ArticleProceedings of the National Academy of Sciences of the United States of America1997
A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 43 citations in OpenAlex.
- A flexible, allosteric loop regulates protein activity and rewires electrostatics.Protein science : a publication of the Protein Society · 2025Article
- The influence of model building schemes and molecular dynamics sampling on QM-cluster models: the chorismate mutase case study.Physical chemistry chemical physics : PCCP · 2024Article
- Mixed, nonclassical behavior in a classic allosteric protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.Microbial cell factories · 2023Review
- Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance.The Journal of biological chemistry · 2020Article
- Article
- Metabolic priming by a secreted fungal effector.Nature · 2011Article
- Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner.The EMBO journal · 2009Article
- Biochemical and structural characterization of the secreted chorismate mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ enzyme not regulated by the aromatic amino acids.Journal of bacteriology · 2006Article
- Refined molecular hinge between allosteric and catalytic domain determines allosteric regulation and stability of fungal chorismate mutase.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.Microbiology and molecular biology reviews : MMBR · 2001Review
- Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Coevolution of transcriptional and allosteric regulation at the chorismate metabolic branch point of Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- HARO7 encodes chorismate mutase of the methylotrophic yeast Hansenula polymorpha and is derepressed upon methanol utilization.Journal of bacteriology · 2000Article
- Yeast chorismate mutase in the R state: simulations of the active site.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Separation of inhibition and activation of the allosteric yeast chorismate mutase.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Chorismate mutase acts at the first branchpoint of aromatic amino acid biosynthesis and catalyzes the conversion of chorismate to prephenate. Comparison of the x-ray structures of allosteric chorismate mutase from the yeast Saccharomyces cerevisiae with Escherichia coli chorismate mutase/prephenate dehydratase suggested conserved active sites between both enzymes. We have replaced all critical amino acid residues, Arg-16, Arg-157, Lys-168, Glu-198, Thr-242, and Glu-246, of yeast chorismate mutase by aliphatic amino acid residues. The resulting enzymes exhibit the necessity of these residues for catalytic function and provide evidence of their localization at the active site. Unlike some bacterial enzymes, yeast chorismate mutase has highest activity at acidic pH values. Replacement of Glu-246 in the yeast chorismate mutase by glutamine changes the pH optimum for activity of the enzyme from a narrow to a broad pH range. These data suggest that Glu-246 in the catalytic center must be protonated for maximum catalysis and restricts optimal activity of the enzyme to low pH.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.