Review
doi: 10.1016/j.copbio.2004.06.007.
Enantioselective biocatalysis optimized by directed evolution
Affiliations
- PMID: 15358000
- DOI: 10.1016/j.copbio.2004.06.007
Item in Clipboard
Review
Enantioselective biocatalysis optimized by directed evolution
Curr Opin Biotechnol.
2004 Aug.
Abstract
Directed evolution methods are now widely used for the optimization of diverse enzyme properties, which include biotechnologically relevant characteristics like stability, regioselectivity and, in particular, enantioselectivity. In principle, three different approaches are followed to optimize enantioselective reactions: the development of whole-cell biocatalysts through the creation of designer organisms; the optimization of enzymes with existing enantioselectivity for process conditions; and the evolution of novel enantioselective biocatalysts starting from non-selective wild-type enzymes.
Similar articles
-
Novel methods for directed evolution of enzymes: quality, not quantity.Curr Opin Biotechnol. 2004 Aug;15(4):291-7. doi: 10.1016/j.copbio.2004.05.004. Curr Opin Biotechnol. 2004. PMID: 15296927 Review.
-
Directed evolution of enzymes for applied biocatalysis.Trends Biotechnol. 2003 Nov;21(11):474-8. doi: 10.1016/j.tibtech.2003.09.001. Trends Biotechnol. 2003. PMID: 14573359
-
Enzyme optimization: moving from blind evolution to statistical exploration of sequence-function space.Trends Biotechnol. 2008 Mar;26(3):132-8. doi: 10.1016/j.tibtech.2007.12.001. Epub 2008 Jan 28. Trends Biotechnol. 2008. PMID: 18222559 Review.
-
Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions.Angew Chem Int Ed Engl. 2011 Jan 3;50(1):138-74. doi: 10.1002/anie.201000826. Angew Chem Int Ed Engl. 2011. PMID: 20715024 Review.
-
Enzyme engineering for enantioselectivity: from trial-and-error to rational design?Trends Biotechnol. 2010 Jan;28(1):46-54. doi: 10.1016/j.tibtech.2009.10.001. Epub 2009 Nov 11. Trends Biotechnol. 2010. PMID: 19913316 Review.
Cited by
-
Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea.EMBO J. 2006 Sep 6;25(17):4152-62. doi: 10.1038/sj.emboj.7601278. Epub 2006 Aug 10. EMBO J. 2006. PMID: 16902403 Free PMC article.
-
Structurally Informed Mutagenesis of a Stereochemically Promiscuous Aldolase Produces Mutants That Catalyze the Diastereoselective Syntheses of All Four Stereoisomers of 3-Deoxy-hexulosonic Acid.ACS Catal. 2022 Sep 16;12(18):11444-11455. doi: 10.1021/acscatal.2c03285. Epub 2022 Sep 6. ACS Catal. 2022. PMID: 36158901 Free PMC article.
-
Advances in chiral nanozymes: a review.Mikrochim Acta. 2019 Nov 15;186(12):782. doi: 10.1007/s00604-019-3922-7. Mikrochim Acta. 2019. PMID: 31729634 Review.
-
Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase.Angew Chem Int Ed Engl. 2016 Feb 18;55(8):2683-7. doi: 10.1002/anie.201508287. Epub 2016 Jan 21. Angew Chem Int Ed Engl. 2016. PMID: 26797714 Free PMC article.
-
Nanozymes-Hitting the Biosensing "Target".Sensors (Basel). 2021 Jul 31;21(15):5201. doi: 10.3390/s21155201. Sensors (Basel). 2021. PMID: 34372441 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
