{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dobrijevic D"],"funding":["Biotechnology and Biological Sciences Research Council","Engineering and Physical Sciences Research Council"],"pagination":["36608-36614"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9075147"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(63)"],"pubmed_abstract":["Ene-reductases (ERs) of the Old Yellow Enzyme family catalyse asymmetric reduction of activated alkenes providing chiral products. They have become an important method in the synthetic chemists' toolbox offering a sustainable alternative to metal-catalysed asymmetric reduction. Development of new biocatalytic alkene reduction routes, however needs easy access to novel biocatalysts. A sequence-based functional metagenomic approach was used to identify novel ERs from a drain metagenome. From the ten putative ER enzymes initially identified, eight exhibited activities towards widely accepted mono-cyclic substrates with several of the ERs giving high reaction yields and stereoselectivities. Two highly performing enzymes that displayed excellent co-solvent tolerance were used for the stereoselective reduction of sterically challenging bicyclic enones where the reactions proceeded in high yields, which is unprecedented to date with wild-type ERs. On a preparative enzymatic scale, reductions of Hajos-Parish, Wieland-Miescher derivatives and a tricyclic ketone proceeded with good to excellent yields."],"journal":["RSC advances"],"pubmed_title":["Metagenomic ene-reductases for the bioreduction of sterically challenging enones."],"pmcid":["PMC9075147"],"funding_grant_id":["BB/N01877X/1","EP/K005030/1","EP/P020410/1","BB/L007444/1"],"pubmed_authors":["Dobrijevic D","Dawson N","Mendez-Sanchez D","Tappertzhofen N","Orengo CA","Benhamou L","Aliev AE","Moody TS","Baud D","Hailes HC","Ward JM"],"additional_accession":[]},"is_claimable":false,"name":"Metagenomic ene-reductases for the bioreduction of sterically challenging enones.","description":"Ene-reductases (ERs) of the Old Yellow Enzyme family catalyse asymmetric reduction of activated alkenes providing chiral products. They have become an important method in the synthetic chemists' toolbox offering a sustainable alternative to metal-catalysed asymmetric reduction. Development of new biocatalytic alkene reduction routes, however needs easy access to novel biocatalysts. A sequence-based functional metagenomic approach was used to identify novel ERs from a drain metagenome. From the ten putative ER enzymes initially identified, eight exhibited activities towards widely accepted mono-cyclic substrates with several of the ERs giving high reaction yields and stereoselectivities. Two highly performing enzymes that displayed excellent co-solvent tolerance were used for the stereoselective reduction of sterically challenging bicyclic enones where the reactions proceeded in high yields, which is unprecedented to date with wild-type ERs. On a preparative enzymatic scale, reductions of Hajos-Parish, Wieland-Miescher derivatives and a tricyclic ketone proceeded with good to excellent yields.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Nov","modification":"2026-05-30T20:53:20.417Z","creation":"2025-04-04T10:02:09.076Z"},"accession":"S-EPMC9075147","cross_references":{"pubmed":["35539044"],"doi":["10.1039/c9ra06088j"]}}