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

The maximum catalytic activity of pyrophosphate: fructosc-6-phosphate 1-phosphotransferase (PPi-PFK) was approximately three fold greater than that of ATP: fructosc-6-phosphate 1-phosphotransferase (ATP-PFK) in Catharanthus roseus cells at any stage of culture. The levels of both enzymes increased after subculture of the cells, reached their maximum levels on day 3-4, and then decreased. PPi-PFK partially purified from Catharanthus roseus required fructose-2,6-bis- phosphate (F2,6BP) for its activity. The Ka value of the enzyme for F2,6BP was 26 nᴍ. The Km values for fructose-6-phosphate (F6P) and sodium pyrophosphate (PPi), at physiological pH (7.2) in the presence of 1 µᴍ F2,6BP, were 0.59 mᴍ and 48 µᴍ, respectively. Intracellular levels of PPi and F6P varied from 17-71 nmol and from 37-65 nm per g fresh weight of the cells during culture. These results suggest that PPi-PFK is functional in Catharanthus roseus cells in vivo. The role of PPi-PFK in carbohydrate metabolism in heterotrophic, cultured plant cells is discussed.

Role of Pyrophosphate: Fructose-6-phosphate 1-Phosphotransferase in Glycolysis in Cultured Catharanthus roseus Cells