<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(1)</volume><submitter>Cavazzini D</submitter><pubmed_abstract>An increasing number of esterases is being revealed by (meta) genomic sequencing projects, but few of them are functionally/structurally characterized, especially enzymes of fungal origin. Starting from a three-member gene family of secreted putative "lipases/esterases" preferentially expressed in the symbiotic phase of the mycorrhizal fungus Tuber melanosporum ("black truffle"), we show here that these enzymes (TmelEST1-3) are dimeric, heat-resistant carboxylesterases capable of hydrolyzing various short/medium chain p-nitrophenyl esters. TmelEST2 was the most active (kcat = 2302 s&lt;sup>-1&lt;/sup> for p-nitrophenyl-butyrate) and thermally stable (T&lt;sub>50&lt;/sub> = 68.3 °C), while TmelEST3 was the only one displaying some activity on tertiary alcohol esters. X-ray diffraction analysis of TmelE</pubmed_abstract><journal>Scientific reports</journal><pagination>7628</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5550427</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum.</pubmed_title><pmcid>PMC5550427</pmcid><pubmed_authors>Cavazzini D</pubmed_authors><pubmed_authors>Ottonello S</pubmed_authors><pubmed_authors>Grossi G</pubmed_authors><pubmed_authors>Vallese F</pubmed_authors><pubmed_authors>Bolchi A</pubmed_authors><pubmed_authors>Levati E</pubmed_authors><pubmed_authors>Zanotti G</pubmed_authors><pubmed_authors>Montanini B</pubmed_authors></additional><is_claimable>false</is_claimable><name>A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum.</name><description>An increasing number of esterases is being revealed by (meta) genomic sequencing projects, but few of them are functionally/structurally characterized, especially enzymes of fungal origin. Starting from a three-member gene family of secreted putative "lipases/esterases" preferentially expressed in the symbiotic phase of the mycorrhizal fungus Tuber melanosporum ("black truffle"), we show here that these enzymes (TmelEST1-3) are dimeric, heat-resistant carboxylesterases capable of hydrolyzing various short/medium chain p-nitrophenyl esters. TmelEST2 was the most active (kcat = 2302 s&lt;sup>-1&lt;/sup> for p-nitrophenyl-butyrate) and thermally stable (T&lt;sub>50&lt;/sub> = 68.3 °C), while TmelEST3 was the only one displaying some activity on tertiary alcohol esters. X-ray diffraction analysis of TmelE</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Aug</publication><modification>2026-04-15T23:14:25.755Z</modification><creation>2019-03-26T23:53:01Z</creation></dates><accession>S-EPMC5550427</accession><cross_references><pubmed>28794466</pubmed><doi>10.1038/s41598-017-08007-9</doi></cross_references></HashMap>