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Mechanism of inactivation of Escherichia coli 5-enolpyruvoylshikimate-3-phosphate synthase by o-phthalaldehyde.

Data up to Jan 2025

Published1990
Citations21
References24

Total Citations Per Year

Abstract

References (24)

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Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements

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Mechanism of enolpyruvylshikimate-3-phosphate synthase exchange of phosphoenolpyruvate with solvent protons

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The complete amino acid sequence of Escherichia coli 5‐enolpyruvylshikimate 3‐phosphate synthase

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Identification of the reactive cysteines of Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase and their nonessentiality for enzymatic catalysis.

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5-Enolpyruvyl shikimate 3-phosphate synthase from Escherichia coli. Identification of Lys-22 as a potential active site residue.

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Site-directed mutagenesis of Petunia hybrida 5-enolpyruvylshikimate-3-phosphate synthase: Lys-23 is essential for substrate binding.

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Arginine chemical modification of Petunia hybrida 5-enol-pyruvylshikimate-3-phosphate synthase

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Reaction of 5-enol-pyruvoylshikimate-3-phosphate synthase with diethyl pyrocarbonate: Evidence for an essential histidine residue

1987 • 17 citations

Evidence for a reactive gamma-carboxyl group (Glu-418) at the herbicide glyphosate binding site of 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli.

1988 • 17 citations

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