Component
Phosphoenolpyruvate / PEP
4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
DAHP synthase combines PEP and erythrose-4-phosphate into DAHP.
Experimental context and source evidence
- evidence_access
- Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction. Primary correction read: duplicated Fig. 7 and incorrect panel reference corrected; not a retraction.
- experimental_model
- Escherichia coli biochemical pathway; source-specific enzyme evidence recorded in the passage.
- interpretation_status
- Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
- limitations
- Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.
- plain_language
- DAHP synthase combines PEP and erythrose-4-phosphate into DAHP.
- primary_references
- Metabolic engineering of Escherichia coli for shikimate pathway derivative production from glucose-xylose co-substrate. | 2020 | DOI 10.1038/s41467-019-14024-1 | PMID 31937786 | https://pubmed.ncbi.nlm.nih.gov/31937786/ | https://doi.org/10.1038/s41467-019-14024-1 | https://pmc.ncbi.nlm.nih.gov/articles/PMC6959354/
- primary_references
- Publisher correction to metabolic engineering of Escherichia coli for shikimate pathway derivative production | 2020 | DOI 10.1038/s41467-020-14710-5 | https://www.nature.com/articles/s41467-020-14710-5
- source_locator
- Reviewed reference lines 9-9; exact primary location described in quoted passage where extracted.
Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 9–9
Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Escherichia coli biochemical pathway; source-specific enzyme evidence recorded in the passage. · source_derived_draft · unverified_draft
**Carbon entry: DAHP formation.** The E. coli pathway map joins phosphoenolpyruvate (PEP) and erythrose-4-phosphate (E4P) through DAHP synthase to form 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP), releasing phosphate. These inputs connect central carbon metabolism to aromatic biosynthesis. The cited engineering study provides pathway and flux-redistribution context; its diagram is not a new kinetic assay for every reaction. Its 2020 publisher correction replaces a duplicated Figure 7 and corrects its legend; the current corrected article is the reference. [Metabolic engineering of Escherichia coli for shikimate pathway derivative production from glucose-xylose co-substrate.](https://pubmed.ncbi.nlm.nih.gov/31937786/) [Publisher correction to metabolic engineering of Escherichia coli for shikimate pathway derivative production](https://www.nature.com/articles/s41467-020-14710-5)
Complete structured claim and evidence
Where it participates (unsigned role)
EPSPS uses PEP and shikimate-3-phosphate to produce EPSP and phosphate.
Experimental context and source evidence
- evidence_access
- Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally.
- experimental_model
- Escherichia coli biochemical pathway; source-specific enzyme evidence recorded in the passage.
- interpretation_status
- Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
- limitations
- Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.
- plain_language
- EPSPS uses PEP and shikimate-3-phosphate to produce EPSP and phosphate.
- primary_references
- Molecular basis for the herbicide resistance of Roundup Ready crops. | 2006 | DOI 10.1073/pnas.0603638103 | PMID 16916934 | https://pubmed.ncbi.nlm.nih.gov/16916934/ | https://doi.org/10.1073/pnas.0603638103 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1559744/
- source_locator
- Reviewed reference lines 17-17; exact primary location described in quoted passage where extracted.
Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 17–17
Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Escherichia coli biochemical pathway; source-specific enzyme evidence recorded in the passage. · source_derived_draft · unverified_draft
**EPSPS uses a second PEP molecule.** E. coli EPSPS (AroA) transfers an enolpyruvyl group from a second PEP molecule to shikimate-3-phosphate, making 5-enolpyruvylshikimate-3-phosphate (EPSP) and phosphate. Glyphosate inhibits this enzyme by occupying the PEP-associated substrate site in the substrate-bound enzyme. Purified-enzyme IC50 estimates were about 2.5 µM for E. coli EPSPS and 11 mM for CP4 EPSPS. These are not interchangeable microbial-growth thresholds or human intestinal effect concentrations. Adding shikimate upstream does not remove the need for EPSPS downstream. [Molecular basis for the herbicide resistance of Roundup Ready crops.](https://pubmed.ncbi.nlm.nih.gov/16916934/)
Complete structured claim and evidenceGlyphosate inhibited cp4-epsps with an approximate purified-enzyme IC50 of 11 millimolar.
Experimental context and source evidence
- evidence_access
- Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally.
- experimental_contrast
- {"intervention": "Glyphosate titration", "comparator": "Enzyme without glyphosate", "endpoint": "Glyphosate inhibited cp4-epsps with an approximate purified-enzyme IC50 of 11 millimolar.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
- experimental_model
- Purified enzyme comparison, Funke 2006.
- interpretation_status
- Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
- limitations
- IC50 depends on assay conditions; not a growth threshold, dietary exposure limit or complete microbiome response.
- plain_language
- Glyphosate inhibited cp4-epsps with an approximate purified-enzyme IC50 of 11 millimolar.
- primary_references
- Molecular basis for the herbicide resistance of Roundup Ready crops. | 2006 | DOI 10.1073/pnas.0603638103 | PMID 16916934 | https://pubmed.ncbi.nlm.nih.gov/16916934/ | https://doi.org/10.1073/pnas.0603638103 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1559744/
- source_locator
- Reviewed reference lines 17-17; exact primary location described in quoted passage where extracted.
Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 17–17
Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Purified enzyme comparison, Funke 2006. · source_derived_draft · unverified_draft
**EPSPS uses a second PEP molecule.** E. coli EPSPS (AroA) transfers an enolpyruvyl group from a second PEP molecule to shikimate-3-phosphate, making 5-enolpyruvylshikimate-3-phosphate (EPSP) and phosphate. Glyphosate inhibits this enzyme by occupying the PEP-associated substrate site in the substrate-bound enzyme. Purified-enzyme IC50 estimates were about 2.5 µM for E. coli EPSPS and 11 mM for CP4 EPSPS. These are not interchangeable microbial-growth thresholds or human intestinal effect concentrations. Adding shikimate upstream does not remove the need for EPSPS downstream. [Molecular basis for the herbicide resistance of Roundup Ready crops.](https://pubmed.ncbi.nlm.nih.gov/16916934/)
Complete structured claim and evidenceGlyphosate inhibited ecoli-aroa with an approximate purified-enzyme IC50 of 2.5 micromolar.
Experimental context and source evidence
- evidence_access
- Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally.
- experimental_contrast
- {"intervention": "Glyphosate titration", "comparator": "Enzyme without glyphosate", "endpoint": "Glyphosate inhibited ecoli-aroa with an approximate purified-enzyme IC50 of 2.5 micromolar.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
- experimental_model
- Purified enzyme comparison, Funke 2006.
- interpretation_status
- Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
- limitations
- IC50 depends on assay conditions; not a growth threshold, dietary exposure limit or complete microbiome response.
- plain_language
- Glyphosate inhibited ecoli-aroa with an approximate purified-enzyme IC50 of 2.5 micromolar.
- primary_references
- Molecular basis for the herbicide resistance of Roundup Ready crops. | 2006 | DOI 10.1073/pnas.0603638103 | PMID 16916934 | https://pubmed.ncbi.nlm.nih.gov/16916934/ | https://doi.org/10.1073/pnas.0603638103 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1559744/
- source_locator
- Reviewed reference lines 17-17; exact primary location described in quoted passage where extracted.
Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 17–17
Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Purified enzyme comparison, Funke 2006. · source_derived_draft · unverified_draft
**EPSPS uses a second PEP molecule.** E. coli EPSPS (AroA) transfers an enolpyruvyl group from a second PEP molecule to shikimate-3-phosphate, making 5-enolpyruvylshikimate-3-phosphate (EPSP) and phosphate. Glyphosate inhibits this enzyme by occupying the PEP-associated substrate site in the substrate-bound enzyme. Purified-enzyme IC50 estimates were about 2.5 µM for E. coli EPSPS and 11 mM for CP4 EPSPS. These are not interchangeable microbial-growth thresholds or human intestinal effect concentrations. Adding shikimate upstream does not remove the need for EPSPS downstream. [Molecular basis for the herbicide resistance of Roundup Ready crops.](https://pubmed.ncbi.nlm.nih.gov/16916934/)
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.