{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Liaw RB"],"funding":["Council of Agriculture, Executive Yuan, Taiwan","Livestock Research Institute, Council of Agriculture, Executive Yuan"],"pagination":["2403"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9786865"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(12)"],"pubmed_abstract":["A new esterase gene, <i>est6</i>, was discovered in an activated sludge metagenomic library. The 729-bp gene encodes a 242-amino acid protein (designated Est6) with a molecular mass of 26.1 kDa. Est6 shared only a moderate identity to a putative hydrolase with the highest BLASTP analysis score. Most of the closely related proteins are uncharacterized and are predicted from genome sequencing data of microorganisms or metagenomic DNA sequences. The phylogenetic analysis of Est6 showed that the protein was assigned to family VI esterases/lipases. The catalytic triad of Est6 was predicted to be Ser135, Asp188, and His219, with Ser135 in a typically conserved pentapeptide (GFSQG) of family VI members, which was further confirmed by site-directed mutagenesis. The <i>est6</i> gene was overexpress"],"journal":["Microorganisms"],"pubmed_title":["Molecular Cloning and Characterization of a New Family VI Esterase from an Activated Sludge Metagenome."],"pmcid":["PMC9786865"],"funding_grant_id":["111AS-2.1.1-LI-L7","99AS-8.1.3-LI-L1, 111AS-2.1.1-LI-L7","99AS-8.1.3-LI-L1"],"pubmed_authors":["Chen JC","Cheng MP","Liaw RB"],"additional_accession":[]},"is_claimable":false,"name":"Molecular Cloning and Characterization of a New Family VI Esterase from an Activated Sludge Metagenome.","description":"A new esterase gene, <i>est6</i>, was discovered in an activated sludge metagenomic library. The 729-bp gene encodes a 242-amino acid protein (designated Est6) with a molecular mass of 26.1 kDa. Est6 shared only a moderate identity to a putative hydrolase with the highest BLASTP analysis score. Most of the closely related proteins are uncharacterized and are predicted from genome sequencing data of microorganisms or metagenomic DNA sequences. The phylogenetic analysis of Est6 showed that the protein was assigned to family VI esterases/lipases. The catalytic triad of Est6 was predicted to be Ser135, Asp188, and His219, with Ser135 in a typically conserved pentapeptide (GFSQG) of family VI members, which was further confirmed by site-directed mutagenesis. The <i>est6</i> gene was overexpress","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-08T03:15:04.624Z","creation":"2025-02-19T03:00:51.462Z"},"accession":"S-EPMC9786865","cross_references":{"pubmed":["36557656"],"doi":["10.3390/microorganisms10122403"]}}