The purification of 5-enolpyruvylshikimate 3-phosphate synthase from an overproducing strain ofEscherichia coli

Site-Directed Mutagenesis, Expression and Biological Activity of E. coli 5-Enolpyruvylshikimate 3-Phosphate Synthase Gene

Site-directed mutagenesis (SDM) as a powerful technique was used to change two important and conserved amino acids in 5-enolpyruvylshikimate 3- phosphate synthase (EPSPS) gene of E. coli. The mutations changed glycine 96 to alanine and alanine 183 to threonine. These two amino acids are very important for intraction of the wide spectrum herbicide, glyphosate, to EPSP synthase enzymes. By design...

Purification and Properties of 5-Enolpyruvylshikimate-3-Phosphate Synthase from Dark-Grown Seedlings of Sorghum bicolor.

5-Enolpyruvylshikimate-3-phosphate (EPSP) synthase (3-phospho-shikimate 1-carboxyvinyltransferase; EC 2.5.1.19) was purified 1300-fold from etiolated shoots of Sorghum bicolor (L.) Moench. Native polyacrylamide gel electrophoresis revealed three barely separated protein bands staining positive for EPSP synthase activity. The native molecular weight was determined to be 51,000. Enzyme activity w...

Progress in cloning, expression and purification of 5-enolpyruvylshikimate-3-phosphate synthase from pathogens causing meningitis.

Phosphate closes the solution structure of the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) from Mycobacterium tuberculosis.

The 5-enolpyruvylshikimate-3-phosphate synthase catalyses the sixth step of the shikimate pathway that is responsible for synthesizing aromatic compounds and is absent in mammals, which makes it a potential target for drugs development against microbial diseases. Here, we report the phosphate binding effects at the structure of the 5-enolpyruvylshikimate-3-phosphate synthase from Mycobacterium ...

site-directed mutagenesis, expression and biological activity of e. coli 5-enolpyruvylshikimate 3-phosphate synthase gene

site-directed mutagenesis (sdm) as a powerful technique was used to change two important and conserved amino acids in 5-enolpyruvylshikimate 3- phosphate synthase (epsps) gene of e. coli. the mutations changed glycine 96 to alanine and alanine 183 to threonine. these two amino acids are very important for intraction of the wide spectrum herbicide, glyphosate, to epsp synthase enzymes. by design...