The enzyme, characterized from the bacterium Streptomyces viridochromogenes, is involved in bialaphos biosynthesis. The enzyme from the bacterium Kitasatospora phosalacinea participates in the biosynthesis of the related compound phosalacine. Both compounds contain the nonproteinogenic amino acid L-phosphinothricin that acts as a potent inhibitor of EC 6.3.1.2, glutamine synthetase. The similar enzyme EC 4.2.1.3, aconitate hydratase, cannot catalyse this reaction.
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The expected taxonomic range for this enzyme is: Streptomyces viridochromogenes
The enzyme, characterized from the bacterium Streptomyces viridochromogenes, is involved in bialaphos biosynthesis. The enzyme from the bacterium Kitasatospora phosalacinea participates in the biosynthesis of the related compound phosalacine. Both compounds contain the nonproteinogenic amino acid L-phosphinothricin that acts as a potent inhibitor of EC 6.3.1.2, glutamine synthetase. The similar enzyme EC 4.2.1.3, aconitate hydratase, cannot catalyse this reaction.
a mutant defective in Pmi fails to produce phosphinothricin tripeptide. Recombinant protein shows no standard aconitase activity with citrate as a substrate, and the corresponding gene is not able to complement an AcnA mutant
a mutant defective in Pmi fails to produce phosphinothricin tripeptide. Recombinant protein shows no standard aconitase activity with citrate as a substrate, and the corresponding gene is not able to complement an AcnA mutant
The phosphinomethylmalate isomerase gene pmi, encoding an aconitase-like enzyme, is involved in the synthesis of phosphinothricin tripeptide in Streptomyces viridochromogenes
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Enzyme Nomenclature
4.2.1.166 phosphinomethylmalate isomerase
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