Tags

Type your tag names separated by a space and hit enter

Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance.

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, 2019.
Jiang W, Fang BS. Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance. Appl Biochem Biotechnol. 2019.
Jiang, W., & Fang, B. S. (2019). Coenzyme Binding Site Analysis of an Isopropanol Dehydrogenase with Wide Substrate Spectrum and Excellent Organic Solvent Tolerance. Applied Biochemistry and Biotechnology, doi: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. 2019 Jul 12; 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/entrez KW - Coenzyme regeneration KW - Docking KW - NAD(P)+-dependent dehydrogenase KW - Organic solvent-tolerant KW - n-Butanol JF - Applied biochemistry and biotechnology JO - Appl. Biochem. Biotechnol. 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 -
Unbound Prime app for iOS iPhone iPadUnbound PubMed app for AndroidAlso Available:
Unbound MEDLINE
Unbound PubMed app for WindowsUnbound PubMed app for MAC OSX Yosemite Macbook Air pro