Component

Human pterin-4-alpha-carbinolamine dehydratase / PCBD1

Context-specific entity; species, compartment and exposure are stated on each claim.

4 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. Two of three adults with homozygous PCBD1 mutations had hypomagnesemia with renal magnesium loss.

    Human pterin-4-alpha-carbinolamine dehydratase / PCBD1 → Urinary magnesium excretion source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Small human case series, three adults with homozygous PCBD1 mutations.
    limitations
    Two also had MODY-like diabetes regardless of magnesium status; neither finding establishes that phenylalanine supplements cause or correct the disorder.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    A genetic defect can connect abnormal phenylalanine handling with magnesium wasting.
    primary_references
    Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24204001/ · DOI 10.1681/ASN.2013040337
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 94–100

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Small human case series, three adults with homozygous PCBD1 mutations. · source_derived_draft · unverified_draft

    ## l-phenylalanine-pcbd-magnesium A genetic defect can connect abnormal phenylalanine handling with magnesium wasting. Two of three adults with homozygous PCBD1 mutations had hypomagnesemia with renal magnesium loss. Model: Small human case series, three adults with homozygous PCBD1 mutations. Limitations: Two also had MODY-like diabetes regardless of magnesium status; neither finding establishes that phenylalanine supplements cause or correct the disorder. Evidence access: Primary abstract Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24204001/ · DOI 10.1681/ASN.2013040337
    Complete structured claim and evidence

  2. Five of seven tested PCBD1 mutations caused proteolytic instability and reduced FXYD2 promoter activity.

    Human pterin-4-alpha-carbinolamine dehydratase / PCBD1 → Human sodium/potassium ATPase regulatory subunit / FXYD2 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human PCBD1 variant expression and promoter assays.
    limitations
    Variant effects are not uniform and do not establish dietary phenylalanine deficiency.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    Some mutations damage the protein and weaken its kidney-related transcriptional function.
    primary_references
    Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24204001/ · DOI 10.1681/ASN.2013040337
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 86–92

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human PCBD1 variant expression and promoter assays. · source_derived_draft · unverified_draft

    ## l-phenylalanine-pcbd-mutants Some mutations damage the protein and weaken its kidney-related transcriptional function. Five of seven tested PCBD1 mutations caused proteolytic instability and reduced FXYD2 promoter activity. Model: Human PCBD1 variant expression and promoter assays. Limitations: Variant effects are not uniform and do not establish dietary phenylalanine deficiency. Evidence access: Primary abstract Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24204001/ · DOI 10.1681/ASN.2013040337
    Complete structured claim and evidence

  3. PCBD1 has a pterin-carbinolamine dehydratase role in BH4 regeneration; biallelic defects are associated with transient neonatal hyperphenylalaninemia and primapterinuria.

    Human pterin-4-alpha-carbinolamine dehydratase / PCBD1 → Tetrahydrobiopterin / BH4 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human PCBD1 mutation study; established biochemical role and disease background.
    limitations
    The renal study does not directly measure whole-body BH4 recycling flux. The transcriptional role below is separately recorded.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    One cofactor-recycling protein has another important job in the kidney.
    primary_references
    Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24204001/ · DOI 10.1681/ASN.2013040337

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 62–68

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human PCBD1 mutation study; established biochemical role and disease background. · source_derived_draft · unverified_draft

    ## l-phenylalanine-pcbd-recycling-role One cofactor-recycling protein has another important job in the kidney. PCBD1 has a pterin-carbinolamine dehydratase role in BH4 regeneration; biallelic defects are associated with transient neonatal hyperphenylalaninemia and primapterinuria. Model: Human PCBD1 mutation study; established biochemical role and disease background. Limitations: The renal study does not directly measure whole-body BH4 recycling flux. The transcriptional role below is separately recorded. Evidence access: Primary abstract Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24204001/ · DOI 10.1681/ASN.2013040337
    Complete structured claim and evidence

  4. Overexpressed wild-type PCBD1 bound HNF1B and increased FXYD2 promoter activity in a human kidney cell line.

    Human pterin-4-alpha-carbinolamine dehydratase / PCBD1 → Human sodium/potassium ATPase regulatory subunit / FXYD2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human kidney-cell overexpression and promoter assay.
    limitations
    Promoter activity is not a direct measurement of magnesium flux or proof that phenylalanine intake regulates magnesium.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    A protein used in phenylalanine metabolism also helps control a kidney transport regulator.
    primary_references
    Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24204001/ · DOI 10.1681/ASN.2013040337

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 78–84

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human kidney-cell overexpression and promoter assay. · source_derived_draft · unverified_draft

    ## l-phenylalanine-pcbd-transcription A protein used in phenylalanine metabolism also helps control a kidney transport regulator. Overexpressed wild-type PCBD1 bound HNF1B and increased FXYD2 promoter activity in a human kidney cell line. Model: Human kidney-cell overexpression and promoter assay. Limitations: Promoter activity is not a direct measurement of magnesium flux or proof that phenylalanine intake regulates magnesium. Evidence access: Primary abstract Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting. · 2014 · https://pubmed.ncbi.nlm.nih.gov/24204001/ · DOI 10.1681/ASN.2013040337
    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.

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