CACrown ArchivesThe cinema collection
Menu
Research dossier · General Reference

Alanine—glyoxylate transaminase

class of enzymes

Cross-disciplinary reference desk with index cards, atlas, dictionary and catalogue
General referenceInterpretive dossier study · Crown Archives visual atlas
Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionJun 22, 2026
Entity authorityQ4708246 ↗
Source-derived summary

Alanine-glyoxylate transaminase (EC 2.6.1.44) is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction

The two substrates of this enzyme characterised from liver and kidney are L-alanine and glyoxylic acid. Its products are pyruvic acid and glycine.

This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:glyoxylate aminotransferase. Other names in common use include AGT, alanine-glyoxylate aminotransferase, alanine-glyoxylic aminotransferase, and L-alanine-glycine transaminase.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1H0C​, PDB: 1J04​, PDB: 1VJO​, PDB: 2BKW​, PDB: 2HUF​, PDB: 2HUI​, and PDB: 2HUU​.

Editorial summary

The public source identifies “Alanine—glyoxylate transaminase” as class of enzymes. This brief keeps that definition visible, then builds a research path around Alanine, glyoxylate and transaminase.

Editorial reviewA practical starting point whose main value is the path it opens into stronger specialist and primary sources. The current lead gives the account dated anchors—2007—that can be checked directly. The selected authority fields contribute no independent date. Its value is orientation rather than verdict, with Alanine, glyoxylate and transaminase providing the first useful test.
Editorial analysis

Why this record matters

A short description can identify a subject without explaining its stakes. For “Alanine—glyoxylate transaminase”, the useful work is to connect “class of enzymes” to the records capable of establishing context and consequence.

Evidence profile

Named sources, stable identifiers and responsible institutions provide the strongest route from overview to verifiable evidence. The source revision retrieved here is dated Jun 22, 2026. The linked authority identifier is Q4708246. None of the 0 selected statements returned an explicit reference. The first chronological checks are 2007.

Critical limits

The absence of detail may reflect summary conventions rather than a lack of surviving documentation. The lead is largely declarative, so disagreement and counter-evidence require a deliberate search beyond the opening account. Authority statements aid reconciliation but still require their own references, qualifiers and ranks to be checked.

How to read it

Use the entry as an orientation point, then follow its citations and revision history. Names, dates and institutional relationships should be checked against the original record.

Best used for
  • Subject orientation
  • Search vocabulary
  • Locating named sources
Verify next

The closest primary source, responsible institution and strongest cited specialist reference.

Three-step research path

  1. Establish the record: confirm the title “Alanine—glyoxylate transaminase”, its source revision and the description used here.
  2. Expand the search: follow Alanine—glyoxylate transaminase primary sources, Alanine—glyoxylate transaminase archive and Alanine research across catalogues and specialist indexes.
  3. Test the account: compare the strongest cited source with the responsible institution’s current record and note any disagreement.

Questions for further research

  1. Which source most directly establishes the central claim about “Alanine—glyoxylate transaminase”?
  2. What terminology or title could unlock a more precise catalogue search?
  3. Which institution is responsible for the underlying evidence?
Subject index

Search terms from this dossier

Source & attribution

This entry incorporates text from “Alanine—glyoxylate transaminase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.