دورية أكاديمية
Mutations Increasing Cofactor Affinity, Improve Stability and Activity of a Baeyer-Villiger Monooxygenase.
العنوان: | Mutations Increasing Cofactor Affinity, Improve Stability and Activity of a Baeyer-Villiger Monooxygenase. |
---|---|
المؤلفون: | Mansouri HR; Institute of Applied Synthetic Chemistry, TU Wien, Getreidemarkt 9, 1060 Vienna, Austria., Gracia Carmona O; Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences, 1190 Vienna, Austria., Jodlbauer J; Institute of Applied Synthetic Chemistry, TU Wien, Getreidemarkt 9, 1060 Vienna, Austria., Schweiger L; Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria., Fink MJ; Institute of Applied Synthetic Chemistry, TU Wien, Getreidemarkt 9, 1060 Vienna, Austria., Breslmayr E; Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria., Laurent C; Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria., Feroz S; Institute of Applied Synthetic Chemistry, TU Wien, Getreidemarkt 9, 1060 Vienna, Austria.; Department of Biosciences, College of Science, University of Hafr Al Batin, PO Box 1803, Hafr Al Batin, 39524, Saudi Arabia., P Goncalves LC; Institut de Chimie de Nice CRNS UMR7272, Université Côte d'Azur, 28 Avenue Valrose, 06108 Nice, France., Rial DV; Área Biología Molecular, Departamento de Ciencias Biológicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario (UNR), and Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Suipacha 531, S2002LRK Rosario, Argentina., Mihovilovic MD; Institute of Applied Synthetic Chemistry, TU Wien, Getreidemarkt 9, 1060 Vienna, Austria., Bommarius AS; School of Chemical & Biomolecular Engineering, Engineered Biosystems Building (EBB), Georgia Institute of Technology, 950 Atlantic Drive, N.W., Atlanta, Georgia 30332, United States., Ludwig R; Biocatalysis and Biosensing Laboratory, Department of Food Science and Technology, BOKU-University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria., Oostenbrink C; Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences, 1190 Vienna, Austria., Rudroff F; Institute of Applied Synthetic Chemistry, TU Wien, Getreidemarkt 9, 1060 Vienna, Austria. |
المصدر: | ACS catalysis [ACS Catal] 2022 Oct 07; Vol. 12 (19), pp. 11761-11766. Date of Electronic Publication: 2022 Sep 13. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 101562209 Publication Model: Print-Electronic Cited Medium: Print ISSN: 2155-5435 (Print) NLM ISO Abbreviation: ACS Catal Subsets: PubMed not MEDLINE |
أسماء مطبوعة: | Original Publication: Washington, DC : American Chemical Society, c2011- |
مستخلص: | The typically low thermodynamic and kinetic stability of enzymes is a bottleneck for their application in industrial synthesis. Baeyer-Villiger monooxygenases, which oxidize ketones to lactones using aerial oxygen, among other activities, suffer particularly from these instabilities. Previous efforts in protein engineering have increased thermodynamic stability but at the price of decreased activity. Here, we solved this trade-off by introducing mutations in a cyclohexanone monooxygenase from Acinetobacter sp., guided by a combination of rational and structure-guided consensus approaches. We developed variants with improved activity (1.5- to 2.5-fold) and increased thermodynamic (+5 °C T Competing Interests: The authors declare no competing financial interest. (© 2022 The Authors. Published by American Chemical Society.) |
References: | J Bacteriol. 1988 Feb;170(2):781-9. (PMID: 3338974) Methods Mol Biol. 2020;2073:163-181. (PMID: 31612442) Biotechnol Bioeng. 2017 Aug;114(8):1670-1678. (PMID: 28409822) J Mol Evol. 2017 Dec;85(5-6):205-218. (PMID: 29177972) Bioorg Med Chem Lett. 2011 Oct 15;21(20):6135-8. (PMID: 21900007) Chem Rev. 2011 Jul 13;111(7):4165-222. (PMID: 21542563) Biotechnol Appl Biochem. 2022 Apr;69(2):389-409. (PMID: 33555054) Angew Chem Int Ed Engl. 2016 Dec 19;55(51):15852-15855. (PMID: 27873437) Chembiochem. 2007 Dec 17;8(18):2295-301. (PMID: 17990264) Enzymes. 2020;47:231-281. (PMID: 32951825) Chem Eng Sci. 2010 Mar 15;65(6):2118-2124. (PMID: 20885990) Angew Chem Int Ed Engl. 2021 Jan 4;60(1):88-119. (PMID: 32558088) Eur J Biochem. 1976 Mar 16;63(1):175-92. (PMID: 1261545) FEBS Open Bio. 2014 Feb 03;4:168-74. (PMID: 24649397) Biotechnol Bioeng. 2019 Sep;116(9):2167-2177. (PMID: 31124128) J Am Chem Soc. 2017 Jan 18;139(2):627-630. (PMID: 28010060) Angew Chem Int Ed Engl. 2017 Jul 24;56(31):8942-8973. (PMID: 28407390) Biotechnol Adv. 2018 Jan - Feb;36(1):247-263. (PMID: 29174001) Chembiochem. 2010 Dec 10;11(18):2589-96. (PMID: 21080396) Chem Soc Rev. 2013 Aug 7;42(15):6534-65. (PMID: 23807146) Curr Opin Struct Biol. 2005 Aug;15(4):447-52. (PMID: 16006119) Appl Environ Microbiol. 2014 Feb;80(4):1515-27. (PMID: 24362426) Chem Commun (Camb). 2015 Feb 18;51(14):2874-7. (PMID: 25583122) J Biotechnol. 2015 Nov 20;214:199-211. (PMID: 26410456) Appl Microbiol Biotechnol. 2005 Jan;66(4):393-400. (PMID: 15599520) Chembiochem. 2020 Apr 1;21(7):971-977. (PMID: 31608538) J Org Chem. 2018 Jul 20;83(14):7453-7458. (PMID: 29932340) Protein Sci. 2001 Sep;10(9):1712-28. (PMID: 11514662) Chembiochem. 2017 Aug 17;18(16):1627-1638. (PMID: 28504873) PLoS Comput Biol. 2007 Jul;3(7):e121. (PMID: 17658942) Chembiochem. 2016 Dec 14;17(24):2312-2315. (PMID: 27735116) |
تواريخ الأحداث: | Date Created: 20221017 Latest Revision: 20221019 |
رمز التحديث: | 20240628 |
مُعرف محوري في PubMed: | PMC9552169 |
DOI: | 10.1021/acscatal.2c03225 |
PMID: | 36249873 |
قاعدة البيانات: | MEDLINE |
كن أول من يترك تعليقا!