Purification and properties of chorismate mutase-prephenate dehydratase and prephenate dehydrogenase from Alcaligenes eutrophus
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چکیده
منابع مشابه
Affinity chromatography and inhibition of chorismate mutase-prephenate dehydrogenase by derivatives of phenylalanine and tyrosine.
Several derivatives of phenylalanine and tyrosine were prepared and tested for inhibition of chorismate mutase-prephenate dehydrogenase (EC 1.3.1.12) from Escherichia coli K12 (strain JP 232). The best inhibitors were N-toluene-p-sulphonyl-L-phenylalanine, N-benzenesulphonyl-L-phenylalanine and N-benzloxycarbonyl-L-phenylalanine. Consequently two compounds, N-toluene-sulphonyl-L-p-aminophenylal...
متن کاملPhenylalanine biosynthesis in Escherichia coli K-12: mutants derepressed for chorismate mutase P-prephenate dehydratase.
Mutants were isolated which are derepressed for the synthesis of chorismate mutase P-prephenate dehydratase. No other enzymes involved in the synthesis of phenylalanine are derepressed in these strains. These mutants are able to grow in concentrations of o- and p-fluorophenylalanine that inhibit the growth of AB3259, the strain from which they were derived. They also excrete phenylalanine. Gene...
متن کاملGenetic separability of the chorismate mutase and prephenate dehydrogenase components of the Escherichia coli tyrA gene product.
Fragments of the tyrA gene of Escherichia coli, when suitably engineered, can express either the chorismate mutase activity or the prephenate dehydrogenase activity without the other.
متن کاملFeedback inhibition of chorismate mutase/prephenate dehydrogenase (TyrA) of Escherichia coli: generation and characterization of tyrosine-insensitive mutants.
In order to get insights into the feedback regulation by tyrosine of the Escherichia coli chorismate mutase/prephenate dehydrogenase (CM/PDH), which is encoded by the tyrA gene, feedback-inhibition-resistant (fbr) mutants were generated by error-prone PCR. The tyrA(fbr) mutants were selected by virtue of their resistance toward m-fluoro-D,L-tyrosine, and seven representatives were characterized...
متن کاملThe mechanism of catalysis of the chorismate to prephenate reaction by the Escherichia coli mutase enzyme.
Molecular dynamics studies of the Escherichia coli chorismate mutase (EcCM), containing at the active site chorismate and in turn the transition state (TS), have been performed. The simulations show that TS is not bound any tighter than chorismate. Comparison of average polar interactions show they are virtually identical for interactions of EcCM with chorismate and the TS, whereas hydrophobic ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1976
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.126.2.712-722.1976