Component

Ovine glutamine synthetase / GLUL

Sheep glutamine synthetase; kept separate from human GLUL.

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.

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. Ovine brain GLUL assays showed optimal Mg:ATP at 2:1 and Mn:ATP at 1:1, with different reported pH optima of 7.5 and 5.0, respectively.

    Experimental context and source evidence
    cross_nutrient
    Mn and Mg can support activity in vitro, with distinct metal:ATP ratios and pH conditions.
    experimental_model
    Ovine brain glutamine synthetase steady-state kinetics and metal-binding measurements
    exposure
    Mn(II) and Mg(II) titrations; binding and tissue metal measurements
    limitations
    Different assay optima are not evidence that Mn is the preferred cofactor at physiological brain pH.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Ovis aries
    plain_language
    Magnesium and manganese supported GLUL under different assay conditions.
    primary_references
    [mn-enz-6129892] Glutamine synthetase from ovine brain is a manganese(II) enzyme. (1982). https://pubmed.ncbi.nlm.nih.gov/6129892/ DOI: 10.1021/bi00268a011
    tissue_or_cell_type
    Brain-derived purified enzyme

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 620–631

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ovine brain glutamine synthetase steady-state kinetics and metal-binding measurements · source_derived_draft · unverified_draft

    ### mn-enz-ovine-glul-metal-kinetics Ovine brain GLUL assays showed optimal Mg:ATP at 2:1 and Mn:ATP at 1:1, with different reported pH optima of 7.5 and 5.0, respectively. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium and manganese supported GLUL under different assay conditions. organism: Ovis aries tissue_or_cell_type: Brain-derived purified enzyme experimental_model: Ovine brain glutamine synthetase steady-state kinetics and metal-binding measurements limitations: Different assay optima are not evidence that Mn is the preferred cofactor at physiological brain pH. exposure: Mn(II) and Mg(II) titrations; binding and tissue metal measurements cross_nutrient: Mn and Mg can support activity in vitro, with distinct metal:ATP ratios and pH conditions. [mn-enz-6129892] Glutamine synthetase from ovine brain is a manganese(II) enzyme. (1982). https://pubmed.ncbi.nlm.nih.gov/6129892/ DOI: 10.1021/bi00268a011
    Complete structured claim and evidence

What acts on it

  1. Cofactor-trapped GLUL from bovine or ovine brain contained 1.5±0.2 Mg per subunit and less than 0.05 Mn per subunit.

    Mg2+ → Ovine glutamine synthetase / GLUL source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Direct native-metal trapping distinguishes Mg occupancy from Mn-supported activity in vitro.
    experimental_model
    Cofactor trapping and immunoprecipitation of bovine and ovine brain glutamine synthetase
    exposure
    Methionine sulfoximine phosphate/ADP cofactor trapping
    limitations
    Extraction with methionine sulfoximine phosphate and ADP; bovine/ovine brain, not direct living human brain measurement.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Bos taurus; Ovis aries
    plain_language
    A cofactor-trapping study recovered mainly magnesium from brain GLUL.
    primary_references
    [mn-enz-2870682] Mg2+ is bound to glutamine synthetase extracted from bovine or ovine brain in the presence of L-methionine-S-sulfoximine phosphate. (1986). https://pubmed.ncbi.nlm.nih.gov/2870682/ DOI: 10.1016/0003-9861(86)90496-0
    tissue_or_cell_type
    Brain extracts and purified enzyme

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 646–657

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cofactor trapping and immunoprecipitation of bovine and ovine brain glutamine synthetase · source_derived_draft · unverified_draft

    ### mn-enz-brain-glul-cofactor-trapping Cofactor-trapped GLUL from bovine or ovine brain contained 1.5±0.2 Mg per subunit and less than 0.05 Mn per subunit. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: A cofactor-trapping study recovered mainly magnesium from brain GLUL. organism: Bos taurus; Ovis aries tissue_or_cell_type: Brain extracts and purified enzyme experimental_model: Cofactor trapping and immunoprecipitation of bovine and ovine brain glutamine synthetase limitations: Extraction with methionine sulfoximine phosphate and ADP; bovine/ovine brain, not direct living human brain measurement. exposure: Methionine sulfoximine phosphate/ADP cofactor trapping cross_nutrient: Direct native-metal trapping distinguishes Mg occupancy from Mn-supported activity in vitro. [mn-enz-2870682] Mg2+ is bound to glutamine synthetase extracted from bovine or ovine brain in the presence of L-methionine-S-sulfoximine phosphate. (1986). https://pubmed.ncbi.nlm.nih.gov/2870682/ DOI: 10.1016/0003-9861(86)90496-0
    Complete structured claim and evidence
  2. The 1986 cofactor-trapping study concluded that Mg, rather than Mn, appears to be bound to bovine/ovine brain GLUL in vivo, although either metal supports assays.

    Mg2+ → Ovine glutamine synthetase / GLUL source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Competing primary interpretation of native GLUL Mn versus Mg identity.
    experimental_model
    Cofactor trapping and immunoprecipitation of bovine and ovine brain glutamine synthetase
    exposure
    Methionine sulfoximine phosphate/ADP cofactor trapping
    limitations
    Author interpretation of extracted enzyme; overlaps the ovine brain question in 1982, with different methods.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Bos taurus; Ovis aries
    plain_language
    Another primary study supported magnesium as the native brain GLUL metal.
    primary_references
    [mn-enz-2870682] Mg2+ is bound to glutamine synthetase extracted from bovine or ovine brain in the presence of L-methionine-S-sulfoximine phosphate. (1986). https://pubmed.ncbi.nlm.nih.gov/2870682/ DOI: 10.1016/0003-9861(86)90496-0
    tissue_or_cell_type
    Brain extracts and purified enzyme

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 659–670

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cofactor trapping and immunoprecipitation of bovine and ovine brain glutamine synthetase · source_derived_draft · unverified_draft

    ### mn-enz-brain-glul-native-mg-interpretation The 1986 cofactor-trapping study concluded that Mg, rather than Mn, appears to be bound to bovine/ovine brain GLUL in vivo, although either metal supports assays. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Another primary study supported magnesium as the native brain GLUL metal. organism: Bos taurus; Ovis aries tissue_or_cell_type: Brain extracts and purified enzyme experimental_model: Cofactor trapping and immunoprecipitation of bovine and ovine brain glutamine synthetase limitations: Author interpretation of extracted enzyme; overlaps the ovine brain question in 1982, with different methods. exposure: Methionine sulfoximine phosphate/ADP cofactor trapping cross_nutrient: Competing primary interpretation of native GLUL Mn versus Mg identity. [mn-enz-2870682] Mg2+ is bound to glutamine synthetase extracted from bovine or ovine brain in the presence of L-methionine-S-sulfoximine phosphate. (1986). https://pubmed.ncbi.nlm.nih.gov/2870682/ DOI: 10.1016/0003-9861(86)90496-0
    Complete structured claim and evidence
  3. From ovine-brain GLUL binding and tissue-metal measurements, the 1982 authors proposed that the enzyme may be manganese-bound in vivo.

    Mn2+ → Ovine glutamine synthetase / GLUL source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Published inference about Mn versus Mg native occupancy; paired with the competing 1986 cofactor-trapping interpretation.
    experimental_model
    Ovine brain glutamine synthetase steady-state kinetics and metal-binding measurements
    exposure
    Mn(II) and Mg(II) titrations; binding and tissue metal measurements
    limitations
    Author inference; not a universal human GLUL cofactor assignment. Contradicted by a later overlapping ovine/bovine study using endogenous-cofactor trapping.
    nutrient_topic
    Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
    organism
    Ovis aries
    plain_language
    One primary study proposed manganese as the native sheep-brain GLUL metal.
    primary_references
    [mn-enz-6129892] Glutamine synthetase from ovine brain is a manganese(II) enzyme. (1982). https://pubmed.ncbi.nlm.nih.gov/6129892/ DOI: 10.1021/bi00268a011
    tissue_or_cell_type
    Brain-derived purified enzyme

    Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 633–644

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ovine brain glutamine synthetase steady-state kinetics and metal-binding measurements · source_derived_draft · unverified_draft

    ### mn-enz-ovine-glul-native-mn-interpretation From ovine-brain GLUL binding and tissue-metal measurements, the 1982 authors proposed that the enzyme may be manganese-bound in vivo. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: One primary study proposed manganese as the native sheep-brain GLUL metal. organism: Ovis aries tissue_or_cell_type: Brain-derived purified enzyme experimental_model: Ovine brain glutamine synthetase steady-state kinetics and metal-binding measurements limitations: Author inference; not a universal human GLUL cofactor assignment. Contradicted by a later overlapping ovine/bovine study using endogenous-cofactor trapping. exposure: Mn(II) and Mg(II) titrations; binding and tissue metal measurements cross_nutrient: Published inference about Mn versus Mg native occupancy; paired with the competing 1986 cofactor-trapping interpretation. [mn-enz-6129892] Glutamine synthetase from ovine brain is a manganese(II) enzyme. (1982). https://pubmed.ncbi.nlm.nih.gov/6129892/ DOI: 10.1021/bi00268a011
    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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