{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhu YH"],"funding":["National Research Foundation of Korea"],"pagination":["225-233"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6458232"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["59(2)"],"pubmed_abstract":["A novel alcohol dehydrogenase from <i>Bartonella apis</i> (BaADH) was heterologous expressed in <i>Escherichia coli</i>. Its biochemical properties were investigated and used to catalyze the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE), which is a chiral intermediate of the cholesterol-lowering drug atorvastatin. The purified recombinant BaADH displayed 182.4 U/mg of the specific activity using ethyl 4-chloroacetoacetate as substrate under the conditions of 50 °C in pH 7.0 Tris-HCl buffer. It was stable in storage buffers of pH 7 to 9 and retains up to 96.7% of the initial activity after 24 h. The <i>K</i> <sub>m</sub> and <i>V</i> <sub>max</sub> values of BaADH were 0.11 mM and 190.4 μmol min<sup>-1</sup> mg<sup>-1</sup>, respectively. Synthesis of (S)-CHBE catalyzed by BaADH was performed with a cofactor regeneration system using a glucose dehydrogenase, and a conversion of 94.9% can be achieved after 1 h reaction. Homology modeling and substrate docking revealed that a typical catalytic triad is in contact with local water molecules to form a catalytic system. The results indicated this ADH could contribute to the further enzymatic synthesis of (S)-CHBE."],"journal":["Indian journal of microbiology"],"pubmed_title":["Cloning, Expression and Characterization of a Highly Active Alcohol Dehydrogenase for Production of Ethyl (S)-4-Chloro-3-Hydroxybutyrate."],"pmcid":["PMC6458232"],"funding_grant_id":["NRF-2018H1D3A2001746"],"pubmed_authors":["Liu CY","Cai S","Zhang YW","Lee JK","Kim IW","Zhu YH","Kalia VC","Guo LB"],"additional_accession":[]},"is_claimable":false,"name":"Cloning, Expression and Characterization of a Highly Active Alcohol Dehydrogenase for Production of Ethyl (S)-4-Chloro-3-Hydroxybutyrate.","description":"A novel alcohol dehydrogenase from <i>Bartonella apis</i> (BaADH) was heterologous expressed in <i>Escherichia coli</i>. Its biochemical properties were investigated and used to catalyze the synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE), which is a chiral intermediate of the cholesterol-lowering drug atorvastatin. The purified recombinant BaADH displayed 182.4 U/mg of the specific activity using ethyl 4-chloroacetoacetate as substrate under the conditions of 50 °C in pH 7.0 Tris-HCl buffer. It was stable in storage buffers of pH 7 to 9 and retains up to 96.7% of the initial activity after 24 h. The <i>K</i> <sub>m</sub> and <i>V</i> <sub>max</sub> values of BaADH were 0.11 mM and 190.4 μmol min<sup>-1</sup> mg<sup>-1</sup>, respectively. Synthesis of (S)-CHBE catalyzed by BaADH was performed with a cofactor regeneration system using a glucose dehydrogenase, and a conversion of 94.9% can be achieved after 1 h reaction. Homology modeling and substrate docking revealed that a typical catalytic triad is in contact with local water molecules to form a catalytic system. The results indicated this ADH could contribute to the further enzymatic synthesis of (S)-CHBE.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jun","modification":"2024-02-15T09:42:22.395Z","creation":"2020-06-04T07:10:35Z"},"accession":"S-EPMC6458232","cross_references":{"pubmed":["31031438"],"doi":["10.1007/s12088-019-00795-0"]}}