Paper348236
Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme.
Duggleby RG and 2 others. Biochemistry, 1978. Cited by 35 papers, by iCite.
11 sourcespapers-2026-11-12-0.1.0
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ConductScience Library. Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme. Papers, record 348236. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/348236
Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
- Chorismate mutase-prephenate dehydratase from Escherichia coli: active sites of a bifunctional enzyme.
- PubMed
Topics7
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| Escherichia coli | Major topic |
| Hydro-Lyases | Major topic |
| Prephenate Dehydratase | Major topic |
| Binding Sites | |
| Catalysis | |
| Kinetics | |
| Models, Chemical |
Source PubMed
Cited by7
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 35 citations.
| PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|
| 41,057,320 | Metabolic interplay drives population cycles in a cross-feeding microbial community. | Nat Commun | 2025 | https://conductscience.org/library/papers/41057320 | PubMed |
| 33,101,336 | Putative Bifunctional Chorismate Mutase/Prephenate Dehydratase Contributes to the Virulence of Acidovorax citrulli. | Front Plant Sci | 2020 | https://conductscience.org/library/papers/33101336 | PubMed |
| 30,370,221 | Bacterial bifunctional chorismate mutase-prephenate dehydratase PheA increases flux into the yeast phenylalanine pathway and improves mandelic acid production. | Metab Eng Commun | 2018 | https://conductscience.org/library/papers/30370221 | PubMed |
| 16,731,976 | Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus. | Protein Sci | 2006 | https://conductscience.org/library/papers/16731976 | PubMed |
| 8,358,292 | In situ conversion of coproporphyrinogen to heme by murine mitochondria: terminal steps of the heme biosynthetic pathway. | Protein Sci | 1993 | https://conductscience.org/library/papers/8358292 | PubMed |
| 3,707,530 | The effect of feedback on pathway transient response. | Biochem J | 1986 | https://conductscience.org/library/papers/3707530 | PubMed |
| 2,865,249 | Occurrence of succinyl derivatives in the catabolism of arginine in Pseudomonas cepacia. | J Bacteriol | 1985 | https://conductscience.org/library/papers/2865249 | PubMed |
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- 2026-11-12
- Gene search
- 2026-11-11
- Pipelines
- 2026-09-18
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- ChEMBL, through Open TargetsCC BY-SA 3.0
- ClinicalTrials.govNo license stated
- HGNCCC0
- iCiteCC BY 4.0
- NCBI GenePublic domain (US government)
- NIH RePORTER's grant and paper linksPublic domain
- Open TargetsCC0 1.0
- PMC's ID filePublic domain (US government)
- PubMedNLM's terms
- PubTator 3Public domain
- UniProtCC BY 4.0
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- ChEMBL, through Open TargetsCC BY-SA 3.0, for the parts from ChEMBL. Read on 8 Nov 2026 at https://platform-docs.opentargets.org/licence
- ClinicalTrials.govnone stated
- HGNCCC0: https://www.genenames.org/about/license/
- iCiteCC BY 4.0
- NCBI GeneNone named for the file. NCBI says information created by or for the US government on its site is in the public domain, and asks that NLM be acknowledged: https://www.ncbi.nlm.nih.gov/home/about/policies/
- NIH RePORTER's grant and paper linksPublic domain (NIH RePORTER)
- Open TargetsCC0 1.0. Open Targets asks that users cite its latest paper: Buniello et al. 2025, Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery, Nucleic Acids Research 53(D1):D1467, PMID 39657122. Read on 8 Nov 2026 at https://platform-docs.opentargets.org/licence
- PMC's ID fileNone named for the file. NCBI says information created by or for the US government on its site is in the public domain, and asks that NLM be acknowledged: https://www.ncbi.nlm.nih.gov/home/about/policies/
- PubMedNLM's terms
- PubTator 3Public domain
- UniProtCC BY 4.0. UniProt's licence file: "All databases and documents in the UniProt FTP directory may be copied and redistributed freely, without advance permission, provided that this copyright statement is reproduced with each copy." UniProt asks that users cite its latest paper: The UniProt Consortium, UniProt: the Universal Protein Knowledgebase in 2025, Nucleic Acids Research 53:D609-D617, https://doi.org/10.1093/nar/gkae1010. Read on 9 Nov 2026 at https://www.uniprot.org/help/license
ClinicalTrials.gov's data carry an international copyright outside the United States: https://clinicaltrials.gov/about-site/terms-conditions.
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