Rational herbicide design by inhibition of tryptophan biosynthesis.

Compounds designed to mimic the tryptophan synthase alpha subunit reactive intermediate were found to be potent inhibitors of the enzyme. These compounds are herbicidal and the herbicidal mode of action was demonstrated to be due to disruption of tryptophan biosynthesis.

Nontoxic and toxic oligopeptides with D-amino acids and unusual residues in Microcystis aeruginosa PCC 7806.

Toxic and nontoxic peptides were isolated from the cyanobacterium Microcystis aeruginosa PCC 7806 by a procedure including extraction of cells with water-saturated 1-butanol, chromatography of the extract on silica gel plates and high performance liquid chromatography (HPLC) on Partisil-5. The toxin was shown to be only a minor constituent, being negatively charged and thus separable by electrophoresis, within the HPLC-purified fraction. It contained erythro-beta-methyl-D-Asp, D-Glu, D-Ala, L-Leu, and L-Arg known to be part of the Microcystis peptide-toxin with Mr 994.

The peptide toxin of the cyanobacterium Microcystis aeruginosa PCC 7941. Isolation and analysis by nuclear magnetic resonance and fast atom bombardment mass spectroscopy.

Toxin was obtained from the cyanobacterium Microcystis aeruginosa PCC7941 by extracting freeze-dried cells with water-saturated, acidified n-butanol, diethyl ether-water distribution, reversed-phase thin-layer chromatography and silica high-performance liquid chromatography (HPLC). Two toxic peptide fractions resulted from HPLC. One of these fractions was analyzed by UV and NMR spectroscopy, amino acid analysis and fast atom bombardment mass spectroscopy.