Inhibition of pea leaf glutamine synthetase by methionine sulphoximine,phosphinothricin and other glutamate analogues |
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Authors: | Mark Leason Denise Cunliffe Donald Parkin Peter J. Lea Benjamin J. Miflin |
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Affiliation: | Department of Biochemistry, Rothamsted Experimental Station, Harpenden, Herts AL5 2JQ, U.K. |
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Abstract: | The kinetics of the inhibition of glutamine synthetase from Pisum sativum leaves by l-methionine sulphoximine and dl-phosphinothricin were determined. Inhibition by both compounds was mixed-competitive, and apparent Ki values of 0.16 mM and 0.073 mM respectively were determined. dl-5-Hydroxylysine, dl-glutamate-4-tetrazole and l-4-methyleneglutamic acid were also strong inhibitors. Analogues of methionine sulphoximine, dl-ethionine sulphoximine and dl-prothionine sulphoximine were poor inhibitors of glutamine synthetase. Other glutamine and glutamate analogues e.g. azaserine, albizziine, asparagine and kainic acid had no inhibitory action. |
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Keywords: | Leguminosae glutamine synthetase inhibition methionine sulphoximine phosphinothricin glutamate analogues. |
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