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

✍ Scribed by Hilary A. Powell; Nigel W. Kerby; Peter Rowell; David M. Mousdale; John R. Coggins

Publisher
Springer-Verlag
Year
1992
Tongue
English
Weight
885 KB
Volume
188
Category
Article
ISSN
0032-0935

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✦ Synopsis

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 Ki 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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