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Volume 139, Issue 6

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

Abstract

Phosphofructokinase II (PFK II) from was partially purified (247-fold). The calculated values for fructose 6-phosphate and ATP were 0·7 m and 40 μ, respectively. Upon incubation in the presence of [γ-P]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 was incubated with ATP-Mg and cAMP. 2,4-Dinitrophenol caused a transient rise in cAMP levels in the fungal cell. These results provide evidence that the fructose 2,6-bisphosphate level in is independent of cAMP concentrations and not related to a cAMP-dependent mechanism, but to the availability of substrate fructose 6-phosphate.

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© Society for General Microbiology 1993
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1993-06-01
2025-04-25
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/content/journal/micro/10.1099/00221287-139-6-1363
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Characterization of phosphofructokinase II and regulation of fructose 2,6-bisphosphate levels in Trichoderma reesei
Microbiology 139, 1363 (1993); https://doi.org/10.1099/00221287-139-6-1363
/content/journal/micro/10.1099/00221287-139-6-1363
/content/journal/micro/10.1099/00221287-139-6-1363
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