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Xylono-1,4-lactonase

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 10, 2026
Entity authorityQ8045467 ↗
Source-derived summary

The enzyme xylono-1,4-lactonase (EC 3.1.1.68) catalyzes the reaction

The enzyme characterised from Pseudomonas fragi and Gluconobacter oxydans hydrolyses D-xylono-1,4-lactone to D-xylonic acid. The enzyme is of interest as a target for metabolic engineering.

This enzyme is a hydrolase, specifically one acting on carboxylic ester bonds. The systematic name of this enzyme class is D-xylono-1,4-lactone lactonohydrolase. Other names in common use include xylono-γ-lactonase, and xylonolactonase.

Editorial summary

“Xylono-1,4-lactonase” enters the record as class of enzymes. Crown Archives preserves that source wording while asking what Xylono-1, 4-lactonase and class can confirm, complicate or overturn.

Editorial reviewA dependable orientation record for establishing vocabulary, names and a first evidence trail. The current 64-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 Xylono-1, 4-lactonase and class.
Editorial analysis

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“Xylono-1,4-lactonase” is worth following because a concise public description often conceals a longer documentary argument. Here, Xylono-1, 4-lactonase 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 10, 2026. The linked authority identifier is Q8045467. None of the 0 selected statements returned an explicit reference.

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Source & attribution

This entry incorporates text from “Xylono-1,4-lactonase” 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.