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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Phosphofructokinase II (PEK II) from Trichoderma reesei was partially purified (247-fold). The calculated Km values for fructose 6-phosphate and ATP were 0.7 mM and 40 microM, respectively. Upon incubation in the presence of [gamma-32P]ATP, the enzyme formed a radioactive phosphoprotein with molecular mass of 67 kDa in autoradiography analysis after SDS-PAGE. Upon incubation in the presence of ATP-Mg and the catalytic subunit of cAMP-dependent protein kinase, its activity was not modified. The same result was obtained when a cell-free extract of T. reesei was incubated with ATP-Mg and cAMP. 2,4-Dinitrophenol caused a transient rise in cAMP levels in the fungal cell. The results provide evidence that the fructose 2,6-bisphosphate level in T. reesei is independent of cAMP concentrations and not related to a cAMP-dependent mechanism, but to the availability of substrate fructose 6-phosphate.

Characterization of phosphofructokinase II and regulation of fructose 2,6-bisphosphate levels in Trichoderma reesei