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2-hydroxypropyl-CoM lyase

class of enzymes

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General referenceInterpretive dossier study · Crown Archives visual atlas
Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionAug 26, 2023
Entity authorityQ13408777 ↗
Source-derived summary

The enzyme 2-hydroxypropyl-CoM lyase (EC 4.4.1.23, epoxyalkane:coenzyme M transferase, epoxyalkane:CoM transferase, epoxyalkane:2-mercaptoethanesulfonate transferase, coenzyme M-epoxyalkane ligase, epoxyalkyl:CoM transferase, epoxypropane:coenzyme M transferase, epoxypropyl:CoM transferase, EaCoMT, 2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming), (R)-2-hydroxypropyl-CoM 2-mercaptoethanesulfonate lyase (cyclizing, (R)-1,2-epoxypropane-forming)) is an enzyme with systematic name (R)-[or (S)]-2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming). This enzyme catalyses the following reaction:

(1) (R)-2-hydroxypropyl-CoM

⇌

{\displaystyle \rightleftharpoons }

(R)-1,2-epoxypropane + HS-CoM

(2) (S)-2-hydroxypropyl-CoM

⇌

{\displaystyle \rightleftharpoons }

(S)-1,2-epoxypropane + HS-CoM

This enzyme requires zinc.

Editorial summary

“2-hydroxypropyl-CoM lyase” enters the record as class of enzymes. Crown Archives preserves that source wording while asking what 2-hydroxypropyl-CoM, lyase and class can confirm, complicate or overturn.

Editorial reviewA practical starting point whose main value is the path it opens into stronger specialist and primary sources. The current 70-word lead offers orientation but no explicit four-digit date, so chronology should not be assumed. The selected authority fields contribute no independent date. Its strongest next move is a source search built around 2-hydroxypropyl-CoM, lyase and class.
Editorial analysis

Why this record matters

“2-hydroxypropyl-CoM lyase” is worth following because a concise public description often conceals a longer documentary argument. Here, 2-hydroxypropyl-CoM, lyase and class provides the most credible route into that argument.

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 Aug 26, 2023. The linked authority identifier is Q13408777.

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 “2-hydroxypropyl-CoM lyase”, its source revision and the description used here.
  2. Expand the search: follow 2-hydroxypropyl-CoM lyase primary sources, 2-hydroxypropyl-CoM lyase archive and 2-hydroxypropyl-CoM 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 “2-hydroxypropyl-CoM lyase”?
  2. Which cited source is closest to the event, object or claim?
  3. Which institution is responsible for the underlying evidence?
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Source & attribution

This entry incorporates text from “2-hydroxypropyl-CoM lyase” 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.