Component
Human serine racemase / SRR
Context-specific entity; species, compartment and exposure are stated on each claim.
2 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 it acts on
Human serine racemase catalyzes the PLP-dependent formation of D-serine from L-serine; replacing Ser84 with alanine shifted its behavior toward serine dehydratase activity.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Recombinant human serine racemase and serine dehydratase mutants with functional comparisons.
- limitations
- Engineered reaction switching does not mean the native enzymes have identical functions.
- nutrient_topic
- L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
- plain_language
- One enzyme creates the D-form used in a distinct signaling pathway.
- primary_references
- Modulating the function of human serine racemase and human serine dehydratase by protein engineering. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23112234/ · DOI 10.1093/protein/gzs078
L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 406–412
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human serine racemase and serine dehydratase mutants with functional comparisons. · source_derived_draft · unverified_draft
## l-serine-srr-racemization One enzyme creates the D-form used in a distinct signaling pathway. Human serine racemase catalyzes the PLP-dependent formation of D-serine from L-serine; replacing Ser84 with alanine shifted its behavior toward serine dehydratase activity. Model: Recombinant human serine racemase and serine dehydratase mutants with functional comparisons. Limitations: Engineered reaction switching does not mean the native enzymes have identical functions. Evidence access: Primary abstract Modulating the function of human serine racemase and human serine dehydratase by protein engineering. · 2012 · https://pubmed.ncbi.nlm.nih.gov/23112234/ · DOI 10.1093/protein/gzs078
Complete structured claim and evidence
What acts on it
The 1.89-angstrom human serine-racemase holoenzyme structure included its bound pyridoxal-phosphate cofactor.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified human SRR crystal structure.
- limitations
- Structural cofactor binding does not establish dietary B6 control of human D-aspartate or an effective supplementation threshold.
- nutrient_topic
- D-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · D-Aspartate
- plain_language
- Vitamin B6-derived PLP is part of the shared racemase machinery.
- primary_references
- Conformational flexibility within the small domain of human serine racemase. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32039887/ · DOI 10.1107/S2053230X20001193
D-Aspartate: synthesis, clearance, neural and endocrine mechanisms (2026-09-19) · lines 56–62
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human SRR crystal structure. · source_derived_draft · unverified_draft
## d-aspartate-srr-plp Vitamin B6-derived PLP is part of the shared racemase machinery. The 1.89-angstrom human serine-racemase holoenzyme structure included its bound pyridoxal-phosphate cofactor. Model: Purified human SRR crystal structure. Limitations: Structural cofactor binding does not establish dietary B6 control of human D-aspartate or an effective supplementation threshold. Evidence access: Primary abstract Conformational flexibility within the small domain of human serine racemase. · 2020 · https://pubmed.ncbi.nlm.nih.gov/32039887/ · DOI 10.1107/S2053230X20001193
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.