, P.; Xu, X.; Gatti, D.L.
Biochemistry
48
3610-3630
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Probing the subunit-subunit interaction of the tetramer of E. coli KDO8P synthase by electrospray ionization mass spectrometry
2009
Li, Z.; Sau, A.
Chin. J. Chem.
27
111-116
Reversing evolution: re-establishing obligate metal ion dependence in a metal-independent KDO8P synthase
2009
Cochrane, F.C.; Cookson, T.V.; Jameson, G.B.; Parker, E.J.
J. Mol. Biol.
390
646-661
Structural studies on Helicobacter pylori 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase using electrospray ionization mass spectrometry: a tetrameric complex composed of dimeric dimers
2009
Li, Z.; Sau, A.K.
Rapid Commun. Mass Spectrom.
23
1573-1578
Enediol mimics as inhibitors of the D-arabinose 5-phosphate isomerase (KdsD) from Francisella tularensis
2011
Yep, A.; Sorenson, R.J.; Wilson, M.R.; Showalter, H.D.; Larsen, S.D.; Keller, P.R.; Woodard, R.W.
Bioorg. Med. Chem. Lett.
21
2679-2682
Targeting bacterial membranes: NMR spectroscopy characterization of substrate recognition and binding requirements of D-arabinose-5-phosphate isomerase
2010
Airoldi, C.; Sommaruga, S.; Merlo, S.; Sperandeo, P.; Cipolla, L.; Polissi, A.; Nicotra, F.
Chemistry
16
1897-1902
Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis
2011
Godinho, L.M.; de Sa-Nogueira, I.
FEBS J.
278
2511-2524
A unique arabinose 5-phosphate isomerase found within a genomic island associated with the uropathogenicity of Escherichia coli CFT073
2011
Mosberg, J.A.; Yep, A.; Meredith, T.C.; Smith, S.; Wang, P.F.; Holler, T.P.; Mobley, H.L.; Woodard, R.W.
J. Bacteriol.
193
2981-2988
Probing the active site of the sugar isomerase domain from E. coli arabinose-5-phosphate isomerase via X-ray crystallography
2010
Gourlay, L.J.; Sommaruga, S.; Nardini, M.; Sperandeo, P.; Deho, G.; Polissi, A.; Bolognesi, M.
Protein Sci.
19
2430-2439
Targeting the role of a key conserved motif for substrate selection and catalysis by 3-deoxy-D-manno-octulosonate 8-phosphate synthase
2011
Allison, T.M.; Hutton, R.D.; Cochrane, F.C.; Yeoman, J.A.; Jameson, G.B.; Parker, E.J.
Biochemistry
50
3686-3695
Specificity and mutational analysis of the metal-dependent 3-deoxy-D-manno-octulosonate 8-phosphate synthase from Acidithiobacillus ferrooxidans
2010
Allison, T.M.; Yeoman, J.A.; Hutton, R.D.; Cochrane, F.C.; Jameson, G.B.; Parker, E.J.
Biochim. Biophys. Acta
1804
1526-1536
Synthesis and evaluation of tetrahedral intermediate mimic inhibitors of 3-deoxy-d-manno-octulosonate 8-phosphate synthase
2012
Harrison, A.N.; Reichau, S.; Parker, E.J.
Bioorg. Med. Chem. Lett.
22
907-911
Targeting bacterial membranes: identification of Pseudomonas aeruginosa D-arabinose-5P isomerase and NMR characterisation of its substrate recognition and binding properties
2011
Airoldi, C.; Sommaruga, S.; Merlo, S.; Sperandeo, P.; Cipolla, L.; Polissi, A.; Nicotra, F.
ChemBioChem
12
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Arabinose 5-phosphate covalently inhibits transaldolase
2014
Light, S.H.; Anderson, W.F.
J. Struct. Funct. Genomics
15
41-44
Structure of 2-keto-3-deoxy-D-manno-octulosonate-8-phosphate synthase from Pseudomonas aeruginosa
2013
Nelson, S.K.; Kelleher, A.; Robinson, G.; Reiling, S.; Asojo, O.A.
Acta Crystallogr. Sect. F
69
1084-1088
Examining the role of intersubunit contacts in catalysis by 3-deoxy-D-manno-octulosonate 8-phosphate synthase
2013
Allison, T.M.; Cochrane, F.C.; Jameson, G.B.; Parker, E.J.
Biochemistry
52
4676-4686
Enzymatic synthesis of 3-deoxy-D-manno-octulosonic acid (KDO) and its application for LPS assembly
2016
Wen, L.; Zheng, Y.; Li, T.; Wang, P.G.
Bioorg. Med. Chem. Lett.
26
2825-2828
Conservation of the 2-keto-3-deoxymanno-octulosonic acid (Kdo) biosynthesis pathway between plants and bacteria
2013
Smyth, K.M.; Marchant, A.
Carbohydr. Res.
380
70-75
Identification of novel scaffolds for potential anti-Helicobacter pylori agents based on the crystal structure of H. pylori 3-deoxy-D-manno-octulosonate 8-phosphate synthase (HpKDO8PS)
2016
Cho, S.; Im, H.; Lee, K.Y.; Chen, J.; Kang, H.J.; Yoon, H.J.; Min, K.H.; Lee, K.R.; Park, H.J.; Lee, B.J.
Eur. J. Med. Chem.
108
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Heterologous expression, purification, crystallization and preliminary X-ray diffraction analysis of KDO8P synthase from Arabidopsis thaliana
2014
Zhang, F.; Xu, Y.; Zhang, Z.
Protein Expr. Purif.
101
133-137
Analysis of the arabinose-5-phosphate isomerase of Bacteroides fragilis provides insight into regulation of single-domain arabinose phosphate isomerases
2014
Cech, D.; Wang, P.F.; Holler, T.P.; Woodard, R.W.
J. Bacteriol.
196
2861-2868
Identification of a D-arabinose-5-phosphate isomerase in the Gram-positive Clostridium tetani
2017
Cech, D.; Markin, K.; Woodard, R.
J. Bacteriol.
199
e00246
Expression, purification and characterization of arabinose-5-phosphate isomerase from Arabidopsis thaliana
2016
Qu, Y.; Zhang, Z.; Wang, C.; Wang, L.; Wu, L.
Sheng Wu Gong Cheng Xue Bao
32
1060-1069
Campylobacter jejuni KDO8P Synthase, its inhibition by KDO8P oxime, and control of the residence time of slow-binding inhibition
2018
Gama, S.R.; Balachandran, N.; Berti, P.J.
Biochemistry
57
5327-5338
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