@article{mbs:/content/journal/micro/10.1099/00221287-129-10-3281, author = "Van Laere, andr J.", title = "Stimulation of Phosphofructokinase from Phycomyces blakesleeanus and Some Other Fungi by Micromolar Concentrations of Fructose 2,6-bisphosphate", journal= "Microbiology", year = "1983", volume = "129", number = "10", pages = "3281-3285", doi = "https://doi.org/10.1099/00221287-129-10-3281", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-129-10-3281", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "The phosphofructokinase in crude extracts of Phycomyces blakesleeanus required the presence of ammonium salts, AMP or fructose 2,6-bisphosphate for its activity. The enzyme had slightly sigmoidal kinetics with respect to fructose 6-phosphate as substrate. It was slightly inhibited by high ATP concentrations and by citrate. Fructose 2,6-bisphosphate stimulated the Phycomyces blakesleeanus phosphofructokinase; the K m for fructose 6-phosphate decreased, the inhibition by ATP was completely relieved and the affinity for the activator ammonia was increased. AMP also stimulated the catalytic activity but there was poor co-operation with fructose 2,6-bisphosphate. Preliminary experiments showed that fructose 2,6-bisphosphate also stimulated the phosphofructokinase from Mucor rouxii, Neurospora tetrasperma and Agaricus bisporus. ", }