Reassessing acetyl-CoA supply and NADPH availability for mevalonate biosynthesis from glycerol in Escherichia coli
- Authors
- Wang, Yan; Zhou, Shenting; Li, Runyi; Liu, Qian; Shao, Xixi; Zhu, Liyan; Kang, Min-Kyoung; Wei, Gongyuan; Kim, Seon-Won; Wang, Chonglong
- Issue Date
- Oct-2022
- Publisher
- Wiley - V C H Verlag GmbbH & Co.
- Keywords
- acetyl-CoA; E; coli; mevalonate; NADPH; phosphoketolase
- Citation
- Biotechnology and Bioengineering, v.119, no.10, pp 2868 - 2877
- Pages
- 10
- Indexed
- SCIE
SCOPUS
- Journal Title
- Biotechnology and Bioengineering
- Volume
- 119
- Number
- 10
- Start Page
- 2868
- End Page
- 2877
- URI
- https://scholarworks.gnu.ac.kr/handle/sw.gnu/849
- DOI
- 10.1002/bit.28167
- ISSN
- 0006-3592
1097-0290
- Abstract
- Mevalonate is an important platform compound for the biosynthesis of isoprenoids. It can be synthesized from acetyl-CoA in the presence of nicotinamide adenine dinucleotide phosphate (NADPH) by the introduced mvaES operon in Escherichia coli. The influences of E. coli hosts, acetyl-CoA supply, and NADPH availability were assessed and engineered to improve the production titer and yield of mevalonate from glycerol. As a result, E. coli DH5 alpha was found to be the best host with high specific capability and titer of mevalonate from glycerol. Through the engineering of phosphoketolase-phosphotransacetylase (xPK-PTA) bypass and NADPH availability, a final titer of 7.21 g/L with a specific capability of 1.36 g/g dry cell weight was gained in flask culture. Our work could offer new information to metabolically engineer the mevalonate pathway for the efficient production of isoprenoids.
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