Component

Enterococcus faecalis tyrosine decarboxylase

Enterococcus faecalis tyrosine decarboxylase

3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

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.

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.

Recorded relationships

What it acts on

  1. Bacterial tyrosine decarboxylases converted levodopa to dopamine despite competing tyrosine or human decarboxylase inhibitors.

    Enterococcus faecalis tyrosine decarboxylase → L-3,4-Dihydroxyphenylalanine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Bacterial enzyme experiments, human PD associations and proximal-intestinal rat studies.
    limitations
    Patient abundance associations and rat plasma effects are not proof that changing dietary tyrosine improves levodopa response.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    Blocking the human enzyme may leave a microbial route active.
    primary_references
    Gut bacterial tyrosine decarboxylases restrict levels of levodopa in the treatment of Parkinson's disease. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30659181/ · DOI 10.1038/s41467-019-08294-y

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 340–346

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Bacterial enzyme experiments, human PD associations and proximal-intestinal rat studies. · source_derived_draft · unverified_draft

    ## l-tyrosine-bacterial-drug Blocking the human enzyme may leave a microbial route active. Bacterial tyrosine decarboxylases converted levodopa to dopamine despite competing tyrosine or human decarboxylase inhibitors. Model: Bacterial enzyme experiments, human PD associations and proximal-intestinal rat studies. Limitations: Patient abundance associations and rat plasma effects are not proof that changing dietary tyrosine improves levodopa response. Evidence access: Primary abstract Gut bacterial tyrosine decarboxylases restrict levels of levodopa in the treatment of Parkinson's disease. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30659181/ · DOI 10.1038/s41467-019-08294-y
    Complete structured claim and evidence

  2. Gut bacterial tyrosine decarboxylase accepts tyrosine and also decarboxylates levodopa.

    Enterococcus faecalis tyrosine decarboxylase → Tyramine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Gut bacterial enzyme/substrate characterization.
    limitations
    This is bacterial metabolism, distinct from human DDC. Tyramine exposure from food is not equivalent to free tyrosine intake.
    nutrient_topic
    L-Tyrosine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Tyrosine
    plain_language
    Microbes can divert the amino acid into a bioactive amine.
    primary_references
    Gut bacterial tyrosine decarboxylases restrict levels of levodopa in the treatment of Parkinson's disease. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30659181/ · DOI 10.1038/s41467-019-08294-y

    L-Tyrosine: catecholamines, thyroid chemistry, pigment, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 332–338

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Gut bacterial enzyme/substrate characterization. · source_derived_draft · unverified_draft

    ## l-tyrosine-bacterial-tyramine Microbes can divert the amino acid into a bioactive amine. Gut bacterial tyrosine decarboxylase accepts tyrosine and also decarboxylates levodopa. Model: Gut bacterial enzyme/substrate characterization. Limitations: This is bacterial metabolism, distinct from human DDC. Tyramine exposure from food is not equivalent to free tyrosine intake. Evidence access: Primary abstract Gut bacterial tyrosine decarboxylases restrict levels of levodopa in the treatment of Parkinson's disease. · 2019 · https://pubmed.ncbi.nlm.nih.gov/30659181/ · DOI 10.1038/s41467-019-08294-y
    Complete structured claim and evidence

What acts on it

  1. Pyridoxine inhibited the tested PLP-dependent bacterial tyrosine decarboxylase preparation.

    Pyridoxine → Enterococcus faecalis tyrosine decarboxylase source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Differentiated human SH-SY5Y and CaCo-2 cells; isolated enzyme assays
    exposure
    5 micromolar pyridoxine; commercial Streptococcus faecalis enzyme (current Enterococcus name).
    exposure-class
    Experimental excess pyridoxine; not dietary B6 deficiency · Pyridoxine
    limitations
    Not human GAD, DDC or PDXK; mechanism of human neuropathy remains unresolved.
    nutrient_topic
    Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B6
    organism
    Enterococcus faecalis (reported as Streptococcus faecalis)
    plain_language
    Pyridoxine interfered with one isolated B6-dependent enzyme.
    primary_references
    [vrolijk-2017-pn] The vitamin B6 paradox: Supplementation with high concentrations of pyridoxine leads to decreased vitamin B6 function (2017). https://doi.org/10.1016/j.tiv.2017.07.009 DOI: 10.1016/j.tiv.2017.07.009
    tissue_or_cell_type
    Cell-free bacterial enzyme

    Vitamin B6: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1258–1269

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Differentiated human SH-SY5Y and CaCo-2 cells; isolated enzyme assays · source_derived_draft · unverified_draft

    ### b6-neuro-pn-enzyme-inhibition Pyridoxine inhibited the tested PLP-dependent bacterial tyrosine decarboxylase preparation. Condition category: normal nutrient_topic: Vitamin B6 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Pyridoxine interfered with one isolated B6-dependent enzyme. organism: Enterococcus faecalis (reported as Streptococcus faecalis) tissue_or_cell_type: Cell-free bacterial enzyme experimental_model: Differentiated human SH-SY5Y and CaCo-2 cells; isolated enzyme assays limitations: Not human GAD, DDC or PDXK; mechanism of human neuropathy remains unresolved. exposure: 5 micromolar pyridoxine; commercial Streptococcus faecalis enzyme (current Enterococcus name). exposure-class: Experimental excess pyridoxine; not dietary B6 deficiency [vrolijk-2017-pn] The vitamin B6 paradox: Supplementation with high concentrations of pyridoxine leads to decreased vitamin B6 function (2017). https://doi.org/10.1016/j.tiv.2017.07.009 DOI: 10.1016/j.tiv.2017.07.009
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards