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Aculeacin-A deacylase

class of enzymes

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Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionAug 19, 2025
Entity authorityQ4677876
Source-derived summary

In enzymology, an aculeacin-A deacylase (EC 3.5.1.70) is an enzyme that catalyzes the chemical reaction that cleaves the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side chain.

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is aculeacin-A amidohydrolase. This enzyme is also called aculeacin A acylase.

References

Takeshima H, Inokoshi J, Takada Y, Tanaka H, Omura S (April 1989). "A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization". The Journal of Biochemistry. 105 (4). Tokyo: 606–610. doi:10.1093/oxfordjournals.jbchem.a122712.

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“Aculeacin-A deacylase” enters the record as class of enzymes. Crown Archives preserves that source wording while asking what Aculeacin-A, deacylase 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 lead gives the account dated anchors—1989, 1093—that can be checked directly. The selected authority fields contribute no independent date. Its strongest next move is a source search built around Aculeacin-A, deacylase and class.
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This entry incorporates text from Aculeacin-A deacylase” 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.