Pyruvate dehydrogenase E1 subunit beta

mammalian protein found in Homo sapiens
Protein protein Q21118903
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Pyruvate dehydrogenase E1 subunit beta

Summary

Pyruvate dehydrogenase E1 subunit beta is a protein[1]. It is known by 8 alternative names across languages and contexts.[2]

Key Facts

  • Pyruvate dehydrogenase E1 subunit beta's instance of is recorded as protein[3].
  • Pyruvate dehydrogenase E1 subunit beta is part of Thiamin diphosphate-binding fold[4].
  • Pyruvate dehydrogenase E1 subunit beta is part of Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II[5].
  • Pyruvate dehydrogenase E1 subunit beta is part of Transketolase-like, pyrimidine-binding domain, protein family[6].
  • Pyruvate dehydrogenase E1 subunit beta is part of Transketolase, C-terminal domain, protein family[7].
  • Pyruvate dehydrogenase E1 subunit beta comprises Transketolase, C-terminal domain[8].
  • Pyruvate dehydrogenase E1 subunit beta comprises Transketolase-like, pyrimidine-binding domain[9].
  • Pyruvate dehydrogenase E1 subunit beta's molecular function is recorded as pyruvate dehydrogenase activity[10].
  • Pyruvate dehydrogenase E1 subunit beta's molecular function is recorded as protein binding[11].
  • Pyruvate dehydrogenase E1 subunit beta's molecular function is recorded as catalytic activity[12].
  • Pyruvate dehydrogenase E1 subunit beta's molecular function is recorded as oxidoreductase activity[13].
  • Pyruvate dehydrogenase E1 subunit beta's molecular function is recorded as pyruvate dehydrogenase (acetyl-transferring) activity[14].
  • Pyruvate dehydrogenase E1 subunit beta's molecular function is recorded as pyruvate dehydrogenase (NAD+) activity[15].
  • Pyruvate dehydrogenase E1 subunit beta's cell component is recorded as pyruvate dehydrogenase complex[16].
  • Pyruvate dehydrogenase E1 subunit beta's cell component is recorded as nucleoplasm[17].
  • Pyruvate dehydrogenase E1 subunit beta's cell component is recorded as mitochondrial matrix[18].
  • Pyruvate dehydrogenase E1 subunit beta's cell component is recorded as mitochondrion[19].
  • Pyruvate dehydrogenase E1 subunit beta's cell component is recorded as extracellular exosome[20].
  • Pyruvate dehydrogenase E1 subunit beta's cell component is recorded as nucleus[21].
  • Pyruvate dehydrogenase E1 subunit beta's cell component is recorded as nucleus[22].
  • Pyruvate dehydrogenase E1 subunit beta's biological process is recorded as mitochondrial acetyl-CoA biosynthetic process from pyruvate[23].
  • Pyruvate dehydrogenase E1 subunit beta's biological process is recorded as tricarboxylic acid cycle[24].
  • Pyruvate dehydrogenase E1 subunit beta's biological process is recorded as regulation of acetyl-CoA biosynthetic process from pyruvate[25].
  • Pyruvate dehydrogenase E1 subunit beta's biological process is recorded as pyruvate metabolic process[26].
  • Pyruvate dehydrogenase E1 subunit beta's biological process is recorded as glucose metabolic process[27].

Why It Matters

Pyruvate dehydrogenase E1 subunit beta is known by 8 alternative names across languages and contexts.[2]

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [3] . Q905695. Retrieved . wikidata.org.
  2. [4] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] . wikidata.org.
  5. [7] . wikidata.org.
  6. [8] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [10] . Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [11] . A Map of Human Mitochondrial Protein Interactions Linked to Neurodegeneration Reveals New Mechanisms of Redox Homeostasis and NF-κB Signaling. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] . Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] . Mutations of the E1beta subunit gene (PDHB) in four families with pyruvate dehydrogenase deficiency. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] . Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] . Proteomic analysis of podocyte exosome-enriched fraction from normal human urine. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] . Proteomic characterization of the human sperm nucleus. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] . Proteomic characterization of the human sperm nucleus. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] . Mutations of the E1beta subunit gene (PDHB) in four families with pyruvate dehydrogenase deficiency. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] . Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] . Wikidata aliases. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Pyruvate dehydrogenase E1 subunit beta. Retrieved May 3, 2026, from https://4ort.xyz/entity/pyruvate-dehydrogenase-e1-subunit-beta
MLA “Pyruvate dehydrogenase E1 subunit beta.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/pyruvate-dehydrogenase-e1-subunit-beta.
BibTeX @misc{4ortxyz_pyruvate-dehydrogenase-e1-subunit-beta_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Pyruvate dehydrogenase E1 subunit beta}}, year = {2026}, url = {https://4ort.xyz/entity/pyruvate-dehydrogenase-e1-subunit-beta}, note = {Accessed: 2026-05-03}}
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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 5w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from
    Encoded by PDHB
    Wikidata description mammalian protein found in Homo sapiens
    Molecular function pyruvate dehydrogenase activity, protein binding, catalytic activity +3
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 1.2.4.1, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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