Protein engineering of oxidoreductases utilizing nicotinamide-based coenzymes, with applications in synthetic biology
Abstract
Two natural nicotinamide-based coenzymes (NAD and NADP) are indispensably required by the vast majority of oxidoreductases for catabolism and anabolism, respectively. Most NAD(P)-dependent oxidoreductases prefer one coenzyme as an electron acceptor or donor to the other depending on their different metabolic roles. This coenzyme preference associated with coenzyme imbalance presents some challenges for the construction of high-efficiency in vivo and in vitro synthetic biology pathways. Changing the coenzyme preference of NAD(P)-dependent oxidoreductases is an important area of protein engineering, which is closely related to product-oriented synthetic biology projects. This review focuses on the methodology of nicotinamide-based coenzyme engineering, with its application in improving product yields and decreasing production costs. Biomimetic nicotinamide-containing coenzymes have been proposed to replace natural coenzymes because they are more stable and less costly than natural coenzymes. Recent advances in the switching of coenzyme preference from natural to biomimetic coenzymes are also covered in this review. Engineering coenzyme preferences from natural to biomimetic coenzymes has become an important direction for coenzyme engineering, especially for in vitro synthetic pathways and in vivo bioorthogonal redox pathways.
- Authors:
-
[3]
- Chinese Academy of Sciences (CAS), Tianjin (China)
- Virginia Polytechnic Institute and State University (Virginia Tech), Blacksburg, VA (United States)
- Chinese Academy of Sciences (CAS), Tianjin (China); Virginia Polytechnic Institute and State University (Virginia Tech), Blacksburg, VA (United States)
- Publication Date:
- Research Org.:
- National Renewable Energy Laboratory (NREL), Golden, CO (United States). Golden Field Office (GFO)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Earth and Environmental Systems Science Division; Key Research Program of the Chinese Academy of Sciences; National Natural Science Foundation of China (NSFC)
- OSTI Identifier:
- 1629769
- Grant/Contract Number:
- EE0006968; ZDRW-ZS-2016-3; 31600636
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Synthetic and Systems Biotechnology
- Additional Journal Information:
- Journal Volume: 2; Journal Issue: 3; Journal ID: ISSN 2405-805X
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; coenzyme engineering; nicotinamide-based coenzymes; NAD; NADP; protein engineering; synthetic biology; biomimetic coenzymes
Citation Formats
You, Chun, Huang, Rui, Wei, Xinlei, Zhu, Zhiguang, and Zhang, Yi-Heng Percival. Protein engineering of oxidoreductases utilizing nicotinamide-based coenzymes, with applications in synthetic biology. United States: N. p., 2017.
Web. doi:10.1016/j.synbio.2017.09.002.
You, Chun, Huang, Rui, Wei, Xinlei, Zhu, Zhiguang, & Zhang, Yi-Heng Percival. Protein engineering of oxidoreductases utilizing nicotinamide-based coenzymes, with applications in synthetic biology. United States. https://doi.org/10.1016/j.synbio.2017.09.002
You, Chun, Huang, Rui, Wei, Xinlei, Zhu, Zhiguang, and Zhang, Yi-Heng Percival. Fri .
"Protein engineering of oxidoreductases utilizing nicotinamide-based coenzymes, with applications in synthetic biology". United States. https://doi.org/10.1016/j.synbio.2017.09.002. https://www.osti.gov/servlets/purl/1629769.
@article{osti_1629769,
title = {Protein engineering of oxidoreductases utilizing nicotinamide-based coenzymes, with applications in synthetic biology},
author = {You, Chun and Huang, Rui and Wei, Xinlei and Zhu, Zhiguang and Zhang, Yi-Heng Percival},
abstractNote = {Two natural nicotinamide-based coenzymes (NAD and NADP) are indispensably required by the vast majority of oxidoreductases for catabolism and anabolism, respectively. Most NAD(P)-dependent oxidoreductases prefer one coenzyme as an electron acceptor or donor to the other depending on their different metabolic roles. This coenzyme preference associated with coenzyme imbalance presents some challenges for the construction of high-efficiency in vivo and in vitro synthetic biology pathways. Changing the coenzyme preference of NAD(P)-dependent oxidoreductases is an important area of protein engineering, which is closely related to product-oriented synthetic biology projects. This review focuses on the methodology of nicotinamide-based coenzyme engineering, with its application in improving product yields and decreasing production costs. Biomimetic nicotinamide-containing coenzymes have been proposed to replace natural coenzymes because they are more stable and less costly than natural coenzymes. Recent advances in the switching of coenzyme preference from natural to biomimetic coenzymes are also covered in this review. Engineering coenzyme preferences from natural to biomimetic coenzymes has become an important direction for coenzyme engineering, especially for in vitro synthetic pathways and in vivo bioorthogonal redox pathways.},
doi = {10.1016/j.synbio.2017.09.002},
journal = {Synthetic and Systems Biotechnology},
number = 3,
volume = 2,
place = {United States},
year = {Fri Oct 06 00:00:00 EDT 2017},
month = {Fri Oct 06 00:00:00 EDT 2017}
}
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