Purification and properties of a glyphosate-tolerant 5-enolpyruvylshikimate 3-phosphate synthase from the cyanobacterium Anabaena variabilis

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...

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Veröffentlicht in:	Planta 1992-11, Vol.188 (4), p.484-490
Hauptverfasser:	Powell, H.A, Kerby N.W, Rowell, P, Mousdale, D.M, Coggins, J.R
Format:	Artikel
Sprache:	eng
Schlagworte:	alkyl (aryl) transferases Anabaena variabilis Biological and medical sciences Biosynthesis Biotechnology Chromatography Cyanobacteria enzyme activity Enzyme engineering Enzymes Fundamental and applied biological sciences. Psychology Gels glyphosate Herbicide resistance Herbicides Improved methods for extraction and purification of enzymes Kinetics Klebsiella pneumoniae Methods. Procedures. Technologies Plants purification tolerance
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Zusammenfassung:	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.
ISSN:	0032-0935 1432-2048
DOI:	10.1007/BF00197039