Cystathionine beta-synthase

mammalian protein found in Homo sapiens
Protein protein Q5201183
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Cystathionine beta-synthase

Summary

Cystathionine beta-synthase is a protein[1]. It draws 87 Wikipedia views per month (protein category, ranking #129 of 987).[2]

Key Facts

  • Cystathionine beta-synthase's instance of is recorded as protein[3].
  • Cystathionine beta-synthase's physically interacts with is recorded as aminooxyacetic acid[4].
  • Cystathionine beta-synthase is part of Cystathionine beta-synthase[5].
  • Cystathionine beta-synthase is part of Tryptophan synthase beta subunit-like PLP-dependent enzyme[6].
  • Cystathionine beta-synthase is part of CBS domain, protein family[7].
  • Cystathionine beta-synthase is part of Pyridoxal-phosphate dependent enzyme family[8].
  • Cystathionine beta-synthase is part of Cysteine synthase/cystathionine beta-synthase, pyridoxal-phosphate attachment site, protein family[9].
  • Cystathionine beta-synthase's Commons category is recorded as Cystathionine beta-synthase[10].
  • Cystathionine beta-synthase comprises Pyridoxal-phosphate dependent enzyme[11].
  • Cystathionine beta-synthase comprises Cysteine synthase/cystathionine beta-synthase, pyridoxal-phosphate attachment site[12].
  • Cystathionine beta-synthase comprises CBS domain[13].
  • Cystathionine beta-synthase's molecular function is recorded as oxygen binding[14].
  • Cystathionine beta-synthase's molecular function is recorded as protein homodimerization activity[15].
  • Cystathionine beta-synthase's molecular function is recorded as cystathionine beta-synthase activity[16].
  • Cystathionine beta-synthase's molecular function is recorded as metal ion binding[17].
  • Cystathionine beta-synthase's molecular function is recorded as nitric oxide binding[18].
  • Cystathionine beta-synthase's molecular function is recorded as catalytic activity[19].
  • Cystathionine beta-synthase's molecular function is recorded as protein binding[20].
  • Cystathionine beta-synthase's molecular function is recorded as heme binding[21].
  • Cystathionine beta-synthase's molecular function is recorded as modified amino acid binding[22].
  • Cystathionine beta-synthase's molecular function is recorded as S-adenosyl-L-methionine binding[23].
  • Cystathionine beta-synthase's molecular function is recorded as lyase activity[24].
  • Cystathionine beta-synthase's molecular function is recorded as identical protein binding[25].
  • Cystathionine beta-synthase's molecular function is recorded as enzyme binding[26].
  • Cystathionine beta-synthase's molecular function is recorded as pyridoxal phosphate binding[27].

Why It Matters

Cystathionine beta-synthase draws 87 Wikipedia views per month (protein category, ranking #129 of 987).[2] It has Wikipedia articles in 5 language editions, a strong signal of global cultural recognition.[28] It is known by 11 alternative names across languages and contexts.[29]

References

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

Direct Wikidata claims

  1. [3] . Q905695. Retrieved . wikidata.org.
  2. [4] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  3. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [7] . wikidata.org.
  6. [8] . wikidata.org.
  7. [9] . wikidata.org.
  8. [10] . wikidata.org.
  9. [11] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [12] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [13] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [14] . NO* binds human cystathionine β-synthase quickly and tightly. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] . Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] . NO* binds human cystathionine β-synthase quickly and tightly. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] . Human cystathionine beta-synthase is a target for sumoylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] . Modulation of cystathionine beta-synthase activity by the Arg-51 and Arg-224 mutations. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] . Novel associations of CPS1, MUT, NOX4, and DPEP1 with plasma homocysteine in a healthy population: a genome-wide evaluation of 13 974 participants in the Women's Genome Health Study. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] . Human cystathionine β-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] . A proteome-scale map of the human interactome network. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] . Human cystathionine beta-synthase is a target for sumoylation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] . Modulation of cystathionine beta-synthase activity by the Arg-51 and Arg-224 mutations. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

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

Aggregate / graph-position facts

  1. [2] . Wikimedia Foundation. dumps.wikimedia.org.
  2. [28] . Wikidata sitelinks. wikidata.org.
  3. [29] . Wikidata aliases. wikidata.org.

📑 Cite this page

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). Cystathionine beta-synthase. Retrieved May 3, 2026, from https://4ort.xyz/entity/cystathionine-beta-synthase
MLA “Cystathionine beta-synthase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/cystathionine-beta-synthase.
BibTeX @misc{4ortxyz_cystathionine-beta-synthase_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Cystathionine beta-synthase}}, year = {2026}, url = {https://4ort.xyz/entity/cystathionine-beta-synthase}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Cystathionine beta-synthase — https://4ort.xyz/entity/cystathionine-beta-synthase (retrieved 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. 6d ago · Boghog · 2026-07-23 view diff on Wikidata ↗
    Instance of
    Part of
    Encoded by CBS
    Biological process transsulfuration, cysteine biosynthetic process via cystathionine, L-serine metabolic process +14
    + 10 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 4.2.1.22, [[:toollabs:quickstatements/#/batch/261457|batch #261457]]"
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