English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

E. coli expression plasmids for yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphatase (EC 3.1.3.11) as wild-type enzyme and as lacZ fusion protein have been constructed from a pUC vector and a fragment of genomic yeast DNA. Both proteins were overexpressed in E. coli strain TG2 as enzymatically active soluble forms and purified to homogeneity. While the wild-type enzyme is indistinguishable from the authentic yeast enzyme with respect to molecular size, specific activity and kinetic properties, the lacZ fusion protein behaves differently. Being a tetramer like the wild-type enzyme, the specific activity of the purified fusion protein is lower than that of the native enzyme. In contrast to the wild-type enzyme the fusion fructose-1,6-bisphosphatase is not inhibited by excess substrate. Inhibition of the fusion protein by the most potent allosteric effectors of fructose-1,6-bisphosphatase, AMP and fructose 2,6-bisphosphate, is weaker than observed with the wild-type enzyme. The fusion protein but not the wild-type enzyme was found to bind to immobilized Procion Navy H-ER. This was employed to purify the fusion fructose-1,6-bisphosphatase by affinity chromatography. Polyclonal antibodies raised in rabbits against the fusion enzyme were found to cross-react with the wild-type enzyme, but not with E. coli proteins. Both fructose-1,6-bisphosphatases complement the fructose-1,6-bisphosphatase mutant DF656 of E. coli.

Overexpression of Catalytically Active Yeast (Saccharomyces cerevisiae) Fructose-1,6-bisphosphatase in Escherichia coli