Determination of Enzymatic Activity of 5-Enolpyruvylshikimate-3-phosphate Synthase by LC/MS.
نویسندگان
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 کاملThe Enzymatic Formation and Isolation of 3-enolpyruvylshikimate 5-phosphate.
Previous investigations (l-5) have established in some detail the path of aromatic biosynthesis in bacteria, starting with glucose and leading to the formation of shikimate 5-phosphate (Fig. 1). This was also true of the conversion of prephenate to phenylalanine (6) and tyrosine (7), and of anthranilate to tryptophan (8-10). On the other hand, it was not known how shikimate 5-phosphate is conve...
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...
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 ...
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...
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ژورنال
عنوان ژورنال: Journal of the Food Hygienic Society of Japan (Shokuhin Eiseigaku Zasshi)
سال: 2003
ISSN: 0015-6426,1882-1006
DOI: 10.3358/shokueishi.44.77