Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/163555
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dc.contributor.authorLi, Pingen_US
dc.contributor.authorJing, Ruxianen_US
dc.contributor.authorZhou, Mengpingen_US
dc.contributor.authorJia, Peien_US
dc.contributor.authorLi, Zhuoyaen_US
dc.contributor.authorLiu, Guoshengen_US
dc.contributor.authorWang, Zhenyuen_US
dc.contributor.authorWang, Haileien_US
dc.date.accessioned2022-12-09T01:46:26Z-
dc.date.available2022-12-09T01:46:26Z-
dc.date.issued2022-
dc.identifier.citationLi, P., Jing, R., Zhou, M., Jia, P., Li, Z., Liu, G., Wang, Z. & Wang, H. (2022). Whole-cell biosynthesis of cytarabine by an unnecessary protein-reduced Escherichia coli that coexpresses purine and uracil phosphorylase. Biotechnology and Bioengineering, 119(7), 1768-1780. https://dx.doi.org/10.1002/bit.28098en_US
dc.identifier.issn0006-3592en_US
dc.identifier.urihttps://hdl.handle.net/10356/163555-
dc.description.abstractCurrently, whole-cell catalysts face challenges due to the complexity of reaction systems, although they have a cost advantage over pure enzymes. In this study, cytarabine was synthesized by purified purine phosphorylase 1 (PNP1) and uracil phosphorylase (UP), and the conversion of cytarabine from adenine arabinoside reached 72.3 ± 4.3%. However, the synthesis was unsuccessful by whole-cell catalysis due to interference from unnecessary proteins (UNPs) in cells. Thus, we carried out a large-scale gene editing involving 377 genes in the genome of Escherichia coli to reduce the negative effect of UNPs on substrate conversion and cytarabine production. Finally, the PNP1 and UP activities of the obtained mutant were increased significantly compared with the parental strain, and more importantly, the conversion rate of cytarabine by whole-cell catalysis reached 67.4 ± 2.5%. The lack of 148 proteins and downregulation of 783 proteins caused by gene editing were equivalent to partial purification of the enzymes within cells, and thus, we provided inspiration to solve the problem caused by UNP interference, which is ubiquitous in the field of whole-cell catalysis.en_US
dc.language.isoenen_US
dc.relation.ispartofBiotechnology and Bioengineeringen_US
dc.rights© 2022 Wiley Periodicals LLC. All rights reserved.en_US
dc.subjectScience::Biological sciencesen_US
dc.titleWhole-cell biosynthesis of cytarabine by an unnecessary protein-reduced Escherichia coli that coexpresses purine and uracil phosphorylaseen_US
dc.typeJournal Articleen
dc.contributor.researchNanyang Environment and Water Research Instituteen_US
dc.contributor.researchAdvanced Environmental Biotechnology Centre (AEBC)en_US
dc.identifier.doi10.1002/bit.28098-
dc.identifier.pmid35383880-
dc.identifier.scopus2-s2.0-85128072813-
dc.identifier.issue7en_US
dc.identifier.volume119en_US
dc.identifier.spage1768en_US
dc.identifier.epage1780en_US
dc.subject.keywordsCytarabineen_US
dc.subject.keywordsEscherichia Colien_US
dc.description.acknowledgementThis study was supported by the Excellent Scientific and Technological Innovation Team of Henan Normal University, China (5101049170501) and the National Science Foundations of China (U160411067).en_US
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