Skip to search formSkip to main content
You are currently offline. Some features of the site may not work correctly.

Chorismate Mutase-Prephenate Dehydratase

Known as: Chorismate Mutase Prephenate Dehydratase, Dehydratase, Chorismate Mutase-Prephenate, Mutase-Prephenate Dehydratase, Chorismate 
 
National Institutes of Health

Related topics

Related topics

1 relation

Broader (1)

Prephenate Dehydratase

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2005
2005
Feedback 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… Expand
  • figure 1
  • figure 2
  • figure 3
  • table 1
  • figure 4
Is this relevant?
2004
2004
Regulation of chorismate mutase in Saccharomyces cerevisiae
SummaryThe Saccharomyces cerevisiae ARO7 gene was cloned by screening a wild-type gene bank for complementation of an aro7… Expand
  • figure 2
  • figure 3
  • figure 4
  • table 1
  • table 2
Is this relevant?
2003
2003
Charge optimization increases the potency and selectivity of a chorismate mutase inhibitor.
The highest affinity inhibitor for chorismate mutases, a conformationally constrained oxabicyclic dicarboxylate transition state… Expand
Is this relevant?
2002
2002
Refined molecular hinge between allosteric and catalytic domain determines allosteric regulation and stability of fungal chorismate mutase.
The yeast chorismate mutase is regulated by tyrosine as feedback inhibitor and tryptophan as crosspathway activator. The monomer… Expand
  • figure 1
  • figure 2
  • table 1
  • figure 3
  • figure 4
Is this relevant?
1996
1996
Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis.
Chorismate mutase (EC 5.4.99.5) catalyzes the intramolecular rearrangement of chorismate to prephenate. Arg-90 in the active site… Expand
  • figure 1
  • figure 2
  • figure 3
  • table 1
  • figure 4
Is this relevant?
1996
1996
Identification of active site residues of chorismate mutase-prephenate dehydrogenase from Escherichia coli.
Chemical modification studies of the bifunctional enzyme chorismate mutase-prephenate dehydrogenase and mass spectral analysis of… Expand
Is this relevant?
1991
1991
Kinetic studies on chorismate mutase-prephenate dehydrogenase from Escherichia coli: models for the feedback inhibition of prephenate dehydrogenase by L-tyrosine.
Kinetic studies have been undertaken to elucidate the mechanism of the allosteric inhibition by tyrosine of the prephenate… Expand
Is this relevant?
1984
1984
Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate.
The prephenate dehydrogenase activity of the bifunctional enzyme chorismate mutase-prephenate dehydrogenase from Escherichia coli… Expand
Is this relevant?
1974
1974
Regulation of aromatic amino acid biosynthesis in Bacillus subtilis 168. Purification, characterization, and subunit structure of the bifunctional enzyme 3-deoxy-D-arabinoheptulosonate 7-phosphate…
Abstract A bifunctional enzyme, consisting of 3-deoxy-d-arabinoheptulosonate 7-phosphate synthetase and chorismate mutase, has… Expand
  • figure 1
  • table I
  • figure 3
  • figure 4
  • figure 5
Is this relevant?
1970
1970
Biosynthesis of 4-aminobenzoate in Escherichia coli.
Two different mutations (pabA and pabB) affecting 4-aminobenzoate biosynthesis were obtained in strains of Escherichia coli… Expand
Is this relevant?
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License
ACCEPT & CONTINUE