Shikimate anion

evidence_access

Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally. Primary publisher article introductory text reviewed; precise affinity estimates are contextual, not newly remeasured.

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

The ecoli-arok kinase phosphorylates shikimate using ATP.

primary_references

Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine. | 2001 | DOI 10.1110/ps.52501 | PMID 11369852 | https://pubmed.ncbi.nlm.nih.gov/11369852/ | https://doi.org/10.1110/ps.52501 | https://pmc.ncbi.nlm.nih.gov/articles/PMC2374015/

primary_references

Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam. | 2002 | DOI 10.1002/prot.10099 | PMID 12001235 | https://pubmed.ncbi.nlm.nih.gov/12001235/ | https://doi.org/10.1002/prot.10099

source_locator

Reviewed reference lines 15-15; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 15–15

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

**ATP and magnesium at shikimate kinase.** Shikimate kinase transfers a phosphoryl group from ATP to shikimate, yielding shikimate-3-phosphate and ADP. The Erwinia chrysanthemi enzyme study identifies magnesium dependence and a Mg–ADP structural complex; this is a microbial enzyme requirement, not a demonstrated human magnesium-deficiency phenotype. E. coli has AroK and AroL kinase isoenzymes with different substrate affinities. The AroK structural paper discusses approximate shikimate Km values of 20 mM versus 0.2 mM for the two systems; these are organism/assay properties, not plasma targets. Loss of both kinases produces aromatic-amino-acid auxotrophy; environmental nutrient rescue and isoenzyme compensation matter. [Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.](https://pubmed.ncbi.nlm.nih.gov/11369852/) [Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam.](https://pubmed.ncbi.nlm.nih.gov/12001235/)

evidence_access

Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally. Primary publisher article introductory text reviewed; precise affinity estimates are contextual, not newly remeasured.

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

The ecoli-arol kinase phosphorylates shikimate using ATP.

primary_references

Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine. | 2001 | DOI 10.1110/ps.52501 | PMID 11369852 | https://pubmed.ncbi.nlm.nih.gov/11369852/ | https://doi.org/10.1110/ps.52501 | https://pmc.ncbi.nlm.nih.gov/articles/PMC2374015/

primary_references

Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam. | 2002 | DOI 10.1002/prot.10099 | PMID 12001235 | https://pubmed.ncbi.nlm.nih.gov/12001235/ | https://doi.org/10.1002/prot.10099

source_locator

Reviewed reference lines 15-15; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 15–15

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

**ATP and magnesium at shikimate kinase.** Shikimate kinase transfers a phosphoryl group from ATP to shikimate, yielding shikimate-3-phosphate and ADP. The Erwinia chrysanthemi enzyme study identifies magnesium dependence and a Mg–ADP structural complex; this is a microbial enzyme requirement, not a demonstrated human magnesium-deficiency phenotype. E. coli has AroK and AroL kinase isoenzymes with different substrate affinities. The AroK structural paper discusses approximate shikimate Km values of 20 mM versus 0.2 mM for the two systems; these are organism/assay properties, not plasma targets. Loss of both kinases produces aromatic-amino-acid auxotrophy; environmental nutrient rescue and isoenzyme compensation matter. [Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.](https://pubmed.ncbi.nlm.nih.gov/11369852/) [Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam.](https://pubmed.ncbi.nlm.nih.gov/12001235/)

evidence_access

Primary indexed abstract reviewed; full results, tables and supplements not independently extracted.

experimental_model

E. coli 1966 isotope tracing; shikimate ring carbon versus methionine methyl carbon.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Carbon incorporation, not complete enzymatic sequence, human MK-7 production or oral vitamin-K efficacy.

plain_language

Isotope-labeled shikimate contributed carbon to E. coli MK-8 in the historical labeling experiment.

primary_references

Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate. | 1974 | DOI 10.1128/jb.118.1.41-45.1974 | PMID 4595202 | https://pubmed.ncbi.nlm.nih.gov/4595202/ | https://doi.org/10.1128/jb.118.1.41-45.1974 | https://pmc.ncbi.nlm.nih.gov/articles/PMC246637/

primary_references

The role of shikimic acid in the biosynthesis of vitamin K2. | 1966 | DOI 10.1042/bj1000001 | PMID 5337721 | https://pubmed.ncbi.nlm.nih.gov/5337721/ | https://doi.org/10.1042/bj1000001 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1265084/

source_locator

Reviewed reference lines 27-27; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 27–27

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 · E. coli 1966 isotope tracing; shikimate ring carbon versus methionine methyl carbon. · source_derived_draft · unverified_draft

**The K and Q branches are organism-specific.** Isotope experiments in E. coli traced shikimate carbon into the benzene ring of menaquinone-8 (MK-8), and methionine-derived methyl carbon into that product. This does not establish increased human MK-7, vitamin-K function or an oral shikimate dose response. Separately, an E. coli ubiC mutant failed to convert chorismate to 4-hydroxybenzoate and produced little ubiquinone unless supplied with 4-hydroxybenzoate. UbiC therefore identifies a branch-specific supply bottleneck; bacterial ubiquinone production is not synonymous with human mitochondrial CoQ10 synthesis. [The role of shikimic acid in the biosynthesis of vitamin K2.](https://pubmed.ncbi.nlm.nih.gov/5337721/) [Biosynthesis of ubiquinone in Escherichia coli K-12: biochemical and genetic characterization of a mutant unable to convert chorismate into 4-hydroxybenzoate.](https://pubmed.ncbi.nlm.nih.gov/4595202/)

evidence_access

Authoritative chemical identity/property records, PUG REST properties retrieved; not a biological experiment. Primary indexed abstract reviewed; full results, tables and supplements not independently extracted.

experimental_model

Chemical identity records; acid-base relation rather than a therapeutic effect.

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

Shikimate is the carboxylate conjugate base of shikimic acid, with the same stereochemical scaffold.

primary_references

PubChem shikimic acid CID 8742 and shikimate CID 7057976 | 2026 | https://pubchem.ncbi.nlm.nih.gov/compound/8742 | https://pubchem.ncbi.nlm.nih.gov/compound/7057976

primary_references

The metabolism of shikimate in the rat. | 1978 | DOI 10.1042/bj1700257 | PMID 637841 | https://pubmed.ncbi.nlm.nih.gov/637841/ | https://doi.org/10.1042/bj1700257 | https://pmc.ncbi.nlm.nih.gov/articles/PMC1183892/

source_locator

Reviewed reference lines 5-5; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 5–5

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 · Chemical identity records; acid-base relation rather than a therapeutic effect. · source_derived_draft · unverified_draft

**One chemical scaffold, two protonation states.** Shikimic acid is (3R,4S,5R)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid, C7H10O5, molecular mass 174.15 g/mol. Its ring is not aromatic, so calling it a phenolic compound is chemically misleading even when a paper does so. Shikimate is its carboxylate conjugate base (C7H9O5−); charge is meaningful, but these must remain connected identities. Neither is oseltamivir, anisatin, triacetylshikimic acid or 3,4-O-isopropylidene shikimic acid. Plants and many microorganisms use the biosynthetic pathway; humans have no complete endogenous shikimate pathway. Absence of that pathway does not mean an ingested molecule cannot be absorbed or metabolized by the host–microbiome system. [PubChem shikimic acid CID 8742 and shikimate CID 7057976](https://pubchem.ncbi.nlm.nih.gov/compound/8742) [The metabolism of shikimate in the rat.](https://pubmed.ncbi.nlm.nih.gov/637841/)

evidence_access

Primary indexed abstract reviewed; full results, tables and supplements not independently extracted. Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction.

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

AroE reduces DHS to shikimate with NADPH oxidation to NADP+.

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

Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. | 2003 | DOI 10.1074/jbc.m300794200 | PMID 12637497 | https://pubmed.ncbi.nlm.nih.gov/12637497/ | https://doi.org/10.1074/jbc.m300794200

source_locator

Reviewed reference lines 13-13; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 13–13

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

**NADPH supplies reducing equivalents.** E. coli AroE reduces DHS to shikimate using NADPH, producing NADP+. The reaction is reversible; direction depends on conditions. Primary structural/biochemical work distinguishes NADP-specific AroE from paralog YdiB, which accepts NAD or NADP and has quinate/shikimate dehydrogenase activity. Do not give every homolog identical cofactor specificity or infer that human niacin supplementation necessarily increases gut pathway flux. [Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.](https://pubmed.ncbi.nlm.nih.gov/12637497/) [Metabolic engineering of Escherichia coli for shikimate pathway derivative production from glucose-xylose co-substrate.](https://pubmed.ncbi.nlm.nih.gov/31937786/)

evidence_access

Primary indexed abstract reviewed; full results, tables and supplements not independently extracted. Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction.

experimental_model

E. coli enzyme cofactor specificity.

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

NADPH provides reducing equivalents for the biosynthetic AroE reaction.

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

Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities. | 2003 | DOI 10.1074/jbc.m300794200 | PMID 12637497 | https://pubmed.ncbi.nlm.nih.gov/12637497/ | https://doi.org/10.1074/jbc.m300794200

source_locator

Reviewed reference lines 13-13; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 13–13

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 · E. coli enzyme cofactor specificity. · source_derived_draft · unverified_draft

**NADPH supplies reducing equivalents.** E. coli AroE reduces DHS to shikimate using NADPH, producing NADP+. The reaction is reversible; direction depends on conditions. Primary structural/biochemical work distinguishes NADP-specific AroE from paralog YdiB, which accepts NAD or NADP and has quinate/shikimate dehydrogenase activity. Do not give every homolog identical cofactor specificity or infer that human niacin supplementation necessarily increases gut pathway flux. [Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.](https://pubmed.ncbi.nlm.nih.gov/12637497/) [Metabolic engineering of Escherichia coli for shikimate pathway derivative production from glucose-xylose co-substrate.](https://pubmed.ncbi.nlm.nih.gov/31937786/)

evidence_access

Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction.

experimental_model

Female Sprague–Dawley rats; 0.5, 50 and 175 mg/kg/day glyphosate-equivalent groups; 12/group.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Study-level direction; no unsupported per-dose significance claim. Pool accumulation is not increased downstream flux.

plain_language

The 90-day glyphosate study recorded cecal shikimate accumulation consistent with pathway inhibition.

primary_references

Use of Shotgun Metagenomics and Metabolomics to Evaluate the Impact of Glyphosate or Roundup MON 52276 on the Gut Microbiota and Serum Metabolome of Sprague-Dawley Rats. | 2021 | DOI 10.1289/ehp6990 | PMID 33502259 | https://pubmed.ncbi.nlm.nih.gov/33502259/ | https://doi.org/10.1289/ehp6990 | https://pmc.ncbi.nlm.nih.gov/articles/PMC7839352/

source_locator

Reviewed reference lines 37-37; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 37–37

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 · Female Sprague–Dawley rats; 0.5, 50 and 175 mg/kg/day glyphosate-equivalent groups; 12/group. · source_derived_draft · unverified_draft

**An upstream pool can rise when flux is blocked.** Mesnage 2021 compared pure glyphosate and Roundup MON52276 in female Sprague–Dawley rats for 90 days at 0.5, 50 and 175 mg/kg/day glyphosate-equivalent exposures, with 12 animals per group. Cecal shikimate and DHS accumulation supported pathway inhibition; abundance alone was less informative. The collection records study-level accumulation rather than asserting every dose had an identical significant effect. Overall alpha-diversity differences were not significant (p=0.09), while beta diversity differed. Selected low-abundance taxa changed, and formulation-specific differences remained. Serum shikimate was undetected with the employed method, whose sensitivity and protein interference limit a zero-exposure interpretation. [Use of Shotgun Metagenomics and Metabolomics to Evaluate the Impact of Glyphosate or Roundup MON 52276 on the Gut Microbiota and Serum Metabolome of Sprague-Dawley Rats.](https://pubmed.ncbi.nlm.nih.gov/33502259/)

evidence_access

Primary full-text HTML and indexed abstract reviewed for the stated results; archived locally. Primary publisher article introductory text reviewed; precise affinity estimates are contextual, not newly remeasured.

experimental_model

Purified Erwinia chrysanthemi enzyme and Mg–ADP structure.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

No human magnesium dose threshold or E. coli-specific quantitative affinity inferred.

plain_language

The studied Erwinia shikimate kinase requires magnesium for its ATP-dependent reaction.

primary_references

Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine. | 2001 | DOI 10.1110/ps.52501 | PMID 11369852 | https://pubmed.ncbi.nlm.nih.gov/11369852/ | https://doi.org/10.1110/ps.52501 | https://pmc.ncbi.nlm.nih.gov/articles/PMC2374015/

primary_references

Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam. | 2002 | DOI 10.1002/prot.10099 | PMID 12001235 | https://pubmed.ncbi.nlm.nih.gov/12001235/ | https://doi.org/10.1002/prot.10099

source_locator

Reviewed reference lines 15-15; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 15–15

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 Erwinia chrysanthemi enzyme and Mg–ADP structure. · source_derived_draft · unverified_draft

**ATP and magnesium at shikimate kinase.** Shikimate kinase transfers a phosphoryl group from ATP to shikimate, yielding shikimate-3-phosphate and ADP. The Erwinia chrysanthemi enzyme study identifies magnesium dependence and a Mg–ADP structural complex; this is a microbial enzyme requirement, not a demonstrated human magnesium-deficiency phenotype. E. coli has AroK and AroL kinase isoenzymes with different substrate affinities. The AroK structural paper discusses approximate shikimate Km values of 20 mM versus 0.2 mM for the two systems; these are organism/assay properties, not plasma targets. Loss of both kinases produces aromatic-amino-acid auxotrophy; environmental nutrient rescue and isoenzyme compensation matter. [Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.](https://pubmed.ncbi.nlm.nih.gov/11369852/) [Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam.](https://pubmed.ncbi.nlm.nih.gov/12001235/)

evidence_access

Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction.

experimental_model

Female Sprague–Dawley rats; 0.5, 50 and 175 mg/kg/day glyphosate-equivalent groups; 12/group.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Study-level direction; no unsupported per-dose significance claim. Pool accumulation is not increased downstream flux.

plain_language

The 90-day roundup-mon52276 study recorded cecal shikimate accumulation consistent with pathway inhibition.

primary_references

Use of Shotgun Metagenomics and Metabolomics to Evaluate the Impact of Glyphosate or Roundup MON 52276 on the Gut Microbiota and Serum Metabolome of Sprague-Dawley Rats. | 2021 | DOI 10.1289/ehp6990 | PMID 33502259 | https://pubmed.ncbi.nlm.nih.gov/33502259/ | https://doi.org/10.1289/ehp6990 | https://pmc.ncbi.nlm.nih.gov/articles/PMC7839352/

source_locator

Reviewed reference lines 37-37; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 37–37

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 · Female Sprague–Dawley rats; 0.5, 50 and 175 mg/kg/day glyphosate-equivalent groups; 12/group. · source_derived_draft · unverified_draft

**An upstream pool can rise when flux is blocked.** Mesnage 2021 compared pure glyphosate and Roundup MON52276 in female Sprague–Dawley rats for 90 days at 0.5, 50 and 175 mg/kg/day glyphosate-equivalent exposures, with 12 animals per group. Cecal shikimate and DHS accumulation supported pathway inhibition; abundance alone was less informative. The collection records study-level accumulation rather than asserting every dose had an identical significant effect. Overall alpha-diversity differences were not significant (p=0.09), while beta diversity differed. Selected low-abundance taxa changed, and formulation-specific differences remained. Serum shikimate was undetected with the employed method, whose sensitivity and protein interference limit a zero-exposure interpretation. [Use of Shotgun Metagenomics and Metabolomics to Evaluate the Impact of Glyphosate or Roundup MON 52276 on the Gut Microbiota and Serum Metabolome of Sprague-Dawley Rats.](https://pubmed.ncbi.nlm.nih.gov/33502259/)

evidence_access

Primary full text retrieved; relevant methods/results/figures reviewed. Selective extraction, not raw-data reanalysis or exhaustive supplemental extraction.

experimental_model

Rat serum assay with matrix and sensitivity limitations.

interpretation_status

Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.

limitations

Non-detection is not zero concentration, proof of no absorption or a measured decline.

plain_language

Serum shikimate was not detected by the reported analytical method in the 90-day study.

primary_references

Use of Shotgun Metagenomics and Metabolomics to Evaluate the Impact of Glyphosate or Roundup MON 52276 on the Gut Microbiota and Serum Metabolome of Sprague-Dawley Rats. | 2021 | DOI 10.1289/ehp6990 | PMID 33502259 | https://pubmed.ncbi.nlm.nih.gov/33502259/ | https://doi.org/10.1289/ehp6990 | https://pmc.ncbi.nlm.nih.gov/articles/PMC7839352/

source_locator

Reviewed reference lines 37-37; exact primary location described in quoted passage where extracted.

Shikimic acid: detailed mechanisms of action (reviewed 5 October 2026) · lines 37–37

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 · Rat serum assay with matrix and sensitivity limitations. · source_derived_draft · unverified_draft

**An upstream pool can rise when flux is blocked.** Mesnage 2021 compared pure glyphosate and Roundup MON52276 in female Sprague–Dawley rats for 90 days at 0.5, 50 and 175 mg/kg/day glyphosate-equivalent exposures, with 12 animals per group. Cecal shikimate and DHS accumulation supported pathway inhibition; abundance alone was less informative. The collection records study-level accumulation rather than asserting every dose had an identical significant effect. Overall alpha-diversity differences were not significant (p=0.09), while beta diversity differed. Selected low-abundance taxa changed, and formulation-specific differences remained. Serum shikimate was undetected with the employed method, whose sensitivity and protein interference limit a zero-exposure interpretation. [Use of Shotgun Metagenomics and Metabolomics to Evaluate the Impact of Glyphosate or Roundup MON 52276 on the Gut Microbiota and Serum Metabolome of Sprague-Dawley Rats.](https://pubmed.ncbi.nlm.nih.gov/33502259/)