Chemical shift mapping of shikimate-3-phosphate binding to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase
نویسندگان
چکیده
منابع مشابه
Sequential 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...
متن کاملSite-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...
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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 ...
متن کاملChorismate synthase. Pre-steady-state kinetics of phosphate release from 5-enolpyruvylshikimate 3-phosphate.
The pre-steady-state kinetics of phosphate formation from 5-enolpyruvylshikimate 3-phosphate catalysed by Escherichia coli chorismate synthase (EC 4.6.1.4) were studied by a rapid-acid-quench technique at 25 degrees C at pH 7.5. No pre-steady-state 'burst' or 'lag' phase was observed, showing that phosphate is released concomitant with the rate-limiting step of the enzyme. The implications of t...
متن کاملsite-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...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2001
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(01)02555-8