ArticleThe EMBO journal2009
Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner.
Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 60 citations in OpenAlex.
- (Reverse) Evolution of a Promiscuous Isochorismate Pyruvate Lyase into an Efficient Chorismate Mutase.Biochemistry · 2025Article
- A general assay platform to study protein pharmacology using ligand-dependent structural dynamics.Nature communications · 2025Article
- Transposon sequencing reveals metabolic pathways essential for Mycobacterium tuberculosis infection.PLoS pathogens · 2024Article
- Influence of Cysteine 440 on the Active Site Properties of 3-Deoxy-d-Arabino-Heptulosonate 7-Phosphate Synthase inACS omega · 2023Article
- What Drives Chorismate Mutase to Top Performance? Insights from a CombinedBiochemistry · 2023Article
- Evaluation of 3-Deoxy-D-Arabino-Heptulosonate 7-Phosphate Synthase (DAHPS) as a Vulnerable Target in Mycobacterium tuberculosis.Microbiology spectrum · 2022Article
- 6-Fluorophenylbenzohydrazides inhibit Mycobacterium tuberculosis growth through alteration of tryptophan biosynthesis.European journal of medicinal chemistry · 2021Article
- The Quantitative Trait Loci Mapping of Rice Plant and the Components of Its Extract Confirmed the Anti-Inflammatory and Platelet Aggregation Effects In Vitro and In Vivo.Antioxidants (Basel, Switzerland) · 2021Article
- Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance.The Journal of biological chemistry · 2020Article
- A single amino acid substitution uncouples catalysis and allostery in an essential biosynthetic enzyme inThe Journal of biological chemistry · 2020Article
- Crystal structure of the TreS:Pep2 complex, initiating α-glucan synthesis in the GlgE pathway of mycobacteria.The Journal of biological chemistry · 2019Article
- Domain cross-talk within a bifunctional enzyme provides catalytic and allosteric functionality in the biosynthesis of aromatic amino acids.The Journal of biological chemistry · 2019Article
- Article
- Structural and functional characterisation of the entry point to pyocyanin biosynthesis inBioscience reports · 2018Article
- Structure of Chorismate Mutase-like Domain of DAHPS from Bacillus subtilis Complexed with Novel Inhibitor Reveals Conformational Plasticity of Active Site.Scientific reports · 2017Article
- X-ray Scattering Studies of Protein Structural Dynamics.Chemical reviews · 2017Review
- Spatial Organization of Metabolic Enzyme Complexes in Cells.Biochemistry · 2017Review
- Quantum chemical modeling of the reaction path of chorismate mutase based on the experimental substrate/product complex.FEBS open bio · 2017Article
- Article
- Interdomain Conformational Changes Provide Allosteric Regulation en Route to Chorismate.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chorismate mutase catalyzes a key step in the shikimate biosynthetic pathway towards phenylalanine and tyrosine. Curiously, the intracellular chorismate mutase of Mycobacterium tuberculosis (MtCM; Rv0948c) has poor activity and lacks prominent active-site residues. However, its catalytic efficiency increases >100-fold on addition of DAHP synthase (MtDS; Rv2178c), another shikimate-pathway enzyme. The 2.35 A crystal structure of the MtCM-MtDS complex bound to a transition-state analogue shows a central core formed by four MtDS subunits sandwiched between two MtCM dimers. Structural comparisons imply catalytic activation to be a consequence of the repositioning of MtCM active-site residues on binding to MtDS. The mutagenesis of the C-terminal extrusion of MtCM establishes conserved residues as part of the activation machinery. The chorismate-mutase activity of the complex, but not of MtCM alone, is inhibited synergistically by phenylalanine and tyrosine. The complex formation thus endows the shikimate pathway of M. tuberculosis with an important regulatory feature. Experimental evidence suggests that such non-covalent enzyme complexes comprising an AroQ(delta) subclass chorismate mutase like MtCM are abundant in the bacterial order Actinomycetales.
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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.