Abstract
5-Enolpyruvylshikimate 3-phosphate (EPSP) synthase (3-phosphoshikimate 1-carboxyvinyltransferase; EC 2.5.1.9) from the glyphosate-tolerant cyanobacterium Anabaena variabilis (ATCC 29413) was purified to homogeneity. The enzyme had a similar relative molecular mass to other EPSP synthases and showed similar kinetic properties except for a greatly elevated K i for the herbicide glyphosate (approximately ten times higher than that of enzymes from other sources). With whole cells, the monoisopropylamine salt of glyphosate was more toxic than the free acid but the effects of the free acid and monoisopropylamine salt on purified EPSP synthase were identical.
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Abbreviations
- EPSP:
-
5-enolpyruvylshikimate 3-phosphate
- Mr :
-
relative molecular mass
- PEP:
-
phosphoenolpyruvate
- SDS-PAGE:
-
sodium dodecyl sulphate-polyacrylamide gel electrophoresis
- S3P:
-
shikimate 3-phosphate
Referencess
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The funding of this work by the Agricultural and Food Research Council and the University of Dundee Research Initiatives Programme is gratefully acknowledged.
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Powell, H.A., Kerby, N.W., Rowell, P. et al. Purification and properties of a glyphosate-tolerant 5-enolpyruvylshikimate 3-phosphate synthase from the cyanobacterium Anabaena variabilis . Planta 188, 484–490 (1992). https://doi.org/10.1007/BF00197039
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DOI: https://doi.org/10.1007/BF00197039