Component
Human arginase 1 / ARG1
Human type I arginase; binuclear manganese enzyme of the cytosolic urea-cycle step.
3 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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
Human ARG1 structures show a binuclear manganese site binding a boronate transition-state analogue, supporting metal stabilization of the arginine-hydrolysis transition state.
Experimental context and source evidence
- experimental_model
- X-ray structures of human ARG1 with boronic-acid transition-state analogues
- exposure
- ABH and BEC inhibitor complexes
- limitations
- Transition-state analogue crystallography and author mechanistic inference; not direct nutritional manganese restriction.
- nutrient_topic
- Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
- organism
- Homo sapiens protein
- plain_language
- ARG1 holds two manganese ions at the site where arginine is hydrolyzed.
- primary_references
- [mn-enz-16141327] Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response. (2005). https://pubmed.ncbi.nlm.nih.gov/16141327/ DOI: 10.1073/pnas.0504027102
- tissue_or_cell_type
- Purified ARG1
Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 534–544
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray structures of human ARG1 with boronic-acid transition-state analogues · source_derived_draft · unverified_draft
### mn-enz-arg1-binuclear-transition-state Human ARG1 structures show a binuclear manganese site binding a boronate transition-state analogue, supporting metal stabilization of the arginine-hydrolysis transition state. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: ARG1 holds two manganese ions at the site where arginine is hydrolyzed. organism: Homo sapiens protein tissue_or_cell_type: Purified ARG1 experimental_model: X-ray structures of human ARG1 with boronic-acid transition-state analogues limitations: Transition-state analogue crystallography and author mechanistic inference; not direct nutritional manganese restriction. exposure: ABH and BEC inhibitor complexes [mn-enz-16141327] Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response. (2005). https://pubmed.ncbi.nlm.nih.gov/16141327/ DOI: 10.1073/pnas.0504027102
Complete structured claim and evidenceFor reconstituted human ARG1, turnover and catalytic efficiency ranked Mn(II) > Ni(II) ≈ Co(II) ≫ Zn(II).
Experimental context and source evidence
- cross_nutrient
- Zinc and cobalt substitutions were less effective than Mn; in-vitro substitution does not establish nutritional equivalence.
- experimental_model
- Metal-substitution crystallography and kinetics of purified human ARG1
- exposure
- Non-native metal reconstitution or added zinc
- limitations
- Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established.
- nutrient_topic
- Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
- organism
- Homo sapiens protein
- plain_language
- Manganese gave the most efficient ARG1 catalysis in this comparison.
- primary_references
- [mn-enz-23061982] Structure and function of non-native metal clusters in human arginase I. (2012). https://pubmed.ncbi.nlm.nih.gov/23061982/ DOI: 10.1021/bi301145n
- tissue_or_cell_type
- Purified enzyme
Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 546–557
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Metal-substitution crystallography and kinetics of purified human ARG1 · source_derived_draft · unverified_draft
### mn-enz-arg1-manganese-optimum For reconstituted human ARG1, turnover and catalytic efficiency ranked Mn(II) > Ni(II) ≈ Co(II) ≫ Zn(II). Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Manganese gave the most efficient ARG1 catalysis in this comparison. organism: Homo sapiens protein tissue_or_cell_type: Purified enzyme experimental_model: Metal-substitution crystallography and kinetics of purified human ARG1 limitations: Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established. exposure: Non-native metal reconstitution or added zinc cross_nutrient: Zinc and cobalt substitutions were less effective than Mn; in-vitro substitution does not establish nutritional equivalence. [mn-enz-23061982] Structure and function of non-native metal clusters in human arginase I. (2012). https://pubmed.ncbi.nlm.nih.gov/23061982/ DOI: 10.1021/bi301145n
Complete structured claim and evidenceAdded Zn(II) bound the H141/E277 region of manganese-loaded human ARG1, revealing a structural basis for zinc inhibition.
Experimental context and source evidence
- cross_nutrient
- Zn inhibition of a Mn enzyme was structurally measured in purified protein; no dietary threshold.
- experimental_model
- Metal-substitution crystallography and kinetics of purified human ARG1
- exposure
- Non-native metal reconstitution or added zinc
- limitations
- Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established.
- nutrient_topic
- Manganese research collection; topical membership is not evidence of a direct dietary effect. · Manganese
- organism
- Homo sapiens protein
- plain_language
- Zinc can inhibit purified manganese-loaded ARG1 at an additional site.
- primary_references
- [mn-enz-23061982] Structure and function of non-native metal clusters in human arginase I. (2012). https://pubmed.ncbi.nlm.nih.gov/23061982/ DOI: 10.1021/bi301145n
- tissue_or_cell_type
- Purified enzyme
Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 559–570
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Metal-substitution crystallography and kinetics of purified human ARG1 · source_derived_draft · unverified_draft
### mn-enz-arg1-zinc-inhibition Added Zn(II) bound the H141/E277 region of manganese-loaded human ARG1, revealing a structural basis for zinc inhibition. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: Zinc can inhibit purified manganese-loaded ARG1 at an additional site. organism: Homo sapiens protein tissue_or_cell_type: Purified enzyme experimental_model: Metal-substitution crystallography and kinetics of purified human ARG1 limitations: Primary experimental scope only; no human dietary threshold, clinical treatment rule, or universal metal substitution is established. exposure: Non-native metal reconstitution or added zinc cross_nutrient: Zn inhibition of a Mn enzyme was structurally measured in purified protein; no dietary threshold. [mn-enz-23061982] Structure and function of non-native metal clusters in human arginase I. (2012). https://pubmed.ncbi.nlm.nih.gov/23061982/ DOI: 10.1021/bi301145n
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.