{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen Y"],"funding":["Shanghai Municipal Education Commission","Shanghai Institute of Technology"],"pagination":["2325-2331"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9059822"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(4)"],"pubmed_abstract":["The production of (<i>S</i>)-<i>N</i>-boc-3-hydroxy piperidine (NBHP) <i>via</i> asymmetric bioreduction of 1-boc-3-piperidinone with reductase is impeded by the need for expensive coenzymes NAD(P)H. In order to regenerate the coenzyme <i>in situ</i>, the gene of alcohol dehydrogenase from <i>Thermoanaerobacter brockii</i> and glucose dehydrogenase from <i>Bacillus subtilis</i> were ligated into the multiple cloning sites of pRSFDuet-1 plasmid to construct the recombinant <i>Escherichia</i> BL21 (DE3) that co-expressing alcohol dehydrogenase and glucose dehydrogenase. Different culture conditions including the medium composition, inducer and pH <i>etc</i> were systematically investigated to improve the enzyme production. The enzyme activity was increased more than 11-fold under optimal cul"],"journal":["RSC advances"],"pubmed_title":["Efficient synthesis of Ibrutinib chiral intermediate in high space-time yield by recombinant <i>E. coli</i> co-expressing alcohol dehydrogenase and glucose dehydrogenase."],"pmcid":["PMC9059822"],"funding_grant_id":["No. ZZyyx15011","No. YJ2015-36"],"pubmed_authors":["Ma B","Cao S","Chen Y","Wu X","Xu Y"],"additional_accession":[]},"is_claimable":false,"name":"Efficient synthesis of Ibrutinib chiral intermediate in high space-time yield by recombinant <i>E. coli</i> co-expressing alcohol dehydrogenase and glucose dehydrogenase.","description":"The production of (<i>S</i>)-<i>N</i>-boc-3-hydroxy piperidine (NBHP) <i>via</i> asymmetric bioreduction of 1-boc-3-piperidinone with reductase is impeded by the need for expensive coenzymes NAD(P)H. In order to regenerate the coenzyme <i>in situ</i>, the gene of alcohol dehydrogenase from <i>Thermoanaerobacter brockii</i> and glucose dehydrogenase from <i>Bacillus subtilis</i> were ligated into the multiple cloning sites of pRSFDuet-1 plasmid to construct the recombinant <i>Escherichia</i> BL21 (DE3) that co-expressing alcohol dehydrogenase and glucose dehydrogenase. Different culture conditions including the medium composition, inducer and pH <i>etc</i> were systematically investigated to improve the enzyme production. The enzyme activity was increased more than 11-fold under optimal cul","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jan","modification":"2025-05-18T12:06:57.788Z","creation":"2025-05-18T12:06:57.788Z"},"accession":"S-EPMC9059822","cross_references":{"pubmed":["35516114"],"doi":["10.1039/c8ra08100j"]}}