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Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance.
Appl Biochem Biotechnol. 2020 Jan; 190(1):18-29.AB

Abstract

NAD(P)H-dependent enzymes are ideal biocatalysts for the industrial production of chiral compounds, such as chiral alcohols, chiral amino acids, and chiral amines; however, efficient strategies for the regeneration of coenzyme are expected as costly of the coenzymes. Herein, a solvent-tolerant isopropanol dehydrogenase (IDH) showing lower similarity (37%) with other proteins was obtained and characterized. The enzyme exhibits high catalysis ability of its substrates methanol, ethanol, ethylene glycol, glycerol, isopropanol, n-butanol, isobutanol, and acetone. And it has good adaptability in organic solvents (isopropanol, acetonitrile, acetone, and acetophenone). Interaction force and the corresponding amino acid residues between IDH and NAD+ or NADP+ were parsed by docking. The wide substrate spectrum, excellent organic solvent tolerance, and good biocatalytic activity make the excavated enzyme a promising biocatalyst for the production of chiral compounds industrially and the construction of coenzyme regeneration systems in aqueous organic phase or organic phase.

Authors+Show Affiliations

Department of Bioengineering and Biotechnology, College of Chemical Engineering, Huaqiao University, Xiamen, 361021, China. tianya416@126.com.Department of Chemical and Biochemical Engineering, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen, 361005, China. fbs@xmu.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31301008

Citation

Jiang, Wei, and Bai-Shan Fang. "Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase With Wide Substrate Spectrum and Excellent Organic Solvent Tolerance." Applied Biochemistry and Biotechnology, vol. 190, no. 1, 2020, pp. 18-29.
Jiang W, Fang BS. Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance. Appl Biochem Biotechnol. 2020;190(1):18-29.
Jiang, W., & Fang, B. S. (2020). Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance. Applied Biochemistry and Biotechnology, 190(1), 18-29. https://doi.org/10.1007/s12010-019-03091-1
Jiang W, Fang BS. Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase With Wide Substrate Spectrum and Excellent Organic Solvent Tolerance. Appl Biochem Biotechnol. 2020;190(1):18-29. PubMed PMID: 31301008.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance. AU - Jiang,Wei, AU - Fang,Bai-Shan, Y1 - 2019/07/12/ PY - 2019/03/28/received PY - 2019/07/05/accepted PY - 2019/7/14/pubmed PY - 2019/7/14/medline PY - 2019/7/14/entrez KW - Coenzyme regeneration KW - Docking KW - NAD(P)+-dependent dehydrogenase KW - Organic solvent-tolerant KW - n-Butanol SP - 18 EP - 29 JF - Applied biochemistry and biotechnology JO - Appl. Biochem. Biotechnol. VL - 190 IS - 1 N2 - NAD(P)H-dependent enzymes are ideal biocatalysts for the industrial production of chiral compounds, such as chiral alcohols, chiral amino acids, and chiral amines; however, efficient strategies for the regeneration of coenzyme are expected as costly of the coenzymes. Herein, a solvent-tolerant isopropanol dehydrogenase (IDH) showing lower similarity (37%) with other proteins was obtained and characterized. The enzyme exhibits high catalysis ability of its substrates methanol, ethanol, ethylene glycol, glycerol, isopropanol, n-butanol, isobutanol, and acetone. And it has good adaptability in organic solvents (isopropanol, acetonitrile, acetone, and acetophenone). Interaction force and the corresponding amino acid residues between IDH and NAD+ or NADP+ were parsed by docking. The wide substrate spectrum, excellent organic solvent tolerance, and good biocatalytic activity make the excavated enzyme a promising biocatalyst for the production of chiral compounds industrially and the construction of coenzyme regeneration systems in aqueous organic phase or organic phase. SN - 1559-0291 UR - https://www.unboundmedicine.com/medline/citation/31301008/Coenzyme_Binding_Site_Analysis_of_an_Isopropanol_Dehydrogenase_with_Wide_Substrate_Spectrum_and_Excellent_Organic_Solvent_Tolerance_ L2 - https://dx.doi.org/10.1007/s12010-019-03091-1 DB - PRIME DP - Unbound Medicine ER -