Construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates
Systems that can regulate and coordinate the expression of multiple enzymes for metabolic regulation and synthesis of important drug intermediates are poorly explored. In this work, a strategy for constructing a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug interm...
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| Format: | Online |
| Language: | English |
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Nature Publishing Group
2016
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4960608/ |
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pubmed-49606082016-08-05 Construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates Jiang, Wei Fang, Baishan Article Systems that can regulate and coordinate the expression of multiple enzymes for metabolic regulation and synthesis of important drug intermediates are poorly explored. In this work, a strategy for constructing a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates was developed and evaluated by connecting protein-protein expressions, regulating the strength of ribosome binding sites (RBS) and detecting the system capacity for producing chiral amino acid. Results demonstrated that the dual-enzyme system had good enantioselectivity, low cost, high stability, high conversion rate and approximately 100% substrate conversion. This study has paved a new way of exploring metabolic mechanism of functional genes and engineering whole cell-catalysts for synthesis of chiral α-hydroxy acids or chiral amino acids. Nature Publishing Group 2016-07-26 /pmc/articles/PMC4960608/ /pubmed/27456301 http://dx.doi.org/10.1038/srep30462 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Jiang, Wei Fang, Baishan |
| spellingShingle |
Jiang, Wei Fang, Baishan Construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates |
| author_facet |
Jiang, Wei Fang, Baishan |
| author_sort |
Jiang, Wei |
| title |
Construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates |
| title_short |
Construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates |
| title_full |
Construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates |
| title_fullStr |
Construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates |
| title_full_unstemmed |
Construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates |
| title_sort |
construction of a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates |
| description |
Systems that can regulate and coordinate the expression of multiple enzymes for metabolic regulation and synthesis of important drug intermediates are poorly explored. In this work, a strategy for constructing a tunable multi-enzyme-coordinate expression system for biosynthesis of chiral drug intermediates was developed and evaluated by connecting protein-protein expressions, regulating the strength of ribosome binding sites (RBS) and detecting the system capacity for producing chiral amino acid. Results demonstrated that the dual-enzyme system had good enantioselectivity, low cost, high stability, high conversion rate and approximately 100% substrate conversion. This study has paved a new way of exploring metabolic mechanism of functional genes and engineering whole cell-catalysts for synthesis of chiral α-hydroxy acids or chiral amino acids. |
| publisher |
Nature Publishing Group |
| publishDate |
2016 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4960608/ |
| _version_ |
1613614907881684992 |