Triple

T15478659
Position Surface form Disambiguated ID Type / Status
Subject kynurenine pathway E376854 entity
Predicate involvesEnzyme P91923 FINISHED
Object kynurenine aminotransferase III
Kynurenine aminotransferase III is an enzyme that catalyzes a transamination step in tryptophan degradation, contributing to the production of kynurenic acid and other metabolites in the kynurenine pathway.
 E1160707 NE FINISHED

How this triple was built (4 steps)

Every LLM step that produced this triple, in pipeline order — named-entity classification, the disambiguation choices (the exact options shown, with the pick highlighted), and the generated description. The batch + timestamp of each is in the Provenance table below.

NER Named-entity recognition gpt-5-mini
Instruction
Given a phrase, classify it is english named entity (e.g., persons, organizations, works of art) in Latin script, or not (e.g., literals, dates, URLs, verbose phrases). For disambiguation, the statement where the phrase occurs as object is also given. Please return a JSON object with `phrase` (string, the phrase being analyzed) and `is_ne` (boolean, indicating whether the phrase is a Named Entity).
Input
Phrase: kynurenine aminotransferase III | Statement: [kynurenine pathway, involvesEnzyme, kynurenine aminotransferase III]
NED1 Entity disambiguation (via context triple) gpt-5-mini-2025-08-07 
Target entity: kynurenine aminotransferase III
Context triple: [kynurenine pathway, involvesEnzyme, kynurenine aminotransferase III]
  • A. kynurenine aminotransferase II
    Kynurenine aminotransferase II is a pyridoxal phosphate-dependent enzyme that converts kynurenine to kynurenic acid, a neuroactive metabolite implicated in brain function and neurodegenerative disorders.
  • B. kynureninase
    Kynureninase is a pyridoxal phosphate-dependent enzyme that catalyzes key steps in tryptophan degradation within the kynurenine pathway, contributing to the production of NAD⁺ and other metabolites.
  • C. kynurenine pathway
    The kynurenine pathway is the primary metabolic route for tryptophan degradation, producing several bioactive metabolites involved in immune regulation, neurobiology, and redox balance.
  • D. tryptophan 2,3-dioxygenase
    Tryptophan 2,3-dioxygenase is a heme-containing enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of tryptophan, playing a key role in tryptophan metabolism and regulation.
  • E. indoleamine 2,3-dioxygenase 2
    Indoleamine 2,3-dioxygenase 2 is an immune-regulatory heme-containing enzyme that catalyzes the oxidative degradation of tryptophan along the kynurenine pathway, influencing inflammation and immune tolerance.
  • F. None of above. chosen
  • G. Unsure - the case is ambiguous/there is not enough information to decide.
NEDg Description generation gpt-5.1
Instruction
Generate a one-sentence description of the target entity. 
You are given a context triple in the form (subject, predicate, object), where the object is the target entity. 
# Instructions
Use the triple to infer relevant information about the entity. Describe the entity based on what is most defining, well-known. 
Avoid repeating the information from the triple, unless really essential.
# Response Format
Return only the sentence: "Description: [one-sentence description of the target entity]"
Input
Entity: kynurenine aminotransferase III
Triple: [kynurenine pathway, involvesEnzyme, kynurenine aminotransferase III]
Generated description
Kynurenine aminotransferase III is an enzyme that catalyzes a transamination step in tryptophan degradation, contributing to the production of kynurenic acid and other metabolites in the kynurenine pathway.
NED2 Entity disambiguation (via description) gpt-5-mini-2025-08-07 
Target entity: kynurenine aminotransferase III
Target entity description: Kynurenine aminotransferase III is an enzyme that catalyzes a transamination step in tryptophan degradation, contributing to the production of kynurenic acid and other metabolites in the kynurenine pathway.
  • A. kynurenine aminotransferase II
    Kynurenine aminotransferase II is a pyridoxal phosphate-dependent enzyme that converts kynurenine to kynurenic acid, a neuroactive metabolite implicated in brain function and neurodegenerative disorders.
  • B. kynureninase
    Kynureninase is a pyridoxal phosphate-dependent enzyme that catalyzes key steps in tryptophan degradation within the kynurenine pathway, contributing to the production of NAD⁺ and other metabolites.
  • C. kynurenine pathway
    The kynurenine pathway is the primary metabolic route for tryptophan degradation, producing several bioactive metabolites involved in immune regulation, neurobiology, and redox balance.
  • D. tryptophan 2,3-dioxygenase
    Tryptophan 2,3-dioxygenase is a heme-containing enzyme that catalyzes the first and rate-limiting step in the oxidative degradation of tryptophan, playing a key role in tryptophan metabolism and regulation.
  • E. indoleamine 2,3-dioxygenase 2
    Indoleamine 2,3-dioxygenase 2 is an immune-regulatory heme-containing enzyme that catalyzes the oxidative degradation of tryptophan along the kynurenine pathway, influencing inflammation and immune tolerance.
  • F. None of above. chosen

Provenance (5 batches)

The batch behind each pipeline step, in order, with when it ran. Timestamps are batch-level — stages were processed in waves, so the object chain (NER → NED1 → NEDg → NED2) reads in order, but predicate / elicitation batches can sit in a different wave.

Step Stage Batch ID Status When
creating Elicitation batch_69d85cd21dcc81908646251b1c26ea00 completed April 10, 2026, 2:13 a.m.
NER Named-entity recognition batch_69e03f8a77a081909f12f13660452f4a completed April 16, 2026, 1:46 a.m.
NED1 Entity disambiguation (via context triple) batch_69ff36595bfc8190a0d60b3cb875ccc5 completed May 9, 2026, 1:27 p.m.
NEDg Description generation batch_69ff376dac388190ab3b7e3553d2de29 completed May 9, 2026, 1:32 p.m.
NED2 Entity disambiguation (via description) batch_69ff382f1bbc8190810d0d825430f9ea completed May 9, 2026, 1:35 p.m.
Created at: April 10, 2026, 3:34 a.m.