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Article

The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family.

Journal of molecular biology - 8 Oct 2004

De Simone Giuseppina, Menchise Valeria, Alterio Vincenzo, Mandrich Luigi, Rossi Mosè, Manco Giuseppe, Pedone Carlo

Abstract excerpt

Esterase 2 (EST2) from the thermophilic eubacterium Alicyclobacillus acidocaldarius is a thermostable serine hydrolase belonging to the H group of the esterase/lipase family. This enzyme hydrolyzes monoacylesters of different acyl-chain length and various compounds with industrial interest. EST2 displays an optimal temperature at 70 degrees C and maximal activity with pNP-esters having acyl-chain bearing from six...

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Identifiers

PMID: 15381425
DOI: 10.1016/j.jmb.2004.08.014

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family.PMID 15381425Read ↗

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