{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(1)"],"submitter":["Cavazzini D"],"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<sup>-1</sup> for p-nitrophenyl-butyrate) and thermally stable (T<sub>50</sub> = 68.3 °C), while TmelEST3 was the only one displaying some activity on tertiary alcohol esters. X-ray diffraction analysis of TmelE"],"journal":["Scientific reports"],"pagination":["7628"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5550427"],"repository":["biostudies-literature"],"pubmed_title":["A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum."],"pmcid":["PMC5550427"],"pubmed_authors":["Cavazzini D","Ottonello S","Grossi G","Vallese F","Bolchi A","Levati E","Zanotti G","Montanini B"],"additional_accession":[]},"is_claimable":false,"name":"A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum.","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<sup>-1</sup> for p-nitrophenyl-butyrate) and thermally stable (T<sub>50</sub> = 68.3 °C), while TmelEST3 was the only one displaying some activity on tertiary alcohol esters. X-ray diffraction analysis of TmelE","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Aug","modification":"2026-04-15T23:14:25.755Z","creation":"2019-03-26T23:53:01Z"},"accession":"S-EPMC5550427","cross_references":{"pubmed":["28794466"],"doi":["10.1038/s41598-017-08007-9"]}}