Evidence for the shikimate-3-phosphate interacting site in the N-terminal domain of 5-enolpyruvyl shikimate-3-phosphate synthase of Bacillus subtilis
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چکیده
منابع مشابه
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...
متن کاملSequential assignments of the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase.
5-Enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the formation of EPSP from shikimate-3phosphate (S3P) and phosphoenolpyruvate (PEP) in the sixth step of the shikimate pathway. This pathway is absent from mammalian systems but present in plants, bacteria, fungi and parasites, making EPSP synthase a promising model for the development of new antibiotics. One suggested approach toward...
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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...
متن کاملPhosphate 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 ...
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ژورنال
عنوان ژورنال: IUBMB Life
سال: 1996
ISSN: 1521-6543
DOI: 10.1080/15216549600201193