Burenina E.A.
Journal of Evolutionary Biochemistry and Physiology 2010; 46(2): 153-162
There have been studied the activity and properties of fructose bisphosphatase (FBPase) of Bothriocephalus scorpii parasitizing in pyloric appendages of the goby Myoxocephalus brandti. All subcellular fractions of B. scorpii (12 g/cytosol, 105 g/cytosol, mitochondria, and microsomes) have the FBPase activity. The enzyme has a high affinity to substrate and needs the presence of bivalent cations (Mg2+ or Mn2+). AMP inhibits the enzyme significantly. Action of various effectors has been studied. The monovalent (Na+, K+, Li+, NH4+) and bivalent cations (Zn2+ and Cu2+) inhibit the enzyme activity.
