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Updated: Oct 18, 2025
Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
Cloning and functional characterization of the geranylgeranyl diphosphate synthase(GGPPS)from Elizabethkingia
Qiang Yang1, Zhiming Zheng2, Genhai Zhao2
1Institute of Intelligent Machines, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei, 230031, PR China; University of Science and Technology of China, Hefei, 230026, PR China.
Abstract:
To date, there is no functional characterization of EmGGPPS (from Elizabethkingia meningoseptica sp.F2) as enzymes catalyzing GGPP. In this research, maltose-binding protein (MBP), disulfide bond A (DbsA), disulfide bond C (DbsC), and two other small protein tags, GB1 (Protein G B1 domain) and ZZ (Protein A IgG ZZ repeat domain), were used as fusion partners to construct an EmGGPPS fusion expression system. The results indicated that the expression of MBP-EmGGPPS was higher than that of the other four fusion proteins in E. coli BL21 (DE3). Additionally, using EmGGPPS as a catalyst for the production of GGPP was verified using a color complementation assay in Escherichia coli. In parallel with it, the enzyme activity experiment in vitro showed that the EmGGPPS protein could produce GGPP, GPP and FPP. Finally, we successfully demonstrated MK-4 production in engineered E. coli by overexpression of EmGGPPS.
