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1 )-liganded forms of Streptococcus pneumoniae EPSP synthase.
2 e is similar to that of the Escherichia coli EPSP synthase.
3 main is very similar to that of S3P bound to EPSP synthase.
4 erties that render it unique among the known EPSP synthases.
5 ed on the active site structures of class II EPSP synthases.
6 5-enolpyruvylshikimate 3-phosphate synthase (EPSP synthase*), a key enzyme in the shikimic acid pathw
7 e enzyme 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase, a prime target for drugs and herbicides.
8 ely to reflect the physiological behavior of EPSP synthase and also add to our understanding of how t
9 d the mechanism of the reaction catalyzed by EPSP synthase and analyzed the reaction products formed
10 We generated a synthetic gene coding for CP4 EPSP synthase and characterized the enzyme using kinetic
11 e lysine, arginine and histidine residues of EPSP synthase and distances to a 13C label in Glp and to
14 r enolpyruvylshikimate 3-phosphate synthase (EPSP synthase, AroA) is protonating the methylene carbon
17 a enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the condensation of shikimate 3
18 a enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the condensation of shikimate-3
20 into the plant genome, the gene product, CP4 EPSP synthase, confers crop resistance to glyphosate.
21 encoding 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the gram-positive pathogen Streptoco
22 lyzed by 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase has been examined using the pseudosubstra
24 xamines a recent claim that the mechanism of EPSP synthase involves two covalent enzyme-intermediates
25 at most of the free energy of S3P binding to EPSP synthase is contributed by the N-terminal domain.
26 As there is a much evidence to suggest that EPSP synthase is essential for bacterial survival, its d
27 The overall topology of the S. pneumoniae EPSP synthase is similar to that of the Escherichia coli
30 NMR experiments, employing a slow catalytic EPSP synthase mutant and a long prelyophilization incuba
31 5-enolpyruvylshikimate-3-phosphate synthase (EPSP synthase or EPSPS) is best known as the target of t
32 rotein (YFP) fused to the transit peptide of EPSP synthase* or the small subunit of Rubisco was not i
33 the binding site of the second substrate of EPSP synthase (phosphoenol pyruvate), mimicking an inter
34 -enol-Pyruvylshikimate-3-phosphate synthase (EPSP synthase; phosphoenolpyruvate:3-phosphoshikimate 1-
36 compared to unrestrained simulations of the EPSP synthase tetrahedral intermediate and its phosphona
37 y enzyme 5-enolpyruvylshikimate 3-phosphate (EPSP) synthase, the functionality of which is absolutely
40 ate S3P to the isolated N-terminal domain of EPSP synthase using a combination of NMR spectroscopy an
42 udy of the pathogenic bacteria S. pneumoniae EPSP synthase with inhibitor and TI will provide invalua
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