Component

Cofactor-bound holo-GAD65

Cofactor-bound holo-GAD65. Species, exposure and limitations are retained in each linked claim.

1 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

Where it participates (unsigned role)

  1. At least 50% of glutamate decarboxylase is present in brain as apoenzyme, that is enzyme without bound cofactor, which serves as a reservoir of inactive enzyme that can be drawn on when additional GABA synthesis is needed, a substantial majority of the apoenzyme in brain is accounted for by GAD65 although GAD67 also contributes, the interaction of the enzyme with pyridoxal 5-phosphate is a major factor in the short-term regulation of its activity, and the apparent localization of GAD65 in nerve terminals together with the large reserve of apo-GAD65 suggest that GAD65 is specialized to respond to short-term changes in demand for transmitter GABA.

    Apo-glutamate decarboxylase, the form without bound cofactor → Synthesis of GABA from glutamate source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/gaba-research/8419527.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0de2df4de7da887745f27b7c4593a75590b6de3649a2b5b35a1d36980a86b755", "start_char": 0, "end_char": 1425, "text_sha256": "0de2df4de7da887745f27b7c4593a75590b6de3649a2b5b35a1d36980a86b755"}
    experimental_model
    Review of the compartments and short-term regulation of brain GABA synthesis
    exposure
    Glutamate decarboxylase measured as apoenzyme and holoenzyme across brain regions
    limitations
    A review of the enzymology. The apoenzyme fraction is given for total glutamate decarboxylase, with GAD65 accounting for a substantial majority of it rather than being separately quantified.
    nutrient_topic
    GABA research collection; topical membership is not evidence of a direct clinical effect, and the sign of a GABA response depends on the chloride gradient of the cell it was measured in. · Gamma-aminobutyric acid
    organism
    Rat and human
    plain_language
    Half the enzyme is sitting idle without its cofactor, held in reserve for when more transmitter is suddenly needed.
    primary_references
    [gb-p8419527] Regulation of gamma-aminobutyric acid synthesis in the brain. (1993). https://pubmed.ncbi.nlm.nih.gov/8419527/ DOI: 10.1111/j.1471-4159.1993.tb03165.x
    tissue_or_cell_type
    Brain

    GABA: a ligand with no sign of its own, the cofactor that limits its synthesis, the barrier that keeps it out of the brain, and the immune settings where the same molecule protects and harms (2026-09-22) · lines 105–116

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Review of the compartments and short-term regulation of brain GABA synthesis · source_derived_draft · unverified_draft

    ### gb-half-the-enzyme-waits At least 50% of glutamate decarboxylase is present in brain as apoenzyme, that is enzyme without bound cofactor, which serves as a reservoir of inactive enzyme that can be drawn on when additional GABA synthesis is needed, a substantial majority of the apoenzyme in brain is accounted for by GAD65 although GAD67 also contributes, the interaction of the enzyme with pyridoxal 5-phosphate is a major factor in the short-term regulation of its activity, and the apparent localization of GAD65 in nerve terminals together with the large reserve of apo-GAD65 suggest that GAD65 is specialized to respond to short-term changes in demand for transmitter GABA. Condition category: normal nutrient_topic: GABA research collection; topical membership is not evidence of a direct clinical effect, and the sign of a GABA response depends on the chloride gradient of the cell it was measured in. plain_language: Half the enzyme is sitting idle without its cofactor, held in reserve for when more transmitter is suddenly needed. organism: Rat and human tissue_or_cell_type: Brain experimental_model: Review of the compartments and short-term regulation of brain GABA synthesis limitations: A review of the enzymology. The apoenzyme fraction is given for total glutamate decarboxylase, with GAD65 accounting for a substantial majority of it rather than being separately quantified. exposure: Glutamate decarboxylase measured as apoenzyme and holoenzyme across brain regions evidence_span: {"source_cache": "artifacts/gaba-research/8419527.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0de2df4de7da887745f27b7c4593a75590b6de3649a2b5b35a1d36980a86b755", "start_char": 0, "end_char": 1425, "text_sha256": "0de2df4de7da887745f27b7c4593a75590b6de3649a2b5b35a1d36980a86b755"} [gb-p8419527] Regulation of gamma-aminobutyric acid synthesis in the brain. (1993). https://pubmed.ncbi.nlm.nih.gov/8419527/ DOI: 10.1111/j.1471-4159.1993.tb03165.x
    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